TY - JOUR
T1 - Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
AU - Tamagnone, Luca
AU - Artigiani, Stefania
AU - Chen, Hang
AU - He, Zhigang
AU - Ming, Guo-Li
AU - Song, Hong-Jun
AU - Chedotal, Alain
AU - Winberg, Margaret L.
AU - Goodman, Corey S.
AU - Poo, Mu-Ming
AU - Tessier-Lavigne, Marc
AU - Comoglio, Paolo M.
PY - 1999
Y1 - 1999
N2 - In Drosophila, plexin A is a functional receptor for semaphorin-1a. Here we show that the human plexin gene family comprises at least nine members in four subfamilies. Plexin-B1 is a receptor for the transmembrane semaphorin Sema4D (CD100), and plexin-C1 is a receptor for the GPI-anchored semaphorin Sema7A (Sema-K1). Secreted (class 3) semaphorins do not bind directly to plexins, but rather plexins associate with neuropilins, coreceptors for these semaphorins. Plexins are widely expressed: in neurons, the expression of a truncated plexin-A1 protein blocks axon repulsion by Sema3A. The cytoplasmic domain of plexins associates with a tyrosine kinase activity. Plexins may also act as ligands mediating repulsion in epithelial cells in vitro. We conclude that plexins are receptors for multiple (and perhaps all) classes of semaphorins, either alone or in combination with neuropilins, and trigger a novel signal transduction pathway controlling cell repulsion.
AB - In Drosophila, plexin A is a functional receptor for semaphorin-1a. Here we show that the human plexin gene family comprises at least nine members in four subfamilies. Plexin-B1 is a receptor for the transmembrane semaphorin Sema4D (CD100), and plexin-C1 is a receptor for the GPI-anchored semaphorin Sema7A (Sema-K1). Secreted (class 3) semaphorins do not bind directly to plexins, but rather plexins associate with neuropilins, coreceptors for these semaphorins. Plexins are widely expressed: in neurons, the expression of a truncated plexin-A1 protein blocks axon repulsion by Sema3A. The cytoplasmic domain of plexins associates with a tyrosine kinase activity. Plexins may also act as ligands mediating repulsion in epithelial cells in vitro. We conclude that plexins are receptors for multiple (and perhaps all) classes of semaphorins, either alone or in combination with neuropilins, and trigger a novel signal transduction pathway controlling cell repulsion.
KW - Biochemistry, Genetics and Molecular Biology (all)
KW - Biochemistry, Genetics and Molecular Biology (all)
UR - http://hdl.handle.net/10807/141415
UR - http://www.cell.com
U2 - 10.1016/S0092-8674(00)80063-X
DO - 10.1016/S0092-8674(00)80063-X
M3 - Article
SN - 0092-8674
VL - 99
SP - 71
EP - 80
JO - Cell
JF - Cell
ER -