PECAM1 interactions

PECAM-1/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-1 mediates cellular interactions by both homophilic and heterophilic interactions. The cytoplasmic domain of PECAM-1 contains tyrosine residues which serves as docking sites for recruitment of cytosolic signaling molecules. Under conditions of platelet activation, PECAM-1 is phosphorylated by Src kinase members. The tyrosine residues 663 and 686 are required for recruitment of the SH2 domain containing PTPs.

PECAM-1/CD31属免疫球蛋白超家族（IgSF）成员，被证实在介导T淋巴细胞与血管壁的粘附及跨内皮迁移、T细胞活化和血管生成过程中发挥作用。该蛋白在其细胞外区域含有六个免疫球蛋白同源结构域，并在其细胞质区域具有ITIM基序。PECAM-1通过同源和异源相互作用介导细胞间的相互作用。PECAM-1的细胞质结构域含有酪氨酸残基，这些残基作为细胞质信号分子的结合位点。在血小板激活的条件下，PECAM-1被Src激酶家族成员磷酸化。酪氨酸残基663和686对于含SH2结构域的PTPs的募集是必需的。