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JAM2

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This is an old revision of this page, as edited by Jimw338 (talk | contribs) at 17:31, 8 January 2017 (Interactions: added link to "VLA-1" for "α4β1" - is this correct? (or is VLA-1 actually the receptor of α4β1)). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

JAM2
Identifiers
AliasesJAM2, C21orf43, CD322, JAM-B, JAMB, PRO245, VE-JAM, VEJAM, junctional adhesion molecule 2, IBGC8
External IDsOMIM: 606870; MGI: 1933820; HomoloGene: 10929; GeneCards: JAM2; OMA:JAM2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001270407
NM_001270408
NM_021219

NM_023844

RefSeq (protein)

NP_001257336
NP_001257337
NP_067042

NP_076333

Location (UCSC)Chr 21: 25.64 – 25.72 MbChr 16: 84.57 – 84.62 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Junctional adhesion molecule B is a protein that in humans is encoded by the JAM2 gene.[5][6][7] 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.[7]

It is purported to promote lymphocyte transendothelial migration.[8] It might also be involved with endothelial cell polarity, by associating to cell polarity protein PAR-3, together with JAM3.[9]

Interactions

JAM2 has been shown to interact with PARD3.[9]

It also interacts with the integrin dimer VLA-4 (also called α4β1).[10]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000154721Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000053062Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  6. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  7. ^ a b "Entrez Gene: JAM2 junctional adhesion molecule 2".
  8. ^ 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.
  9. ^ a b 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.
  10. ^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

Further reading

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