Title: | A seven-transmembrane RGS protein that modulates plant cell proliferation |
Author(s): | Chen JG; Willard FS; Huang J; Liang J; Chasse SA; Jones AM; Siderovski DP; |
Address: | "Department of Biology, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA" |
ISSN/ISBN: | 1095-9203 (Electronic) 0036-8075 (Linking) |
Abstract: | "G protein-coupled receptors (GPCRs) at the cell surface activate heterotrimeric G proteins by inducing the G protein alpha (Galpha) subunit to exchange guanosine diphosphate for guanosine triphosphate. Regulators of G protein signaling (RGS) proteins accelerate the deactivation of Galpha subunits to reduce GPCR signaling. Here we identified an RGS protein (AtRGS1) in Arabidopsis that has a predicted structure similar to a GPCR as well as an RGS box with GTPase accelerating activity. Expression of AtRGS1 complemented the pheromone supersensitivity phenotype of a yeast RGS mutant, sst2Delta. Loss of AtRGS1 increased the activity of the Arabidopsis Galpha subunit, resulting in increased cell elongation in hypocotyls in darkness and increased cell production in roots grown in light. These findings suggest that AtRGS1 is a critical modulator of plant cell proliferation" |
Keywords: | Alleles Amino Acid Sequence Arabidopsis/*cytology/genetics/*metabolism Arabidopsis Proteins/chemistry/genetics/*metabolism Cell Differentiation *Cell Division Cell Membrane/metabolism *GTP-Binding Protein alpha Subunits Heterotrimeric GTP-Binding Proteins; |
Notes: | "MedlineChen, Jin-Gui Willard, Francis S Huang, Jirong Liang, Jiansheng Chasse, Scott A Jones, Alan M Siderovski, David P eng GM65533/GM/NIGMS NIH HHS/ R01 GM065989-02/GM/NIGMS NIH HHS/ GM055316/GM/NIGMS NIH HHS/ GM65989/GM/NIGMS NIH HHS/ R01 GM065989-01/GM/NIGMS NIH HHS/ GM62338/GM/NIGMS NIH HHS/ R01 GM065989/GM/NIGMS NIH HHS/ R01 GM065989-04/GM/NIGMS NIH HHS/ R01 GM065989-03/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. 2003/09/23 Science. 2003 Sep 19; 301(5640):1728-31. doi: 10.1126/science.1087790" |