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XB-ART-11326
J Cell Biol March 20, 2000; 148 (6): 1283-93.

Determination of cell adhesion sites of neuropilin-1.

Shimizu M , Murakami Y , Suto F , Fujisawa H .


Abstract
Neuropilin-1 is a type 1 membrane protein with three distinct functions. First, it can mediate cell adhesion via a heterophilic molecular interaction. Second, in neuronal cells, neuropilin-1 binds the class 3 semaphorins, which are neuronal chemorepellents, and plays a role in the directional guidance of axons. Neuropilin-1 is expected to form complexes with the plexinA subfamily members and mediate the semaphorin-elicited inhibitory signals into neurons. Third, in endothelial cells, neuropilin-1 binds a potent endothelial cell mitogen, vascular endothelial growth factor (VEGF)(165), and regulates vessel formation. Though the binding sites in neuropilin-1 for the class 3 semaphorins and VEGF(165) have been analyzed, the sites involved in cell adhesion activity of the molecule have not been identified. In this study, we produced a variety of mutant neuropilin-1s and tested their cell adhesion activity. We showed that the b1 and b2 domains within the extracellular segment of neuropilin-1 were required for the cell adhesion activity, and peptides with an 18-amino acid stretch in the b1 and b2 domains were sufficient to induce the cell adhesion activity. In addition, we demonstrated that the cell adhesion ligands for neuropilin-1 were proteins and distributed in embryonic mesenchymal cells but distinct from the class 3 semaphorins, VEGF, or plexins.

PubMed ID: 10725340
PMC ID: PMC2174302
Article link: J Cell Biol

Genes referenced: myc nppc nrp1 prss1 sema3a sema3b sema3c tubb2b vegfa


Article Images: [+] show captions
References [+] :
, Unified nomenclature for the semaphorins/collapsins. Semaphorin Nomenclature Committee. 1999, Pubmed


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