The interaction of RGSZ1 with @entity70713 attenuates the ability of XXXX to promote microtubule disassembly.

@entity46337 @entity375 @entity70713
@entity46337 proteins (regulators of G protein signaling) are a diverse family of proteins that act to negatively regulate signaling by heterotrimeric G proteins. Initially characterized as GTPase-activating proteins for Galpha subunits, recent data have implied additional functions for @entity46337 proteins. We previously identified an @entity46337 protein (termed RGSZ1) whose expression is quite specific to neuronal tissue (Glick, J. L., Meigs, T. E., Miron, A., and Casey, P. J. (1998) J. Biol. Chem. 273, 26008-26013). In a continuing effort to understand the role of RGSZ1 in cellular signaling, the yeast two-hybrid system was employed to identify potential effector proteins of RGSZ1. The microtubule-destabilizing protein @entity70713 (superior cervical ganglia, neural specific 10) was found to directly interact with RGSZ1 in the @entity375 system, and this interaction was further verified using direct binding assays. Treatment of PC12 cells with nerve growth factor resulted in Golgi-specific distribution of @entity70713 . A green fluorescent protein-tagged variant of RGSZ1 translocated to the Golgi complex upon treatment of PC12 cells with nerve growth factor, providing evidence that RGSZ1 and @entity70713 interact in cells as well as in vitro. Analysis of in vitro microtubule polymerization/depolymerization showed that binding of RGSZ1 to @entity70713 effectively blocked the ability of @entity70713 to induce microtubule disassembly as determined by both turbidimetric and microscopy-based assays. These results identify a novel connection between @entity46337 proteins and the cytoskeletal network that points to a broader role than previously envisioned for @entity46337 proteins in regulating biological processes.
