Abstract
The Rho protein family of small guanosine triphosphatases (GTPases) regulates axon migration by modulating the actin cytoskeleton. Wong et al. show that interaction of the secreted protein Slit, with its receptor Roundabout (Robo), decreased activity of the GTPase Cdc42 in primary rodent forebrain neurons. This signaling is mediated by the interaction of a proline-rich motif in the cytoplasmic domain of Robo with the SH3 domain of GTPase-activating proteins (GAPs) called srGAPs. The expression pattern of srGAPs in rodent neural tissue coincided with the presence of neurons that are repulsed when exposed to Slit. The authors suggest that a localized decrease in Cdc42 activity may underlie localized actin depolymerization and cause a neuron to move away from Slit. K. Wong, X.-R. Ren, Y.-Z. Huang, Y. Xie, G. Liu, H. Saito, H. Tang, L. Wen, S. M. Brady-Kalnay, L. Mei, J. Y. Wu, W.-C. Xiong, Y. Rao, Signal transduction in neuronal migration: Roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway. Cell 107 , 209-221 (2001). [Online Journal]
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
