Plexins are a family of large integral membrane proteins that complex with neuropilins to form semaphorin co-receptors. The extracellular region of plexins contains a semaphorin domain, multiple glycine-rich motifs, and MET-related sequences. The cytoplasmic region contains a Sex/Plexin domain and putative tyrosine phosphorylation sites that mediate signal transduction after activation. In addition, Plexin B1 and B2 contain cleavage sites for subtilisin-like proprotein convertases. These cleavage sites may be important for regulating assembly of heterodimeric receptors or release of the extracellular domain. Plexin-B1 is expressed as a 300 kDa precursor protein that can be cleaved into a 200 kDa a-subunit and a 100 kDa b-subunit. This plexin is the receptor for the class IV semaphorin, Sema-4D. Sema-4D activation of Plexin B1 recruits and activates c-Met, which can promote cell survival, migration, and angiogenesis.
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*For more information, see UniProt Accession O43157
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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