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 AbstractMolecular characterization of atmospheric particulate organosulfates in a port environment using ultrahigh resolution mass spectrometry: Identification of traffic emissions    Next AbstractIdentification of candidate olfactory genes in cicada Subpsaltria yangi by antennal transcriptome analysis »

J Cell Sci


Title:Formin-induced actin cables are required for polarized recruitment of the Ste5 scaffold and high level activation of MAPK Fus3
Author(s):Qi M; Elion EA;
Address:"Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, MA 02115, USA"
Journal Title:J Cell Sci
Year:2005
Volume:20050616
Issue:Pt 13
Page Number:2837 - 2848
DOI: 10.1242/jcs.02418
ISSN/ISBN:0021-9533 (Print) 0021-9533 (Linking)
Abstract:"Little is known about how a mitogen-activated protein kinase (MAPK) cascade is targeted to specific sites at the plasma membrane during receptor stimulation. In budding yeast, the Ste5 scaffold is recruited to a receptor-coupled G protein during mating pheromone stimulation, allowing the tethered MAPK cascade to be activated by Ste20, a Cdc42-anchored kinase. Here we show that stable recruitment of Ste5 at cortical sites requires the formin Bni1, Bni1-induced actin cables, Rho1 and Myo2. Rho1 directs recruitment of Bni1 via the Rho-binding domain, and Bni1 mediates localization of Ste5 through actin cables and Myo2, which co-immunoprecipitates with Ste5 during receptor stimulation. Bni1 is also required for polarized recruitment and full activation of MAPK Fus3, which must bind Ste5 to be activated, and polarized recruitment of Cdc24, the guanine exchange factor that binds Ste5 and promotes its recruitment to the G protein. In contrast, Bni1 is not important for activation of MAPK Kss1, which can be activated while not bound to Ste5 and does not accumulate at cortical sites. These findings reveal that Bni1 mediates the formation of a Ste5 scaffold/Fus3 MAPK signaling complex at polarized sites, and suggests that a pool of Ste5 may translocate along formin-induced actin cables to the cell cortex"
Keywords:"Actins/*metabolism Adaptor Proteins, Signal Transducing/*metabolism Bridged Bicyclo Compounds, Heterocyclic/pharmacology *Cell Polarity Microfilament Proteins/*metabolism Mitogen-Activated Protein Kinases/drug effects/*metabolism Myosin Heavy Chains/metab;"
Notes:"MedlineQi, Maosong Elion, Elaine A eng GM46962/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. England 2005/06/18 J Cell Sci. 2005 Jul 1; 118(Pt 13):2837-48. doi: 10.1242/jcs.02418. Epub 2005 Jun 16"

 
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 16-11-2024