High impact information on RGS20

• In summary, these data suggest that RGSZ1 serves as a GTPase accelerating protein for Galpha(i) and regulates Galpha(i)-mediated signaling, thus expanding the potential role of RGSZ1 in G protein-mediated cellular activities [1].
• Analysis of in vitro microtubule polymerization/depolymerization showed that binding of RGSZ1 to SCG10 effectively blocked the ability of SCG10 to induce microtubule disassembly as determined by both turbidimetric and microscopy-based assays [2].
• Furthermore, RGSZ1 attenuated D2 dopamine receptor agonist-induced serum response element reporter gene activity in Chinese hamster ovary cells [1].
• The microtubule-destabilizing protein SCG10 (superior cervical ganglia, neural specific 10) was found to directly interact with RGSZ1 in the yeast system, and this interaction was further verified using direct binding assays [2].
• Using glutathione S-transferase fusion protein pull-down assays, glutathione S-transferase-RGSZ1 protein was shown to bind (35)S-labeled Galpha(i1) protein in an AlF(4)(-)dependent manner [1].

Biological context of RGS20

• RGS20 spans approximately 107 kb and contains at least seven exons [3].
• Phosphorylation of Galphaz by protein kinase C inhibited the GAP activity of RGSZ1 and other RGS proteins, providing a mechanism for potentiation of Gz signaling by protein kinase C [4].
• The interaction between RGSZ1 and Galpha(i) was confirmed further by co-immunoprecipitation studies and yeast two-hybrid experiments using a quantitative luciferase reporter gene [1].

Anatomical context of RGS20

• Northern blot analysis revealed that expression of RGSZ1 was limited to brain, and expression was particularly high in the caudate nucleus [5].
• The interaction of RGSZ1 with SCG10 attenuates the ability of SCG10 to promote microtubule disassembly [2].
• 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 SCG10 interact in cells as well as in vitro [2].

Associations of RGS20 with chemical compounds

• Deletion of the N-terminal domain of RGSZ that includes the cysteine motif promoted nuclear localization of RGSZ [6].

Physical interactions of RGS20

• RGSZ1 has been reported to interact with G-protein subunits of the Galphai family and function as a GTPase-accelerating protein on intrinsic Galphai GTPase activity [7].

Other interactions of RGS20

• Other enzymological properties of RGSZ1, brain Gz GAP, and RET-RGS1 were identical; GAIP differed only in Mg2+ dependence and in its slightly lower selectivity for Galphaz [4].
• Phosphorylation of Gzalpha by protein kinase C, an event known to occur in cells and that was previously shown to influence alpha-betagamma interactions of Gz, rendered the G protein much less susceptible to RGSZ1 action [5].
• PAK1-phosphorylated Galpha(z) was resistant both to RGSZ1, a G(z)-selective GTPase-activating protein (GAP), and to RGS4, a relatively nonselective GAP for the G(i) and G(q) families of G proteins [8].
• Previously, we employed the yeast two-hybrid system and identified the microtubule-destabilizing protein, superior cervical ganglia neural-specific 10 protein (SCG10), as a potential effector protein of RGSZ1 [9].

References