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{{Infobox_gene}}
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
'''Integrin beta-1''' also known as '''CD29''' is a [[protein]] that in humans is encoded by the ''ITGB1'' [[gene]].<ref name="pmid2524991">{{cite journal | vauthors = Goodfellow PJ, Nevanlinna HA, Gorman P, Sheer D, Lam G, Goodfellow PN | title = Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2 | journal = Annals of Human Genetics | volume = 53 | issue = Pt 1 | pages = 15–22 | date = Jan 1989 | pmid = 2524991 | pmc =  | doi = 10.1111/j.1469-1809.1989.tb01118.x }}</ref> CD29 is an [[integrin]] unit associated with very late antigen receptors. It is known to conjoin with [[CD49c|alpha-3 subunit]] to create α3β1 complex that reacts to such molecules as [[NTN1|netrin-1]] and [[reelin]]. In [[cardiac muscle]] and [[skeletal muscle]], the integrin beta-1D isoform is specifically expressed, and localizes to [[costamere]]s, where it aids in the lateral force transmission from the [[sarcomere|Z-discs]] to the [[extracellular matrix]]. Abnormal levels of integrin beta-1D have been found in [[limb girdle muscular dystrophy]] and [[polyneuropathy]].
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)
| HGNCid = 6153
| Symbol = ITGB1
| AltSymbols =; CD29; FNRB; GPIIA; MDF2; MSK12; VLAB
| OMIM = 135630
| ECnumber =
| Homologene = 22999
| MGIid = 96610
  | GeneAtlas_image1 = PBB_GE_ITGB1_211945_s_at.png
  <!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = 00:13, 15 September 2007 (UTC)
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0016477 |text = cell migration}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3688
    | Hs_Ensembl = ENSG00000150093
    | Hs_RefseqProtein = NP_002202
    | Hs_RefseqmRNA = NM_002211
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 33229326
    | Hs_GenLoc_end = 33287204
    | Hs_Uniprot = P05556
    | Mm_EntrezGene = 16412
    | Mm_Ensembl = ENSMUSG00000025809
    | Mm_RefseqmRNA = NM_010578
    | Mm_RefseqProtein = NP_034708
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 131591503
    | Mm_GenLoc_end = 131618179
    | Mm_Uniprot = Q3TIW5
  }}
}}


'''Integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)''', also known as '''ITGB1''' or '''CD29''', is a human [[gene]].  '''CD29''' is an [[integrin]] unit associated with very late antigen receptors.
== Structure ==


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Integrin beta-1 can exist as different [[isoform]]s via [[alternative splicing]]. Six [[alternative splicing|alternatively spliced]] variants have been found for this gene which encode five proteins with alternate [[C-terminus|C-termini]].<ref>{{cite web | title = Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3688| accessdate = }}</ref> Integrin receptors exist as heterodimers, and greater than 20 different integrin heterodimeric receptors have been described. All integrins, alpha and beta forms, have large extracellular and short intracellular domains.<ref name = "Hynes_1992">{{cite journal | vauthors = Hynes RO | title = Integrins: versatility, modulation, and signaling in cell adhesion | journal = Cell | volume = 69 | issue = 1 | pages = 11–25 | date = Apr 1992 | pmid = 1555235 | doi=10.1016/0092-8674(92)90115-s}}</ref> The cytoplasmic domain of integrin beta-1 binds to the [[actin]] [[cytoskeleton]].<ref name = "Sastry_1993">{{cite journal | vauthors = Sastry SK, Horwitz AF | title = Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling | journal = Current Opinion in Cell Biology | volume = 5 | issue = 5 | pages = 819–31 | date = Oct 1993 | pmid = 8240826 | doi=10.1016/0955-0674(93)90031-k}}</ref> Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.<ref name = "Hynes_1992"/>
{{PBB_Summary
| section_title =
| summary_text = Integrins are heterodimeric proteins made up of alpha and beta subunits. At least 18 alpha and 8 beta subunits have been described in mammals. Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metatastatic diffusion of tumor cells. The protein encoded by this gene is a beta subunit. Six alternatively spliced variants have been found for this gene which encode five proteins with alternate carboxy termini.<ref>{{cite web | title = Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3688| accessdate = }}</ref>
}}


==References==
== Function ==
{{reflist|2}}
 
==Further reading==
Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, [[hemostasis]], tissue repair, [[immune response]] and metastatic diffusion of tumor cells.<ref name = "Hynes_1992"/> Integrins link the [[actin]] [[cytoskeleton]] with the [[extracellular matrix]] and they transmit signals bidirectionally between the [[extracellular matrix]] and [[cytoplasm]]ic domains.<ref>{{cite journal | vauthors = Burridge K, Chrzanowska-Wodnicka M | title = Focal adhesions, contractility, and signaling | journal = Annual Review of Cell and Developmental Biology | volume = 12 | pages = 463–518 | date = 1996 | pmid = 8970735 | doi = 10.1146/annurev.cellbio.12.1.463 }}</ref><ref>{{cite journal | vauthors = Schwartz MA, Schaller MD, Ginsberg MH | title = Integrins: emerging paradigms of signal transduction | journal = Annual Review of Cell and Developmental Biology | volume = 11 | pages = 549–99 | date = 1995 | pmid = 8689569 | doi = 10.1146/annurev.cb.11.110195.003001 }}</ref>
{{refbegin | 2}}
Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainly [[focal adhesion]]s.<ref name = "Sastry_1993"/><ref>{{cite journal | vauthors = LaFlamme SE, Akiyama SK, Yamada KM | title = Regulation of fibronectin receptor distribution | journal = The Journal of Cell Biology | volume = 117 | issue = 2 | pages = 437–47 | date = Apr 1992 | pmid = 1373145 | doi=10.1083/jcb.117.2.437 | pmc=2289425}}</ref> Integrin beta-1 mutants lose the ability to target to sites of [[focal adhesion]]s.<ref>{{cite journal | vauthors = Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE | title = Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras | journal = The Journal of Biological Chemistry | volume = 269 | issue = 23 | pages = 15961–4 | date = Jun 1994 | pmid = 7515874 }}</ref><ref>{{cite journal | vauthors = Reszka AA, Hayashi Y, Horwitz AF | title = Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association | journal = The Journal of Cell Biology | volume = 117 | issue = 6 | pages = 1321–30 | date = Jun 1992 | pmid = 1376731 | doi=10.1083/jcb.117.6.1321 | pmc=2289496}}</ref>
{{PBB_Further_reading
 
| citations =  
Three novel isoforms of integrin beta-1 have been identified, termed beta-1B, beta-1C and beta-1D. Integrin beta-1B is transcribed when the proximal 26 [[amino acid]]s of the [[cytoplasm]]ic domain in exon 6 are retained and then succeeded by a 12 [[amino acid]] stretch from an adjacent [[intron]]ic region.<ref>{{cite journal | vauthors = Altruda F, Cervella P, Tarone G, Botta C, Balzac F, Stefanuto G, Silengo L | title = A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing | journal = Gene | volume = 95 | issue = 2 | pages = 261–6 | date = Nov 1990 | pmid = 2249781 | doi=10.1016/0378-1119(90)90369-3}}</ref> The integrin beta-1B [[isoform]] appears to act as a dominant negative in that it inhibits cell adhesion.<ref>{{cite journal | vauthors = Balzac F, Retta SF, Albini A, Melchiorri A, Koteliansky VE, Geuna M, Silengo L, Tarone G | title = Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility | journal = The Journal of Cell Biology | volume = 127 | issue = 2 | pages = 557–65 | date = Oct 1994 | pmid = 7523423 | doi=10.1083/jcb.127.2.557 | pmc=2120206}}</ref> A second integrin beta-1 [[isoform]], termed beta-1C, was described to have an additional 48 [[amino acid]]s appended to the 26 [[amino acid]]s in the [[cytoplasm]]ic domain;<ref>{{cite journal | vauthors = Languino LR, Ruoslahti E | title = An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain | journal = The Journal of Biological Chemistry | volume = 267 | issue = 10 | pages = 7116–20 | date = Apr 1992 | pmid = 1551917 }}</ref> the function of this isoform was an inhibitory one on [[DNA synthesis]] in the [[G1 phase]] of the [[cell cycle]].<ref>{{cite journal | vauthors = Meredith J, Takada Y, Fornaro M, Languino LR, Schwartz MA | title = Inhibition of cell cycle progression by the alternatively spliced integrin beta 1C | journal = Science | volume = 269 | issue = 5230 | pages = 1570–2 | date = Sep 1995 | pmid = 7545312 | doi=10.1126/science.7545312}}</ref>  The third [[isoform]], termed beta-1D, is a [[striated muscle]]-specific isoform, which replaces the canonical beta-1A [[isoform]] in [[cardiac muscle|cardiac]] and [[skeletal muscle]] cells. This [[isoform]] is produced from splicing into a novel additional exon between exons 6 and 7. The [[cytoplasm]]ic domain of integrin beta-1D replaces the distal 21 [[amino acid]]s (present in integrin beta-1A) with an alternative stretch of 24 [[amino acid]]s (13 unique).<ref>{{cite journal | vauthors = Zhidkova NI, Belkin AM, Mayne R | title = Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle | journal = Biochemical and Biophysical Research Communications | volume = 214 | issue = 1 | pages = 279–85 | date = Sep 1995 | pmid = 7545396 | doi = 10.1006/bbrc.1995.2285 }}</ref><ref name = "van_der_Flier_1995">{{cite journal | vauthors = van der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A | title = A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle | journal = FEBS Letters | volume = 369 | issue = 2–3 | pages = 340–4 | date = Aug 1995 | pmid = 7544298 | doi=10.1016/0014-5793(95)00814-p}}</ref>
*{{cite journal  | author=Evans JP |title=Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization. |journal=Bioessays |volume=23 |issue= 7 |pages= 628-39 |year= 2001 |pmid= 11462216 |doi= 10.1002/bies.1088 }}
 
*{{cite journal | author=Armulik A |title=Splice variants of human beta 1 integrins: origin, biosynthesis and functions. |journal=Front. Biosci. |volume=7 |issue=  |pages= d219-27 |year= 2002 |pmid= 11779688 |doi= }}
Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,<ref name = "van_der_Flier_1995"/> appearing immediately following the fusion of [[myoblast]]s in [[C2C12]] cell with rising levels throughout [[myofibril]]lar differentiation.<ref name = "Belkin_1996">{{cite journal | vauthors = Belkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K | title = Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells | journal = The Journal of Cell Biology | volume = 132 | issue = 1–2 | pages = 211–26 | date = Jan 1996 | pmid = 8567725 | doi=10.1083/jcb.132.1.211 | pmc=2120711}}</ref> Integrin beta-1D is specifically localized to [[costamere]]s and [[intercalated disc]]s of [[cardiac muscle]] and [[costamere]]s, myotendinous junctions and [[neuromuscular junction]]s of [[skeletal muscle]], and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface of [[Chinese hamster ovary cell|CHO cells]] resulted in [[tyrosine]] [[phosphorylation]] of [[PTK2|pp125FAK]] and induced [[mitogen-activated protein kinase]] activation.<ref name = "Belkin_1996"/>
*{{cite journal | author=Brakebusch C, Fässler R |title=beta 1 integrin function in vivo: adhesion, migration and more. |journal=Cancer Metastasis Rev. |volume=24 |issue= 3 |pages= 403-11 |year= 2006 |pmid= 16258728 |doi= 10.1007/s10555-005-5132-5 }}
 
}}
==Clinical significance==
In patients with [[limb girdle muscular dystrophy]], type 2C, beta-1D integrin has been shown to be severely reduced in [[skeletal muscle]] biopsies, coordinate with a reduction in [[ITGA7|alpha 7B-integrin]] and [[FLNC|filamin 2]].<ref>{{cite journal | vauthors = Anastasi G, Cutroneo G, Trimarchi F, Santoro G, Bruschetta D, Bramanti P, Pisani A, Favaloro A | title = Evaluation of sarcoglycans, vinculin-talin-integrin system and filamin2 in alpha- and gamma-sarcoglycanopathy: an immunohistochemical study | journal = International Journal of Molecular Medicine | volume = 14 | issue = 6 | pages = 989–99 | date = Dec 2004 | pmid = 15547664 }}</ref>
 
In patients with sensitive-motor [[polyneuropathy]], levels of [[ITGA7|integrin alpha-7B]], integrin beta-1D and [[agrin]] were significantly reduced nearly to undetectable levels; and this corresponded with lower [[mRNA]] levels.<ref>{{cite journal | vauthors = Anastasi G, Cutroneo G, Santoro G, Arco A, Rizzo G, Bramanti P, Rinaldi C, Sidoti A, Amato A, Favaloro A | title = Costameric proteins in human skeletal muscle during muscular inactivity | journal = Journal of Anatomy | volume = 213 | issue = 3 | pages = 284–95 | date = Sep 2008 | pmid = 18537849 | doi = 10.1111/j.1469-7580.2008.00921.x | pmc=2732038}}</ref>
 
== Interactions ==
 
CD29 has been shown to [[Protein-protein interaction|interact]] with
{{div col|colwidth=20em}}
* [[ACTN1]];<ref>{{cite journal | vauthors = Otey CA, Pavalko FM, Burridge K | title = An interaction between alpha-actinin and the beta 1 integrin subunit in vitro | journal = The Journal of Cell Biology | volume = 111 | issue = 2 | pages = 721–9 | date = Aug 1990 | pmid = 2116421 | doi=10.1083/jcb.111.2.721 | pmc=2116186}}</ref><ref>{{cite journal | vauthors = Otey CA, Vasquez GB, Burridge K, Erickson BW | title = Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain | journal = The Journal of Biological Chemistry | volume = 268 | issue = 28 | pages = 21193–7 | date = Oct 1993 | pmid = 7691808 }}</ref>
* [[CD46]],<ref name=pmid10741407>{{cite journal | vauthors = Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E | title = CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans | journal = European Journal of Immunology | volume = 30 | issue = 3 | pages = 900–7 | date = Mar 2000 | pmid = 10741407 | doi = 10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X }}</ref>
* [[CD9]],<ref name=pmid8630057>{{cite journal | vauthors = Radford KJ, Thorne RF, Hersey P | title = CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma | journal = Biochemical and Biophysical Research Communications | volume = 222 | issue = 1 | pages = 13–8 | date = May 1996 | pmid = 8630057 | doi = 10.1006/bbrc.1996.0690 }}</ref><ref name=pmid12175627>{{cite journal | vauthors = Mazzocca A, Carloni V, Sciammetta S, Cordella C, Pantaleo P, Caldini A, Gentilini P, Pinzani M | title = Expression of transmembrane 4 superfamily (TM4SF) proteins and their role in hepatic stellate cell motility and wound healing migration | journal = Journal of Hepatology | volume = 37 | issue = 3 | pages = 322–30 | date = Sep 2002 | pmid = 12175627 | doi = 10.1016/S0168-8278(02)00175-7 }}</ref>
* [[FHL2]],<ref name=pmid10906324>{{cite journal | vauthors = Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M | title = The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes | journal = The Journal of Biological Chemistry | volume = 275 | issue = 43 | pages = 33669–78 | date = Oct 2000 | pmid = 10906324 | doi = 10.1074/jbc.M002519200 }}</ref>
* [[Filamin]],<ref name= "pmid11807098">{{cite journal | vauthors = van der Flier A, Kuikman I, Kramer D, Geerts D, Kreft M, Takafuta T, Shapiro SS, Sonnenberg A | title = Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits | journal = The Journal of Cell Biology | volume = 156 | issue = 2 | pages = 361–76 | date = Jan 2002 | pmid = 11807098 | pmc = 2199218 | doi = 10.1083/jcb.200103037 }}</ref><ref name=pmid9722563>{{cite journal | vauthors = Loo DT, Kanner SB, Aruffo A | title = Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction | journal = The Journal of Biological Chemistry | volume = 273 | issue = 36 | pages = 23304–12 | date = Sep 1998 | pmid = 9722563 | doi = 10.1074/jbc.273.36.23304 }}</ref>
* [[FLNB]],<ref name = "pmid11807098"/>
* [[CD81]],<ref name=pmid12175627/><ref name=pmid10229664>{{cite journal | vauthors = Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E | title = Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions | journal = The Biochemical Journal | volume = 340 | issue = Pt 1 | pages = 103–11 | date = May 1999 | pmid = 10229664 | pmc = 1220227 | doi = 10.1042/0264-6021:3400103 }}</ref>
* [[GNB2L1]],<ref name=pmid12435334/><ref name=pmid9442085>{{cite journal | vauthors = Liliental J, Chang DD | title = Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit | journal = The Journal of Biological Chemistry | volume = 273 | issue = 4 | pages = 2379–83 | date = Jan 1998 | pmid = 9442085 | doi = 10.1074/jbc.273.4.2379 }}</ref>
* [[ITGB1BP1]],<ref name=pmid9281591>{{cite journal | vauthors = Chang DD, Wong C, Smith H, Liu J | title = ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin | journal = The Journal of Cell Biology | volume = 138 | issue = 5 | pages = 1149–57 | date = Sep 1997 | pmid = 9281591 | pmc = 2136751 | doi = 10.1083/jcb.138.5.1149 }}</ref><ref name=pmid11741908>{{cite journal | vauthors = Chang DD, Hoang BQ, Liu J, Springer TA | title = Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin | journal = The Journal of Biological Chemistry | volume = 277 | issue = 10 | pages = 8140–5 | date = Mar 2002 | pmid = 11741908 | doi = 10.1074/jbc.M109031200 }}</ref>
* [[LGALS8]],<ref name=pmid10852818>{{cite journal | vauthors = Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y | title = Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis | journal = Journal of Cell Science | volume = 113 | issue = 13| pages = 2385–97 | date = Jul 2000 | pmid = 10852818 }}</ref> 
* [[MAP4K4]],<ref name=pmid11967148>{{cite journal | vauthors = Poinat P, De Arcangelis A, Sookhareea S, Zhu X, Hedgecock EM, Labouesse M, Georges-Labouesse E | title = A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans | journal = Current Biology | volume = 12 | issue = 8 | pages = 622–31 | date = Apr 2002 | pmid = 11967148 | doi = 10.1016/S0960-9822(02)00764-9 }}</ref>
* [[NME1]],<ref name=pmid11919189>{{cite journal | vauthors = Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C | title = Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement | journal = The Journal of Biological Chemistry | volume = 277 | issue = 23 | pages = 20895–902 | date = Jun 2002 | pmid = 11919189 | doi = 10.1074/jbc.M200200200 }}</ref>
* [[PKC alpha]],<ref name=pmid12435334>{{cite journal | vauthors = Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM | title = Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction | journal = Osteoarthritis and Cartilage / OARS, Osteoarthritis Research Society | volume = 10 | issue = 11 | pages = 890–7 | date = Nov 2002 | pmid = 12435334 | doi = 10.1053/joca.2002.0842 }}</ref><ref name=pmid12138200>{{cite journal | vauthors = Parsons M, Keppler MD, Kline A, Messent A, Humphries MJ, Gilchrist R, Hart IR, Quittau-Prevostel C, Hughes WE, Parker PJ, Ng T | title = Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis | journal = Molecular and Cellular Biology | volume = 22 | issue = 16 | pages = 5897–911 | date = Aug 2002 | pmid = 12138200 | pmc = 133968 | doi = 10.1128/MCB.22.16.5897-5911.2002 }}</ref>
* [[TLN1]],<ref>{{cite journal | vauthors = Tapley P, Horwitz A, Buck C, Duggan K, Rohrschneider L | title = Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts | journal = Oncogene | volume = 4 | issue = 3 | pages = 325–33 | date = Mar 1989 | pmid = 2468126 }}</ref><ref>{{cite journal | vauthors = Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K | title = Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage | journal = Nature | volume = 320 | issue = 6062 | pages = 531–3 | date = 1986 | pmid = 2938015 | doi = 10.1038/320531a0 }}</ref>
* [[TSPAN4]],<ref name=pmid9360996>{{cite journal | vauthors = Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME | title = NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins | journal = The Journal of Biological Chemistry | volume = 272 | issue = 46 | pages = 29181–9 | date = Nov 1997 | pmid = 9360996 | doi = 10.1074/jbc.272.46.29181 }}</ref> and
* [[YWHAB]].<ref name=pmid11313964>{{cite journal | vauthors = Han DC, Rodriguez LG, Guan JL | title = Identification of a novel interaction between integrin beta1 and 14-3-3beta | journal = Oncogene | volume = 20 | issue = 3 | pages = 346–57 | date = Jan 2001 | pmid = 11313964 | doi = 10.1038/sj.onc.1204068 }}</ref>
{{Div col end}}
{{Clear}}
 
== References ==
{{reflist|33em}}
 
== Further reading ==
{{refbegin|33em}}
* {{cite journal | vauthors = Evans JP | title = Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization | journal = BioEssays | volume = 23 | issue = 7 | pages = 628–39 | date = Jul 2001 | pmid = 11462216 | doi = 10.1002/bies.1088 }}
* {{cite journal | vauthors = Armulik A | title = Splice variants of human beta 1 integrins: origin, biosynthesis and functions | journal = Frontiers in Bioscience | volume = 7 | issue =  | pages = d219-27 | date = Jan 2002 | pmid = 11779688 | doi = 10.2741/armulik }}
* {{cite journal | vauthors = Brakebusch C, Fässler R | title = beta 1 integrin function in vivo: adhesion, migration and more | journal = Cancer Metastasis Reviews | volume = 24 | issue = 3 | pages = 403–11 | date = Sep 2005 | pmid = 16258728 | doi = 10.1007/s10555-005-5132-5 }}
{{refend}}
{{refend}}


 
== External links ==
==External links==
* {{MeshName|CD29+Antigen}}
* {{MeshName|CD29+Antigen}}
* {{UCSC gene info|ITGB1}}


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Latest revision as of 09:22, 30 August 2017

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Integrin beta-1 also known as CD29 is a protein that in humans is encoded by the ITGB1 gene.[1] CD29 is an integrin unit associated with very late antigen receptors. It is known to conjoin with alpha-3 subunit to create α3β1 complex that reacts to such molecules as netrin-1 and reelin. In cardiac muscle and skeletal muscle, the integrin beta-1D isoform is specifically expressed, and localizes to costameres, where it aids in the lateral force transmission from the Z-discs to the extracellular matrix. Abnormal levels of integrin beta-1D have been found in limb girdle muscular dystrophy and polyneuropathy.

Structure

Integrin beta-1 can exist as different isoforms via alternative splicing. Six alternatively spliced variants have been found for this gene which encode five proteins with alternate C-termini.[2] Integrin receptors exist as heterodimers, and greater than 20 different integrin heterodimeric receptors have been described. All integrins, alpha and beta forms, have large extracellular and short intracellular domains.[3] The cytoplasmic domain of integrin beta-1 binds to the actin cytoskeleton.[4] Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.[3]

Function

Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, hemostasis, tissue repair, immune response and metastatic diffusion of tumor cells.[3] Integrins link the actin cytoskeleton with the extracellular matrix and they transmit signals bidirectionally between the extracellular matrix and cytoplasmic domains.[5][6] Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainly focal adhesions.[4][7] Integrin beta-1 mutants lose the ability to target to sites of focal adhesions.[8][9]

Three novel isoforms of integrin beta-1 have been identified, termed beta-1B, beta-1C and beta-1D. Integrin beta-1B is transcribed when the proximal 26 amino acids of the cytoplasmic domain in exon 6 are retained and then succeeded by a 12 amino acid stretch from an adjacent intronic region.[10] The integrin beta-1B isoform appears to act as a dominant negative in that it inhibits cell adhesion.[11] A second integrin beta-1 isoform, termed beta-1C, was described to have an additional 48 amino acids appended to the 26 amino acids in the cytoplasmic domain;[12] the function of this isoform was an inhibitory one on DNA synthesis in the G1 phase of the cell cycle.[13] The third isoform, termed beta-1D, is a striated muscle-specific isoform, which replaces the canonical beta-1A isoform in cardiac and skeletal muscle cells. This isoform is produced from splicing into a novel additional exon between exons 6 and 7. The cytoplasmic domain of integrin beta-1D replaces the distal 21 amino acids (present in integrin beta-1A) with an alternative stretch of 24 amino acids (13 unique).[14][15]

Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,[15] appearing immediately following the fusion of myoblasts in C2C12 cell with rising levels throughout myofibrillar differentiation.[16] Integrin beta-1D is specifically localized to costameres and intercalated discs of cardiac muscle and costameres, myotendinous junctions and neuromuscular junctions of skeletal muscle, and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface of CHO cells resulted in tyrosine phosphorylation of pp125FAK and induced mitogen-activated protein kinase activation.[16]

Clinical significance

In patients with limb girdle muscular dystrophy, type 2C, beta-1D integrin has been shown to be severely reduced in skeletal muscle biopsies, coordinate with a reduction in alpha 7B-integrin and filamin 2.[17]

In patients with sensitive-motor polyneuropathy, levels of integrin alpha-7B, integrin beta-1D and agrin were significantly reduced nearly to undetectable levels; and this corresponded with lower mRNA levels.[18]

Interactions

CD29 has been shown to interact with

References

  1. ↑ Goodfellow PJ, Nevanlinna HA, Gorman P, Sheer D, Lam G, Goodfellow PN (Jan 1989). "Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2". Annals of Human Genetics. 53 (Pt 1): 15–22. doi:10.1111/j.1469-1809.1989.tb01118.x. PMID 2524991.
  2. ↑ "Entrez Gene: ITGB1 integrin, beta 1 (fibronectin receptor, beta polypeptide, antigen CD29 includes MDF2, MSK12)".
  3. ↑ 3.0 3.1 3.2 Hynes RO (Apr 1992). "Integrins: versatility, modulation, and signaling in cell adhesion". Cell. 69 (1): 11–25. doi:10.1016/0092-8674(92)90115-s. PMID 1555235.
  4. ↑ 4.0 4.1 Sastry SK, Horwitz AF (Oct 1993). "Integrin cytoplasmic domains: mediators of cytoskeletal linkages and extra- and intracellular initiated transmembrane signaling". Current Opinion in Cell Biology. 5 (5): 819–31. doi:10.1016/0955-0674(93)90031-k. PMID 8240826.
  5. ↑ Burridge K, Chrzanowska-Wodnicka M (1996). "Focal adhesions, contractility, and signaling". Annual Review of Cell and Developmental Biology. 12: 463–518. doi:10.1146/annurev.cellbio.12.1.463. PMID 8970735.
  6. ↑ Schwartz MA, Schaller MD, Ginsberg MH (1995). "Integrins: emerging paradigms of signal transduction". Annual Review of Cell and Developmental Biology. 11: 549–99. doi:10.1146/annurev.cb.11.110195.003001. PMID 8689569.
  7. ↑ LaFlamme SE, Akiyama SK, Yamada KM (Apr 1992). "Regulation of fibronectin receptor distribution". The Journal of Cell Biology. 117 (2): 437–47. doi:10.1083/jcb.117.2.437. PMC 2289425. PMID 1373145.
  8. ↑ Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE (Jun 1994). "Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras". The Journal of Biological Chemistry. 269 (23): 15961–4. PMID 7515874.
  9. ↑ Reszka AA, Hayashi Y, Horwitz AF (Jun 1992). "Identification of amino acid sequences in the integrin beta 1 cytoplasmic domain implicated in cytoskeletal association". The Journal of Cell Biology. 117 (6): 1321–30. doi:10.1083/jcb.117.6.1321. PMC 2289496. PMID 1376731.
  10. ↑ Altruda F, Cervella P, Tarone G, Botta C, Balzac F, Stefanuto G, Silengo L (Nov 1990). "A human integrin beta 1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing". Gene. 95 (2): 261–6. doi:10.1016/0378-1119(90)90369-3. PMID 2249781.
  11. ↑ Balzac F, Retta SF, Albini A, Melchiorri A, Koteliansky VE, Geuna M, Silengo L, Tarone G (Oct 1994). "Expression of beta 1B integrin isoform in CHO cells results in a dominant negative effect on cell adhesion and motility". The Journal of Cell Biology. 127 (2): 557–65. doi:10.1083/jcb.127.2.557. PMC 2120206. PMID 7523423.
  12. ↑ Languino LR, Ruoslahti E (Apr 1992). "An alternative form of the integrin beta 1 subunit with a variant cytoplasmic domain". The Journal of Biological Chemistry. 267 (10): 7116–20. PMID 1551917.
  13. ↑ Meredith J, Takada Y, Fornaro M, Languino LR, Schwartz MA (Sep 1995). "Inhibition of cell cycle progression by the alternatively spliced integrin beta 1C". Science. 269 (5230): 1570–2. doi:10.1126/science.7545312. PMID 7545312.
  14. ↑ Zhidkova NI, Belkin AM, Mayne R (Sep 1995). "Novel isoform of beta 1 integrin expressed in skeletal and cardiac muscle". Biochemical and Biophysical Research Communications. 214 (1): 279–85. doi:10.1006/bbrc.1995.2285. PMID 7545396.
  15. ↑ 15.0 15.1 van der Flier A, Kuikman I, Baudoin C, van der Neut R, Sonnenberg A (Aug 1995). "A novel beta 1 integrin isoform produced by alternative splicing: unique expression in cardiac and skeletal muscle". FEBS Letters. 369 (2–3): 340–4. doi:10.1016/0014-5793(95)00814-p. PMID 7544298.
  16. ↑ 16.0 16.1 Belkin AM, Zhidkova NI, Balzac F, Altruda F, Tomatis D, Maier A, Tarone G, Koteliansky VE, Burridge K (Jan 1996). "Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells". The Journal of Cell Biology. 132 (1–2): 211–26. doi:10.1083/jcb.132.1.211. PMC 2120711. PMID 8567725.
  17. ↑ Anastasi G, Cutroneo G, Trimarchi F, Santoro G, Bruschetta D, Bramanti P, Pisani A, Favaloro A (Dec 2004). "Evaluation of sarcoglycans, vinculin-talin-integrin system and filamin2 in alpha- and gamma-sarcoglycanopathy: an immunohistochemical study". International Journal of Molecular Medicine. 14 (6): 989–99. PMID 15547664.
  18. ↑ Anastasi G, Cutroneo G, Santoro G, Arco A, Rizzo G, Bramanti P, Rinaldi C, Sidoti A, Amato A, Favaloro A (Sep 2008). "Costameric proteins in human skeletal muscle during muscular inactivity". Journal of Anatomy. 213 (3): 284–95. doi:10.1111/j.1469-7580.2008.00921.x. PMC 2732038. PMID 18537849.
  19. ↑ Otey CA, Pavalko FM, Burridge K (Aug 1990). "An interaction between alpha-actinin and the beta 1 integrin subunit in vitro". The Journal of Cell Biology. 111 (2): 721–9. doi:10.1083/jcb.111.2.721. PMC 2116186. PMID 2116421.
  20. ↑ Otey CA, Vasquez GB, Burridge K, Erickson BW (Oct 1993). "Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain". The Journal of Biological Chemistry. 268 (28): 21193–7. PMID 7691808.
  21. ↑ Lozahic S, Christiansen D, Manié S, Gerlier D, Billard M, Boucheix C, Rubinstein E (Mar 2000). "CD46 (membrane cofactor protein) associates with multiple beta1 integrins and tetraspans". European Journal of Immunology. 30 (3): 900–7. doi:10.1002/1521-4141(200003)30:3<900::AID-IMMU900>3.0.CO;2-X. PMID 10741407.
  22. ↑ Radford KJ, Thorne RF, Hersey P (May 1996). "CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma". Biochemical and Biophysical Research Communications. 222 (1): 13–8. doi:10.1006/bbrc.1996.0690. PMID 8630057.
  23. ↑ 23.0 23.1 Mazzocca A, Carloni V, Sciammetta S, Cordella C, Pantaleo P, Caldini A, Gentilini P, Pinzani M (Sep 2002). "Expression of transmembrane 4 superfamily (TM4SF) proteins and their role in hepatic stellate cell motility and wound healing migration". Journal of Hepatology. 37 (3): 322–30. doi:10.1016/S0168-8278(02)00175-7. PMID 12175627.
  24. ↑ Wixler V, Geerts D, Laplantine E, Westhoff D, Smyth N, Aumailley M, Sonnenberg A, Paulsson M (Oct 2000). "The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes". The Journal of Biological Chemistry. 275 (43): 33669–78. doi:10.1074/jbc.M002519200. PMID 10906324.
  25. ↑ 25.0 25.1 van der Flier A, Kuikman I, Kramer D, Geerts D, Kreft M, Takafuta T, Shapiro SS, Sonnenberg A (Jan 2002). "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin [beta] subunits". The Journal of Cell Biology. 156 (2): 361–76. doi:10.1083/jcb.200103037. PMC 2199218. PMID 11807098.
  26. ↑ Loo DT, Kanner SB, Aruffo A (Sep 1998). "Filamin binds to the cytoplasmic domain of the beta1-integrin. Identification of amino acids responsible for this interaction". The Journal of Biological Chemistry. 273 (36): 23304–12. doi:10.1074/jbc.273.36.23304. PMID 9722563.
  27. ↑ Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E (May 1999). "Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions". The Biochemical Journal. 340 (Pt 1): 103–11. doi:10.1042/0264-6021:3400103. PMC 1220227. PMID 10229664.
  28. ↑ 28.0 28.1 Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM (Nov 2002). "Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction". Osteoarthritis and Cartilage / OARS, Osteoarthritis Research Society. 10 (11): 890–7. doi:10.1053/joca.2002.0842. PMID 12435334.
  29. ↑ Liliental J, Chang DD (Jan 1998). "Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit". The Journal of Biological Chemistry. 273 (4): 2379–83. doi:10.1074/jbc.273.4.2379. PMID 9442085.
  30. ↑ Chang DD, Wong C, Smith H, Liu J (Sep 1997). "ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin". The Journal of Cell Biology. 138 (5): 1149–57. doi:10.1083/jcb.138.5.1149. PMC 2136751. PMID 9281591.
  31. ↑ Chang DD, Hoang BQ, Liu J, Springer TA (Mar 2002). "Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin". The Journal of Biological Chemistry. 277 (10): 8140–5. doi:10.1074/jbc.M109031200. PMID 11741908.
  32. ↑ Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (Jul 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". Journal of Cell Science. 113 (13): 2385–97. PMID 10852818.
  33. ↑ Poinat P, De Arcangelis A, Sookhareea S, Zhu X, Hedgecock EM, Labouesse M, Georges-Labouesse E (Apr 2002). "A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans". Current Biology. 12 (8): 622–31. doi:10.1016/S0960-9822(02)00764-9. PMID 11967148.
  34. ↑ Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C (Jun 2002). "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement". The Journal of Biological Chemistry. 277 (23): 20895–902. doi:10.1074/jbc.M200200200. PMID 11919189.
  35. ↑ Parsons M, Keppler MD, Kline A, Messent A, Humphries MJ, Gilchrist R, Hart IR, Quittau-Prevostel C, Hughes WE, Parker PJ, Ng T (Aug 2002). "Site-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis". Molecular and Cellular Biology. 22 (16): 5897–911. doi:10.1128/MCB.22.16.5897-5911.2002. PMC 133968. PMID 12138200.
  36. ↑ Tapley P, Horwitz A, Buck C, Duggan K, Rohrschneider L (Mar 1989). "Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts". Oncogene. 4 (3): 325–33. PMID 2468126.
  37. ↑ Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K (1986). "Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage". Nature. 320 (6062): 531–3. doi:10.1038/320531a0. PMID 2938015.
  38. ↑ Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (Nov 1997). "NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins". The Journal of Biological Chemistry. 272 (46): 29181–9. doi:10.1074/jbc.272.46.29181. PMID 9360996.
  39. ↑ Han DC, Rodriguez LG, Guan JL (Jan 2001). "Identification of a novel interaction between integrin beta1 and 14-3-3beta". Oncogene. 20 (3): 346–57. doi:10.1038/sj.onc.1204068. PMID 11313964.

Further reading

  • Evans JP (Jul 2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization". BioEssays. 23 (7): 628–39. doi:10.1002/bies.1088. PMID 11462216.
  • Armulik A (Jan 2002). "Splice variants of human beta 1 integrins: origin, biosynthesis and functions". Frontiers in Bioscience. 7: d219–27. doi:10.2741/armulik. PMID 11779688.
  • Brakebusch C, Fässler R (Sep 2005). "beta 1 integrin function in vivo: adhesion, migration and more". Cancer Metastasis Reviews. 24 (3): 403–11. doi:10.1007/s10555-005-5132-5. PMID 16258728.

External links

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