Interaction of a G-protein β-subunit with a conserved sequence in Ste20/PAK family protein kinases View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-01

AUTHORS

Thomas Leeuw, Cunle Wu, Joseph D. Schrag, Malcolm Whiteway, David Y. Thomas, Ekkehard Leberer

ABSTRACT

Serine/threonine protein kinases of the Ste20/PAK family have been implicated in the signalling from heterotrimeric G proteins to mitogen-activated protein (MAP) kinase cascades1,2. In the yeast Saccharomyces cerevisiae, Ste20 is involved in transmitting the mating-pheromone signal from the βγ-subunits (encoded by the STE4 and STE18 genes, respectively) of a heterotrimeric G protein to a downstream MAP kinase cascade1. We have identified a binding site for the G-protein β-subunit (Gβ) in the non-catalytic carboxy-terminal regions of Ste20 and its mammalian homologues, the p21-activated protein kinases (PAKs). Association of Gβ with this site in Ste20 was regulated by binding of pheromone to the receptor. Mutations in Gβ and Ste20 that prevented this association blocked activation of the MAP kinase cascade. Considering the high degree of structural and functional conservation of Ste20/PAK family members and G-protein subunits, our results provide a possible model for a role of these kinases in Gβγ-mediated signal transduction in organisms ranging from yeast to mammals. More... »

PAGES

191-195

Journal

TITLE

Nature

ISSUE

6663

VOLUME

391

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/34448

DOI

http://dx.doi.org/10.1038/34448

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003977887

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9428767


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