JCB logo
MBoC5 from Garland Science
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 20 January 2004. doi:10.1083/jcb.200310021
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 2, 267-277
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kusari, A. B.
Right arrow Articles by Bardwell, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kusari, A. B.
Right arrow Articles by Bardwell, L.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1

Anasua B. Kusari, Douglas M. Molina, Walid Sabbagh, Jr., Chang S. Lau, and Lee Bardwell

Department of Developmental and Cell Biology, University of California, Irvine, Irvine, CA 92697

Address correspondence to Lee Bardwell, Dept. of Developmental and Cell Biology, 5205 McGaugh Hall, University of California, Irvine, Irvine, CA 92697-2300. Tel.: (949) 824-6902. Fax: (949) 824-4709. email: bardwell{at}uci.edu

The Saccharomyces cerevisiae mitogen-activated protein kinases (MAPKs) Fus3 and Kss1 bind to multiple regulators and substrates. We show that mutations in a conserved docking site in these MAPKs (the CD/7m region) disrupt binding to an important subset of their binding partners, including the Ste7 MAPK kinase, the Ste5 adaptor/scaffold protein, and the Dig1 and Dig2 transcriptional repressors. Supporting the possibility that Ste5 and Ste7 bind to the same region of the MAPKs, they partially competed for Fus3 binding. In vivo, some of the MAPK mutants displayed reduced Ste7-dependent phosphorylation, and all of them exhibited multiple defects in mating and pheromone response. The Kss1 mutants were also defective in Kss1-imposed repression of Ste12. We conclude that MAPKs contain a structurally and functionally conserved docking site that mediates an overall positively acting network of interactions with cognate docking sites on their regulators and substrates. Key features of this interaction network appear to have been conserved from yeast to humans.

Key Words: mitogen-activated protein kinases; signal transduction; phosphorylation; binding sites; protein binding

A.B. Kusari and D.M. Molina contributed equally to this work.

The online version of this article includes supplemental material.

A.B. Kusari's present address is Keck Graduate Institute of Applied Life Sciences, 535 Watson Dr., Claremont, CA 91711.

Abbreviations used in this paper: CD, conserved docking; ERK, extracellular signal–regulated kinase; FRE, filamentation response element; GBD, Gal4 DNA-binding domain; JNK, c-Jun N-terminal kinase; MEK, MAPK/ERK kinase; MEKK, MEK kinase; MKK, MAPK kinase.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents