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Sci. Signal., 17 January 2012
Vol. 5, Issue 207, p. ra6
Activating a GAP by Dimerization
Plexins are receptors for semaphorins, a family of axon guidance molecules. The biochemical and structural analyses performed by Wang et al. suggested that semaphorin binding triggered activation of plexin by inducing dimerization. Furthermore, they found that plexins could act as guanosine triphosphatase (GTPase)–activating proteins for the small GTPase Rap and that the ability of semaphorins to trigger the collapse of axonal growth cones required the inactivation of Rap by plexins. Thus, these results provide a plexin-mediated signaling pathway that could be exploited in regenerative therapies for axon-severing injuries.
Citation: Y. Wang, H. He, N. Srivastava, S. Vikarunnessa, Y.-b. Chen, J. Jiang, C. W. Cowan, X. Zhang, Plexins Are GTPase-Activating Proteins for Rap and Are Activated by Induced Dimerization. Sci. Signal.5, ra6 (2012).
Neuroimmune Guidance Cue Semaphorin 3E Is Expressed in Atherosclerotic Plaques and Regulates Macrophage Retention.
A. Wanschel, T. Seibert, B. Hewing, B. Ramkhelawon, T. D. Ray, J. M. van Gils, K. J. Rayner, J. E. Feig, E. R. O'Brien, E. A. Fisher, et al. (2013)
Arterioscler Thromb Vasc Biol
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Plexin B1 inhibits MET through direct association and regulates Shp2 expression in melanocytes.