JAM2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Junctional adhesion molecule B''' is a [[protein]] that in humans is encoded by the ''JAM2'' [[gene]].<ref name="pmid10779521">{{cite journal |vauthors=Palmeri D, van Zante A, Huang CC, Hemmerich S, Rosen SD | title = Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells | journal = J Biol Chem | volume = 275 | issue = 25 | pages = 19139–45 |date=Aug 2000 | pmid = 10779521 | doi = 10.1074/jbc.M003189200 }}</ref><ref name="pmid10945976">{{cite journal |vauthors=Cunningham SA, Arrate MP, Rodriguez JM, Bjercke RJ, Vanderslice P, Morris AP, Brock TA | title = A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions | journal = J Biol Chem | volume = 275 | issue = 44 | pages = 34750–6 |date=Nov 2000 | pmid = 10945976 | doi = 10.1074/jbc.M002718200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: JAM2 junctional adhesion molecule 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58494| accessdate = }}</ref> JAM2 has also been designated as '''CD322''' ([[cluster of differentiation]] 322).
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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. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Junctional adhesion molecule 2
| HGNCid = 14686
| Symbol = JAM2
| AltSymbols =; C21orf43; CD322; JAM-B; JAMB; PRO245; VE-JAM; VEJAM
| OMIM = 606870
| ECnumber = 
| Homologene = 10929
| MGIid = 1933820
| GeneAtlas_image1 = PBB_GE_JAM2_219213_at_tn.png
| Function =  
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005923 |text = tight junction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 58494
    | Hs_Ensembl = ENSG00000154721
    | Hs_RefseqProtein = NP_067042
    | Hs_RefseqmRNA = NM_021219
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 21
    | Hs_GenLoc_start = 25933515
    | Hs_GenLoc_end = 26009078
    | Hs_Uniprot = P57087
    | Mm_EntrezGene = 67374
    | Mm_Ensembl = ENSMUSG00000053062
    | Mm_RefseqmRNA = NM_023844
    | Mm_RefseqProtein = NP_076333
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 84657025
    | Mm_GenLoc_end = 84707359
    | Mm_Uniprot = Q9JI59
  }}
}}
'''Junctional adhesion molecule 2''', also known as '''JAM2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: JAM2 junctional adhesion molecule 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58494| accessdate = }}</ref> JAM2 has also been designated as '''CD322''' ([[cluster of differentiation]] 322).


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Tight junction]]s represent one mode of cell-to-cell adhesion in [[endothelial cell]] sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the [[paracellular transport|paracellular space]]. The protein encoded by this [[immunoglobulin domain|immunoglobulin]] superfamily gene member is localized in the tight junctions between [[High endothelial venules|high endothelial cells]]. It acts as an adhesive ligand for interacting with a variety of [[immune cell]] types and may play a role in [[lymphocyte]] [[Lymphocyte homing receptor|homing]] to secondary [[lymphatic system|lymphoid organs]].<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. It acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.<ref name="entrez">{{cite web | title = Entrez Gene: JAM2 junctional adhesion molecule 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=58494| accessdate = }}</ref>
}}


==References==
It is purported to promote lymphocyte transendothelial migration.<ref name="pmid12239159">{{cite journal |vauthors=Johnson-Léger CA, Aurrand-Lions M, Beltraminelli N, Fasel N, Imhof BA | title = Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration | journal = Blood | volume = 100 | issue = 7 | pages = 2479–86 |date=October 2002 | pmid = 12239159 | doi = 10.1182/blood-2001-11-0098 }}</ref> It might also be involved with endothelial cell polarity, by associating to cell polarity protein PAR-3, together with JAM3.<ref name="pmid12953056">{{cite journal |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D | title = The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity | journal = J. Cell Sci. | volume = 116 | issue = Pt 19 | pages = 3879–91 |date=October 2003 | pmid = 12953056 | doi = 10.1242/jcs.00704 }}</ref>
{{reflist|2}}


==Further reading==
== Interactions ==
 
JAM2 has been shown to [[Protein-protein interaction|interact]] with [[PARD3]].<ref name="pmid12953056"/>
 
It also interacts with the [[integrin]] dimer [[VLA-4]] (also called α4β1).<ref name="pmid12070135">{{cite journal |vauthors=Cunningham SA, Rodriguez JM, Arrate MP, Tran TM, Brock TA | title = JAM2 interacts with alpha4beta1. Facilitation by JAM3 | journal = J. Biol. Chem. | volume = 277 | issue = 31 | pages = 27589–92 |date=August 2002 | pmid = 12070135 | doi = 10.1074/jbc.C200331200 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
*{{cite journal  | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327–34 |year= 2003 |pmid= 12810109 |doi=10.1016/S1471-4906(03)00117-0 }}
| citations =
*{{cite journal  | author=Bazzoni G |title=The JAM family of junctional adhesion molecules. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 525–30 |year= 2004 |pmid= 14519386 |doi=10.1016/S0955-0674(03)00104-2  }}
*{{cite journal  | author=Muller WA |title=Leukocyte-endothelial-cell interactions in leukocyte transmigration and the inflammatory response. |journal=Trends Immunol. |volume=24 |issue= 6 |pages= 327-34 |year= 2003 |pmid= 12810109 |doi=  }}
*{{cite journal   |vauthors=Hattori M, Fujiyama A, Taylor TD, etal |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311–9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal  | author=Bazzoni G |title=The JAM family of junctional adhesion molecules. |journal=Curr. Opin. Cell Biol. |volume=15 |issue= 5 |pages= 525-30 |year= 2004 |pmid= 14519386 |doi= }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal  | author=Palmeri D, van Zante A, Huang CC, ''et al.'' |title=Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 19139-45 |year= 2000 |pmid= 10779521 |doi= 10.1074/jbc.M003189200 }}
*{{cite journal   |vauthors=Arrate MP, Rodriguez JM, Tran TM, etal |title=Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45826–32 |year= 2002 |pmid= 11590146 |doi= 10.1074/jbc.M105972200 }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
*{{cite journal   |vauthors=Liang TW, Chiu HH, Gurney A, etal |title=Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1618–26 |year= 2002 |pmid= 11823489 |doi=  10.4049/jimmunol.168.4.1618}}
*{{cite journal  | author=Cunningham SA, Arrate MP, Rodriguez JM, ''et al.'' |title=A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34750-6 |year= 2000 |pmid= 10945976 |doi= 10.1074/jbc.M002718200 }}
*{{cite journal  |vauthors=Gardiner K, Slavov D, Bechtel L, Davisson M |title=Annotation of human chromosome 21 for relevance to Down syndrome: gene structure and expression analysis. |journal=Genomics |volume=79 |issue= 6 |pages= 833–43 |year= 2002 |pmid= 12036298 |doi= 10.1006/geno.2002.6782 }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal   |vauthors=Cunningham SA, Rodriguez JM, Arrate MP, etal |title=JAM2 interacts with alpha4beta1. Facilitation by JAM3. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27589–92 |year= 2002 |pmid= 12070135 |doi= 10.1074/jbc.C200331200 }}
*{{cite journal | author=Arrate MP, Rodriguez JM, Tran TM, ''et al.'' |title=Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45826-32 |year= 2002 |pmid= 11590146 |doi= 10.1074/jbc.M105972200 }}
*{{cite journal   |vauthors=Aurrand-Lions M, Johnson-Leger C, Lamagna C, etal |title=Junctional adhesion molecules and interendothelial junctions. |journal=Cells Tissues Organs (Print) |volume=172 |issue= 3 |pages= 152–60 |year= 2004 |pmid= 12476045 |doi=10.1159/000066967 }}
*{{cite journal | author=Liang TW, Chiu HH, Gurney A, ''et al.'' |title=Vascular endothelial-junctional adhesion molecule (VE-JAM)/JAM 2 interacts with T, NK, and dendritic cells through JAM 3. |journal=J. Immunol. |volume=168 |issue= 4 |pages= 1618-26 |year= 2002 |pmid= 11823489 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Gardiner K, Slavov D, Bechtel L, Davisson M |title=Annotation of human chromosome 21 for relevance to Down syndrome: gene structure and expression analysis. |journal=Genomics |volume=79 |issue= 6 |pages= 833-43 |year= 2002 |pmid= 12036298 |doi= 10.1006/geno.2002.6782 }}
*{{cite journal   |vauthors=Ebnet K, Aurrand-Lions M, Kuhn A, etal |title=The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. |journal=J. Cell Sci. |volume=116 |issue= Pt 19 |pages= 3879–91 |year= 2004 |pmid= 12953056 |doi= 10.1242/jcs.00704 }}
*{{cite journal | author=Cunningham SA, Rodriguez JM, Arrate MP, ''et al.'' |title=JAM2 interacts with alpha4beta1. Facilitation by JAM3. |journal=J. Biol. Chem. |volume=277 |issue= 31 |pages= 27589-92 |year= 2002 |pmid= 12070135 |doi= 10.1074/jbc.C200331200 }}
*{{cite journal   |vauthors=Clark HF, Gurney AL, Abaya E, etal |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265–70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 | pmc=403697 }}
*{{cite journal | author=Aurrand-Lions M, Johnson-Leger C, Lamagna C, ''et al.'' |title=Junctional adhesion molecules and interendothelial junctions. |journal=Cells Tissues Organs (Print) |volume=172 |issue= 3 |pages= 152-60 |year= 2004 |pmid= 12476045 |doi=  }}
*{{cite journal  |vauthors=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819–24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 | pmc=2286551 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Ebnet K, Aurrand-Lions M, Kuhn A, ''et al.'' |title=The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity. |journal=J. Cell. Sci. |volume=116 |issue= Pt 19 |pages= 3879-91 |year= 2004 |pmid= 12953056 |doi= 10.1242/jcs.00704 }}
*{{cite journal   |vauthors=Wiemann S, Arlt D, Huber W, etal |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930 }}
*{{cite journal | author=Clark HF, Gurney AL, Abaya E, ''et al.'' |title=The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. |journal=Genome Res. |volume=13 |issue= 10 |pages= 2265-70 |year= 2003 |pmid= 12975309 |doi= 10.1101/gr.1293003 }}
*{{cite journal   |vauthors=Liu T, Qian WJ, Gritsenko MA, etal |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070–80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 | pmc=1850943 }}
*{{cite journal  | author=Zhang Z, Henzel WJ |title=Signal peptide prediction based on analysis of experimentally verified cleavage sites. |journal=Protein Sci. |volume=13 |issue= 10 |pages= 2819-24 |year= 2005 |pmid= 15340161 |doi= 10.1110/ps.04682504 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal | author=Liu T, Qian WJ, Gritsenko MA, ''et al.'' |title=Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. |journal=J. Proteome Res. |volume=4 |issue= 6 |pages= 2070-80 |year= 2006 |pmid= 16335952 |doi= 10.1021/pr0502065 }}
}}
{{refend}}
{{refend}}


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* {{MeshName|JAM2+protein,+human}}
* {{MeshName|JAM2+protein,+human}}


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{{Clusters of differentiation}}
{{Clusters of differentiation}}
[[Category:Clusters of differentiation]]
[[Category:Clusters of differentiation]]
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Revision as of 20:08, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Junctional adhesion molecule B is a protein that in humans is encoded by the JAM2 gene.[1][2][3] JAM2 has also been designated as CD322 (cluster of differentiation 322).

Function

Tight junctions represent one mode of cell-to-cell adhesion in endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. It acts as an adhesive ligand for interacting with a variety of immune cell types and may play a role in lymphocyte homing to secondary lymphoid organs.[3]

It is purported to promote lymphocyte transendothelial migration.[4] It might also be involved with endothelial cell polarity, by associating to cell polarity protein PAR-3, together with JAM3.[5]

Interactions

JAM2 has been shown to interact with PARD3.[5]

It also interacts with the integrin dimer VLA-4 (also called α4β1).[6]

References

  1. ↑ Palmeri D, van Zante A, Huang CC, Hemmerich S, Rosen SD (Aug 2000). "Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells". J Biol Chem. 275 (25): 19139–45. doi:10.1074/jbc.M003189200. PMID 10779521.
  2. ↑ Cunningham SA, Arrate MP, Rodriguez JM, Bjercke RJ, Vanderslice P, Morris AP, Brock TA (Nov 2000). "A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions". J Biol Chem. 275 (44): 34750–6. doi:10.1074/jbc.M002718200. PMID 10945976.
  3. ↑ 3.0 3.1 "Entrez Gene: JAM2 junctional adhesion molecule 2".
  4. ↑ Johnson-Léger CA, Aurrand-Lions M, Beltraminelli N, Fasel N, Imhof BA (October 2002). "Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration". Blood. 100 (7): 2479–86. doi:10.1182/blood-2001-11-0098. PMID 12239159.
  5. ↑ 5.0 5.1 Ebnet K, Aurrand-Lions M, Kuhn A, Kiefer F, Butz S, Zander K, Meyer zu Brickwedde MK, Suzuki A, Imhof BA, Vestweber D (October 2003). "The junctional adhesion molecule (JAM) family members JAM-2 and JAM-3 associate with the cell polarity protein PAR-3: a possible role for JAMs in endothelial cell polarity". J. Cell Sci. 116 (Pt 19): 3879–91. doi:10.1242/jcs.00704. PMID 12953056.
  6. ↑ Cunningham SA, Rodriguez JM, Arrate MP, Tran TM, Brock TA (August 2002). "JAM2 interacts with alpha4beta1. Facilitation by JAM3". J. Biol. Chem. 277 (31): 27589–92. doi:10.1074/jbc.C200331200. PMID 12070135.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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