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PMID: 8846783 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating.

The EMBO journal ·Vol. 14 ·No. 23 ·1995-12-01 ·Pages 5908-19

Ottilie S, Miller PJ, Johnson DI, Creasy CL, Sells MA, Bagrodia S, Forsburg SL, Chernoff J

Abstract

A STE20/p65pak homolog was isolated from fission yeast by PCR. The pak1+ gene encodes a 72 kDa protein containing a putative p21-binding domain near its amino-terminus and a serine/threonine kinase domain near its carboxyl-terminus. The Pak1 protein autophosphorylates on serine residues and preferentially binds to activated Cdc42p both in vitro and in vivo. This binding is mediated through the p21 binding domain on Pak1p and the effector domain on Cdc42p. Overexpression of an inactive mutant form of pak1 gives rise to cells with markedly abnormal shape with mislocalized actin staining. Pak1 overexpression does not, however, suppress lethality associated with cdc42-null cells or the morphologic defeat caused by overexpression of mutant cdc42 alleles. Gene disruption of pak1+ establishes that, like cdc42+, pak1+ function is required for cell viability. In budding yeast, pak1+ expression restores mating function to STE20-null cells and, in fission yeast, overexpression of an inactive form of Pak inhibits mating. These results indicate that the Pak1 protein is likely to be an effector for Cdc42p or a related GTPase, and suggest that Pak1p is involved in the maintenance of cell polarity and in mating.

MeSH Terms
Actins/genetics,metabolism Amino Acid Sequence Base Sequence Cell Cycle Proteins/metabolism Cell Polarity/genetics Cloning, Molecular Fungal Proteins/metabolism GTP Phosphohydrolases/metabolism GTP-Binding Proteins/metabolism Gene Expression Regulation, Fungal Genes, Fungal/genetics Microscopy, Fluorescence Molecular Sequence Data Mutation/genetics Phenotype Protein Serine-Threonine Kinases/chemistry,genetics,metabolism Saccharomyces cerevisiae/genetics,physiology Saccharomyces cerevisiae Proteins Schizosaccharomyces/genetics,physiology Sequence Analysis Sequence Homology, Amino Acid cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Chemicals
Actins Cell Cycle Proteins Fungal Proteins Saccharomyces cerevisiae Proteins PRK1 protein, S cerevisiae Protein Serine-Threonine Kinases GTP Phosphohydrolases GTP-Binding Proteins cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Ottilie S
Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92186, USA.
Miller P J
Johnson D I
Creasy C L
Sells M A
Bagrodia S
Forsburg S L
Chernoff J
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1995-12-01
Pages
5908-19
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394709
Subset
IM
Grants
NCI NIH HHS · CA-09370 · United States
NCI NIH HHS · CA14195 · United States
NCI NIH HHS · CA58836 · United States
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GENBANK
U22371
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