Interaction of PECAM-1 and SHIP

Stable Identifier
Reaction [binding]
Homo sapiens
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PECAM/CD31 is a member of the immunoglobulin superfamily (IgSF) and has been implicated to mediate the adhesion and trans-endothelial migration of T-lymphocytes into the vascular wall, T cell activation and angiogenesis. It has six Ig homology domains within its extracellularly and an ITIM motif within its cytoplasmic region.
PECAM-mediated adhesion is complex, because it is capable of binding both to itself (homophilic adhesion) and to non-PECAM ligands (heterophilic adhesion). The trans-homophilic interaction between the two PECAM-1 molecules is mediated by their NH2-terminal membrane distal Ig homology domains 1 and 2 plus the proper spacing formed by the six Ig-homology domains.

Literature References
PubMed ID Title Journal Year
10350061 Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31

Pumphrey, NJ, Taylor, V, Freeman, S, Douglas, MR, Bradfield, PF, Young, SP, Lord, JM, Wakelam, MJ, Bird, IN, Salmon, M, Buckley, CD

FEBS Lett 1999
Orthologous Events
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