Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractVolatile organic compound emission in tundra shrubs - Dependence on species characteristics and the near-surface environment    Next AbstractA simple structure-based calculator for estimating vapor pressure »

Life Sci Alliance


Title:Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis
Author(s):Simke WC; Johnson CP; Hart AJ; Mayhue S; Craig PL; Sojka S; Kelley JB;
Address:"Department of Molecular and Biomedical Sciences, University of Maine, Orono, ME, USA. Graduate School of Biomedical Science and Engineering, University of Maine, Orono, ME, USA. Department of Molecular and Biomedical Sciences, University of Maine, Orono, ME, USA joshua.b.kelley@maine.edu"
Journal Title:Life Sci Alliance
Year:2022
Volume:20220819
Issue:10
Page Number: -
DOI: 10.26508/lsa.202101245
ISSN/ISBN:2575-1077 (Electronic) 2575-1077 (Linking)
Abstract:"Yeast use the G-protein-coupled receptor signaling pathway to detect and track the mating pheromone. The G-protein-coupled receptor pathway is inhibited by the regulator of G-protein signaling (RGS) Sst2 which induces Galpha GTPase activity and inactivation of downstream signaling. G-protein signaling activates the MAPK Fus3, which phosphorylates the RGS; however, the role of this modification is unknown. We found that pheromone-induced RGS phosphorylation peaks early; the phospho-state of RGS controls its localization and influences MAPK spatial distribution. Surprisingly, phosphorylation of the RGS promotes completion of cytokinesis before pheromone-induced growth. Completion of cytokinesis in the presence of pheromone is promoted by the kelch-repeat protein, Kel1 and antagonized by the formin Bni1. We found that RGS complexes with Kel1 and prefers the unphosphorylatable RGS mutant. We also found overexpression of unphosphorylatable RGS exacerbates cytokinetic defects, whereas they are rescued by overexpression of Kel1. These data lead us to a model where Kel1 promotes completion of cytokinesis before pheromone-induced polarity but is inhibited by unphosphorylated RGS binding"
Keywords:"*Cytokinesis/genetics GTP-Binding Proteins/metabolism GTPase-Activating Proteins Microfilament Proteins/metabolism *Mitogen-Activated Protein Kinases/metabolism Pheromones/metabolism Phosphorylation *RGS Proteins/metabolism Receptors, G-Protein-Coupled/me;"
Notes:"MedlineSimke, William C Johnson, Cory P Hart, Andrew J Mayhue, Sari Craig, P Lucas Sojka, Savannah Kelley, Joshua B eng R15 GM128026/GM/NIGMS NIH HHS/ R15 GM140409/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't 2022/08/20 Life Sci Alliance. 2022 Aug 19; 5(10):e202101245. doi: 10.26508/lsa.202101245. Print 2022 Oct"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 27-12-2024