Actinin alpha 4: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Alpha-actinin-4''' is a [[protein]] that in humans is encoded by the ''ACTN4'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTN4 actinin, alpha 4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ACTN4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wlx.
| PDB = {{PDB2|1wlx}}, {{PDB2|2eyi}}, {{PDB2|2eyn}}
| Name = Actinin, alpha 4
| HGNCid = 166
| Symbol = ACTN4
| AltSymbols =; DKFZp686K23158; FSGS; FSGS1
| OMIM = 604638
| ECnumber = 
| Homologene = 55857
| MGIid = 1890773
| GeneAtlas_image1 = PBB_GE_ACTN4_200601_at_tn.png
| Function = {{GNF_GO|id=GO:0001882 |text = nucleoside binding}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0001725 |text = stress fiber}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030863 |text = cortical cytoskeleton}} {{GNF_GO|id=GO:0031143 |text = pseudopodium}} {{GNF_GO|id=GO:0043234 |text = protein complex}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0032417 |text = positive regulation of sodium:hydrogen antiporter activity}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0048549 |text = positive regulation of pinocytosis}} {{GNF_GO|id=GO:0051017 |text = actin filament bundle formation}} {{GNF_GO|id=GO:0051271 |text = negative regulation of cell motility}} {{GNF_GO|id=GO:0051272 |text = positive regulation of cell motility}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 81
    | Hs_Ensembl = ENSG00000130402
    | Hs_RefseqProtein = NP_004915
    | Hs_RefseqmRNA = NM_004924
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 43830167
    | Hs_GenLoc_end = 43913010
    | Hs_Uniprot = O43707
    | Mm_EntrezGene = 60595
    | Mm_Ensembl = ENSMUSG00000054808
    | Mm_RefseqmRNA = NM_021895
    | Mm_RefseqProtein = NP_068695
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 7
    | Mm_GenLoc_start = 28602011
    | Mm_GenLoc_end = 28671040
    | Mm_Uniprot = Q1A602
  }}
}}
'''Actinin, alpha 4''', also known as '''ACTN4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ACTN4 actinin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins.  Alpha actinin is an actin-binding protein with multiple roles in different cell types.  In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane.  In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.  This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes.  Mutations in this gene have been associated with focal and segmental glomerulosclerosis.<ref name="entrez">{{cite web | title = Entrez Gene: ACTN4 actinin, alpha 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=81| accessdate = }}</ref>
| summary_text = Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins.  Alpha actinin is an actin-binding protein with multiple roles in different cell types.  In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane.  In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.  This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes.  Mutations in this gene have been associated with focal and segmental glomerulosclerosis.<ref name="entrez" />
}}
}}
==Interactions==
Actinin alpha 4 has been shown to [[Protein-protein interaction|interact]] with [[PDLIM1]],<ref name=pmid16189514>{{cite journal |last=Rual |first=Jean-François |author2=Venkatesan Kavitha |author3=Hao Tong |author4=Hirozane-Kishikawa Tomoko |author5=Dricot Amélie |author6=Li Ning |author7=Berriz Gabriel F |author8=Gibbons Francis D |author9=Dreze Matija |author10=Ayivi-Guedehoussou Nono |author11=Klitgord Niels |author12=Simon Christophe |author13=Boxem Mike |author14=Milstein Stuart |author15=Rosenberg Jennifer |author16=Goldberg Debra S |author17=Zhang Lan V |author18=Wong Sharyl L |author19=Franklin Giovanni |author20=Li Siming |author21=Albala Joanna S |author22=Lim Janghoo |author23=Fraughton Carlene |author24=Llamosas Estelle |author25=Cevik Sebiha |author26=Bex Camille |author27=Lamesch Philippe |author28=Sikorski Robert S |author29=Vandenhaute Jean |author30=Zoghbi Huda Y |author31=Smolyar Alex |author32=Bosak Stephanie |author33=Sequerra Reynaldo |author34=Doucette-Stamm Lynn |author35=Cusick Michael E |author36=Hill David E |author37=Roth Frederick P |author38=Vidal Marc |date=Oct 2005 |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=[[Nature (journal)|Nature]] |volume=437 |issue=7062 |pages=1173–8 |publisher= |location = England| issn = | pmid = 16189514 |doi = 10.1038/nature04209 | bibcode =2005Natur.437.1173R | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref><ref name=pmid10753915>{{cite journal |doi=10.1074/jbc.275.15.11100 |last=Vallenius |first=T |author2=Luukko K|author3=Mäkelä T P |date=Apr 2000 |title=CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4 |journal=J. Biol. Chem. |volume=275 |issue=15 |pages=11100–5 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 10753915 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Sodium-hydrogen exchange regulatory cofactor 2]],<ref name=pmid11948184>{{cite journal |last=Kim |first=Jae Ho |author2=Lee-Kwon Whaseon |author3=Park Jong Bae |author4=Ryu Sung Ho|author5=Yun C H Chris |author6=Donowitz Mark |date=Jun 2002 |title=Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis |journal=J. Biol. Chem. |volume=277 |issue=26 |pages=23714–24 |publisher= |location = United States| issn = 0021-9258| pmid = 11948184 |doi = 10.1074/jbc.M200835200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[Collagen, type XVII, alpha 1]],<ref name=pmid11739652>{{cite journal |last=Gonzalez |first=A M |author2=Otey C|author3=Edlund M|author4=Jones J C |date=Dec 2001 |title=Interactions of a hemidesmosome component and actinin family members |journal=J. Cell Sci. |volume=114 |issue=Pt 23 |pages=4197–206 |publisher= |location = England| issn = 0021-9533| pmid = 11739652 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[CAMK2A]],<ref name=pmid11160423>{{cite journal |last=Walikonis |first=R S |author2=Oguni A |author3=Khorosheva E M |author4=Jeng C J |author5=Asuncion F J |author6=Kennedy M B  |date=Jan 2001 |title=Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin |journal=J. Neurosci. |volume=21 |issue=2 |pages=423–33 |publisher= |location = United States| issn = | pmid = 11160423 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[CAMK2B]],<ref name=pmid11160423/> [[MAGI1]]<ref name=pmid12042308>{{cite journal |last=Patrie |first=Kevin M |author2=Drescher Andrew J|author3=Welihinda Ajith|author4=Mundel Peter|author5= Margolis Ben |date=Aug 2002 |title=Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1 |journal=J. Biol. Chem. |volume=277 |issue=33 |pages=30183–90 |publisher= |location = United States| issn = 0021-9258| pmid = 12042308 |doi = 10.1074/jbc.M203072200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and [[TRIM3]].<ref name=pmid10673389>{{cite journal |last=El-Husseini |first=A E |author2=Kwasnicka D |author3=Yamada T |author4=Hirohashi S |author5=Vincent S R  |date=Jan 2000 |title=BERP, a novel ring finger protein, binds to alpha-actinin-4 |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue=3 |pages=906–11 |publisher= |location = UNITED STATES| issn = 0006-291X| pmid = 10673389 |doi = 10.1006/bbrc.1999.2045 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>
==See also==
* [[Focal segmental glomerulosclerosis]]


==References==
==References==
{{reflist|2}}
{{Reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi=  }}
*{{cite journal  |vauthors=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317–20 |year= 1992 |pmid= 1602151 |doi=10.1016/S0163-4453(05)80037-4 }}
*{{cite journal  | author=Yürüker B, Niggli V |title=Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. |journal=J. Cell. Sci. |volume=101 ( Pt 2) |issue=  |pages= 403-14 |year= 1992 |pmid= 1629252 |doi=  }}
*{{cite journal  |vauthors=Yürüker B, Niggli V |title=Alpha-actinin and vinculin in human neutrophils: reorganization during adhesion and relation to the actin network. | series=101 |journal=J. Cell Sci. |volume=( Pt 2) |issue=  |pages= 403–14 |year= 1992 |pmid= 1629252 |doi=  }}
*{{cite journal  | author=Otey CA, Pavalko FM, Burridge K |title=An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. |journal=J. Cell Biol. |volume=111 |issue= 2 |pages= 721-9 |year= 1990 |pmid= 2116421 |doi= }}
*{{cite journal  |vauthors=Otey CA, Pavalko FM, Burridge K |title=An interaction between alpha-actinin and the beta 1 integrin subunit in vitro. |journal=J. Cell Biol. |volume=111 |issue= 2 |pages= 721–9 |year= 1990 |pmid= 2116421 |doi=10.1083/jcb.111.2.721  | pmc=2116186  }}
*{{cite journal  | author=Pavalko FM, LaRoche SM |title=Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. |journal=J. Immunol. |volume=151 |issue= 7 |pages= 3795-807 |year= 1993 |pmid= 8104223 |doi=  }}
*{{cite journal  |vauthors=Pavalko FM, LaRoche SM |title=Activation of human neutrophils induces an interaction between the integrin beta 2-subunit (CD18) and the actin binding protein alpha-actinin. |journal=J. Immunol. |volume=151 |issue= 7 |pages= 3795–807 |year= 1993 |pmid= 8104223 |doi=  }}
*{{cite journal  | author=Mathis BJ, Kim SH, Calabrese K, ''et al.'' |title=A locus for inherited focal segmental glomerulosclerosis maps to chromosome 19q13. |journal=Kidney Int. |volume=53 |issue= 2 |pages= 282-6 |year= 1998 |pmid= 9461087 |doi= 10.1046/j.1523-1755.1998.00828.x }}
*{{cite journal  |vauthors=Mathis BJ, Kim SH, Calabrese K |title=A locus for inherited focal segmental glomerulosclerosis maps to chromosome 19q13. |journal=Kidney Int. |volume=53 |issue= 2 |pages= 282–6 |year= 1998 |pmid= 9461087 |doi= 10.1046/j.1523-1755.1998.00828.x |display-authors=etal}}
*{{cite journal  | author=Honda K, Yamada T, Endo R, ''et al.'' |title=Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion. |journal=J. Cell Biol. |volume=140 |issue= 6 |pages= 1383-93 |year= 1998 |pmid= 9508771 |doi=  }}
*{{cite journal  |vauthors=Honda K, Yamada T, Endo R |title=Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion. |journal=J. Cell Biol. |volume=140 |issue= 6 |pages= 1383–93 |year= 1998 |pmid= 9508771 |doi=10.1083/jcb.140.6.1383 | pmc=2132673  |display-authors=etal}}
*{{cite journal  | author=Zhang H, Wang L, Kao S, ''et al.'' |title=Functional interaction between the cytoplasmic leucine-zipper domain of HIV-1 gp41 and p115-RhoGEF. |journal=Curr. Biol. |volume=9 |issue= 21 |pages= 1271-4 |year= 1999 |pmid= 10556093 |doi= }}
*{{cite journal  |vauthors=Zhang H, Wang L, Kao S |title=Functional interaction between the cytoplasmic leucine-zipper domain of HIV-1 gp41 and p115-RhoGEF. |journal=Curr. Biol. |volume=9 |issue= 21 |pages= 1271–4 |year= 1999 |pmid= 10556093 |doi=10.1016/S0960-9822(99)80511-9  |display-authors=etal}}
*{{cite journal  | author=Nikolopoulos SN, Spengler BA, Kisselbach K, ''et al.'' |title=The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells. |journal=Oncogene |volume=19 |issue= 3 |pages= 380-6 |year= 2000 |pmid= 10656685 |doi= 10.1038/sj.onc.1203310 }}
*{{cite journal  |vauthors=Nikolopoulos SN, Spengler BA, Kisselbach K |title=The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells. |journal=Oncogene |volume=19 |issue= 3 |pages= 380–6 |year= 2000 |pmid= 10656685 |doi= 10.1038/sj.onc.1203310 |display-authors=etal}}
*{{cite journal  | author=El-Husseini AE, Kwasnicka D, Yamada T, ''et al.'' |title=BERP, a novel ring finger protein, binds to alpha-actinin-4. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 3 |pages= 906-11 |year= 2000 |pmid= 10673389 |doi= 10.1006/bbrc.1999.2045 }}
*{{cite journal  |vauthors=El-Husseini AE, Kwasnicka D, Yamada T |title=BERP, a novel ring finger protein, binds to alpha-actinin-4. |journal=Biochem. Biophys. Res. Commun. |volume=267 |issue= 3 |pages= 906–11 |year= 2000 |pmid= 10673389 |doi= 10.1006/bbrc.1999.2045 |display-authors=etal}}
*{{cite journal  | author=Kaplan JM, Kim SH, North KN, ''et al.'' |title=Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. |journal=Nat. Genet. |volume=24 |issue= 3 |pages= 251-6 |year= 2000 |pmid= 10700177 |doi= 10.1038/73456 }}
*{{cite journal  |vauthors=Kaplan JM, Kim SH, North KN |title=Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. |journal=Nat. Genet. |volume=24 |issue= 3 |pages= 251–6 |year= 2000 |pmid= 10700177 |doi= 10.1038/73456 |display-authors=etal}}
*{{cite journal  | author=Vallenius T, Luukko K, Mäkelä TP |title=CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11100-5 |year= 2000 |pmid= 10753915 |doi=  }}
*{{cite journal  |vauthors=Vallenius T, Luukko K, Mäkelä TP |title=CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11100–5 |year= 2000 |pmid= 10753915 |doi=10.1074/jbc.275.15.11100 }}
*{{cite journal  | author=Holliday LS, Lu M, Lee BS, ''et al.'' |title=The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 32331-7 |year= 2000 |pmid= 10915794 |doi= 10.1074/jbc.M004795200 }}
*{{cite journal  |vauthors=Holliday LS, Lu M, Lee BS |title=The amino-terminal domain of the B subunit of vacuolar H+-ATPase contains a filamentous actin binding site. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 32331–7 |year= 2000 |pmid= 10915794 |doi= 10.1074/jbc.M004795200 |display-authors=etal}}
*{{cite journal  | author=Walikonis RS, Oguni A, Khorosheva EM, ''et al.'' |title=Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. |journal=J. Neurosci. |volume=21 |issue= 2 |pages= 423-33 |year= 2001 |pmid= 11160423 |doi=  }}
*{{cite journal  |vauthors=Walikonis RS, Oguni A, Khorosheva EM |title=Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin. |journal=J. Neurosci. |volume=21 |issue= 2 |pages= 423–33 |year= 2001 |pmid= 11160423 |doi=  |display-authors=etal}}
*{{cite journal  | author=Echchakir H, Mami-Chouaib F, Vergnon I, ''et al.'' |title=A point mutation in the alpha-actinin-4 gene generates an antigenic peptide recognized by autologous cytolytic T lymphocytes on a human lung carcinoma. |journal=Cancer Res. |volume=61 |issue= 10 |pages= 4078-83 |year= 2001 |pmid= 11358829 |doi=  }}
*{{cite journal  |vauthors=Echchakir H, Mami-Chouaib F, Vergnon I |title=A point mutation in the alpha-actinin-4 gene generates an antigenic peptide recognized by autologous cytolytic T lymphocytes on a human lung carcinoma. |journal=Cancer Res. |volume=61 |issue= 10 |pages= 4078–83 |year= 2001 |pmid= 11358829 |doi=  |display-authors=etal}}
*{{cite journal  | author=Xu F, Zhao R, Peng Y, ''et al.'' |title=Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29479-84 |year= 2001 |pmid= 11382784 |doi= 10.1074/jbc.M104428200 }}
*{{cite journal  |vauthors=Xu F, Zhao R, Peng Y |title=Association of tyrosine phosphatase SHP-2 with F-actin at low cell densities. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29479–84 |year= 2001 |pmid= 11382784 |doi= 10.1074/jbc.M104428200 |display-authors=etal}}
*{{cite journal  | author=Hüttelmaier S, Illenberger S, Grosheva I, ''et al.'' |title=Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins. |journal=J. Cell Biol. |volume=155 |issue= 5 |pages= 775-86 |year= 2002 |pmid= 11724819 |doi= 10.1083/jcb.200105044 }}
*{{cite journal  |vauthors=Hüttelmaier S, Illenberger S, Grosheva I |title=Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and microfilament attachment proteins. |journal=J. Cell Biol. |volume=155 |issue= 5 |pages= 775–86 |year= 2002 |pmid= 11724819 |doi= 10.1083/jcb.200105044 | pmc=2150882 |display-authors=etal}}
*{{cite journal  | author=Renoult C, Blondin L, Fattoum A, ''et al.'' |title=Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin. |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6165-75 |year= 2002 |pmid= 11733011 |doi=  }}
*{{cite journal  |vauthors=Renoult C, Blondin L, Fattoum A |title=Binding of gelsolin domain 2 to actin. An actin interface distinct from that of gelsolin domain 1 and from ADF/cofilin. |journal=Eur. J. Biochem. |volume=268 |issue= 23 |pages= 6165–75 |year= 2002 |pmid= 11733011 |doi=10.1046/j.0014-2956.2001.02574.x |display-authors=etal}}
*{{cite journal  | author=Gonzalez AM, Otey C, Edlund M, Jones JC |title=Interactions of a hemidesmosome component and actinin family members. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4197-206 |year= 2002 |pmid= 11739652 |doi=  }}
*{{cite journal  |vauthors=Gonzalez AM, Otey C, Edlund M, Jones JC |title=Interactions of a hemidesmosome component and actinin family members. |journal=J. Cell Sci. |volume=114 |issue= Pt 23 |pages= 4197–206 |year= 2002 |pmid= 11739652 |doi=  }}
*{{cite journal  | author=Lukoyanova N, VanLoock MS, Orlova A, ''et al.'' |title=Each actin subunit has three nebulin binding sites: implications for steric blocking. |journal=Curr. Biol. |volume=12 |issue= 5 |pages= 383-8 |year= 2002 |pmid= 11882289 |doi=  }}
*{{cite journal  |vauthors=Lukoyanova N, VanLoock MS, Orlova A |title=Each actin subunit has three nebulin binding sites: implications for steric blocking. |journal=Curr. Biol. |volume=12 |issue= 5 |pages= 383–8 |year= 2002 |pmid= 11882289 |doi=10.1016/S0960-9822(02)00678-4 |display-authors=etal}}
*{{cite journal  | author=Kim JH, Lee-Kwon W, Park JB, ''et al.'' |title=Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23714-24 |year= 2002 |pmid= 11948184 |doi= 10.1074/jbc.M200835200 }}
*{{cite journal  |vauthors=Kim JH, Lee-Kwon W, Park JB |title=Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis. |journal=J. Biol. Chem. |volume=277 |issue= 26 |pages= 23714–24 |year= 2002 |pmid= 11948184 |doi= 10.1074/jbc.M200835200 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=81}}
==External links==
* {{UCSC gene info|ACTN4}}
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{{Cytoskeletal Proteins}}


{{protein-stub}}
[[Category:EF-hand-containing proteins]]
[[Category:Human proteins]]

Latest revision as of 17:08, 22 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Alpha-actinin-4 is a protein that in humans is encoded by the ACTN4 gene.[1]

Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments. This gene encodes a nonmuscle, alpha actinin isoform which is concentrated in the cytoplasm, and thought to be involved in metastatic processes. Mutations in this gene have been associated with focal and segmental glomerulosclerosis.[1]

Interactions

Actinin alpha 4 has been shown to interact with PDLIM1,[2][3] Sodium-hydrogen exchange regulatory cofactor 2,[4] Collagen, type XVII, alpha 1,[5] CAMK2A,[6] CAMK2B,[6] MAGI1[7] and TRIM3.[8]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: ACTN4 actinin, alpha 4".
  2. ↑ Rual, Jean-François; Venkatesan Kavitha; Hao Tong; Hirozane-Kishikawa Tomoko; Dricot Amélie; Li Ning; Berriz Gabriel F; Gibbons Francis D; Dreze Matija; Ayivi-Guedehoussou Nono; Klitgord Niels; Simon Christophe; Boxem Mike; Milstein Stuart; Rosenberg Jennifer; Goldberg Debra S; Zhang Lan V; Wong Sharyl L; Franklin Giovanni; Li Siming; Albala Joanna S; Lim Janghoo; Fraughton Carlene; Llamosas Estelle; Cevik Sebiha; Bex Camille; Lamesch Philippe; Sikorski Robert S; Vandenhaute Jean; Zoghbi Huda Y; Smolyar Alex; Bosak Stephanie; Sequerra Reynaldo; Doucette-Stamm Lynn; Cusick Michael E; Hill David E; Roth Frederick P; Vidal Marc (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. England. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
  3. ↑ Vallenius, T; Luukko K; Mäkelä T P (Apr 2000). "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4". J. Biol. Chem. UNITED STATES. 275 (15): 11100–5. doi:10.1074/jbc.275.15.11100. ISSN 0021-9258. PMID 10753915.
  4. ↑ Kim, Jae Ho; Lee-Kwon Whaseon; Park Jong Bae; Ryu Sung Ho; Yun C H Chris; Donowitz Mark (Jun 2002). "Ca(2+)-dependent inhibition of Na+/H+ exchanger 3 (NHE3) requires an NHE3-E3KARP-alpha-actinin-4 complex for oligomerization and endocytosis". J. Biol. Chem. United States. 277 (26): 23714–24. doi:10.1074/jbc.M200835200. ISSN 0021-9258. PMID 11948184.
  5. ↑ Gonzalez, A M; Otey C; Edlund M; Jones J C (Dec 2001). "Interactions of a hemidesmosome component and actinin family members". J. Cell Sci. England. 114 (Pt 23): 4197–206. ISSN 0021-9533. PMID 11739652.
  6. ↑ 6.0 6.1 Walikonis, R S; Oguni A; Khorosheva E M; Jeng C J; Asuncion F J; Kennedy M B (Jan 2001). "Densin-180 forms a ternary complex with the (alpha)-subunit of Ca2+/calmodulin-dependent protein kinase II and (alpha)-actinin". J. Neurosci. United States. 21 (2): 423–33. PMID 11160423.
  7. ↑ Patrie, Kevin M; Drescher Andrew J; Welihinda Ajith; Mundel Peter; Margolis Ben (Aug 2002). "Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1". J. Biol. Chem. United States. 277 (33): 30183–90. doi:10.1074/jbc.M203072200. ISSN 0021-9258. PMID 12042308.
  8. ↑ El-Husseini, A E; Kwasnicka D; Yamada T; Hirohashi S; Vincent S R (Jan 2000). "BERP, a novel ring finger protein, binds to alpha-actinin-4". Biochem. Biophys. Res. Commun. UNITED STATES. 267 (3): 906–11. doi:10.1006/bbrc.1999.2045. ISSN 0006-291X. PMID 10673389.

Further reading

External links

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