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- W2149373178 startingPage "4557" @default.
- W2149373178 abstract "All eukaryotic cells sense extracellular stimuli and activate intracellular signaling cascades via G protein-coupled receptors (GPCR) and associated heterotrimeric G proteins. The Saccharomyces cerevisiae GPCR Gpr1 and associated Gα subunit Gpa2 sense extracellular carbon sources (including glucose) to govern filamentous growth. In contrast to conventional Gα subunits, Gpa2 forms an atypical G protein complex with the kelch repeat Gβ mimic proteins Gpb1 and Gpb2. Gpb1/2 negatively regulate cAMP signaling by inhibiting Gpa2 and an as yet unidentified target. Here we show that Gpa2 requires lipid modifications of its N-terminus for membrane localization but association with the Gpr1 receptor or Gpb1/2 subunits is dispensable for membrane targeting. Instead, Gpa2 promotes membrane localization of its associated Gβ mimic subunit Gpb2. We also show that the Gpa2 N-terminus binds both to Gpb2 and to the C-terminal tail of the Gpr1 receptor and that Gpb1/2 binding interferes with Gpr1 receptor coupling to Gpa2. Our studies invoke novel mechanisms involving GPCR-G protein modules that may be conserved in multicellular eukaryotes." @default.
- W2149373178 created "2016-06-24" @default.
- W2149373178 creator A5051709961 @default.
- W2149373178 creator A5052159588 @default.
- W2149373178 date "2005-10-01" @default.
- W2149373178 modified "2023-09-23" @default.
- W2149373178 title "Gα Subunit Gpa2 Recruits Kelch Repeat Subunits That Inhibit Receptor-G Protein Coupling during cAMP-induced Dimorphic Transitions in<i>Saccharomyces cerevisiae</i>" @default.
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- W2149373178 doi "https://doi.org/10.1091/mbc.e05-05-0403" @default.
- W2149373178 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1237064" @default.