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MBC in Press, published online ahead of print April 11, 2007
Mol. Biol. Cell 10.1091/mbc.E07-01-0069

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Submitted on January 26, 2007
Revised on March 20, 2007
Accepted on March 29, 2007

Functional Interaction between Phosducin-like Protein 2 and Cytosolic Chaperonin Is Essential for Cytoskeletal Protein Function and Cell Cycle Progression

Peter C. Stirling,* Martin Srayko,{dagger}{ddagger} Karam S. Takhar,*{sect} Andrei Pozniakovsky,{dagger} Anthony A. Hyman,{dagger} and Michel R. Leroux*

*Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada, V5A 1S6; {dagger}Max-Planck Institute of Molecular Cell Biology and Genetics, 03107 Dresden, Germany

Monitoring Editor: Jonathan Weissman

The chaperonin CCT maintains cellular protein folding homeostasis in the eukaryotic cytosol by assisting the biogenesis of many proteins, including actins, tubulins, and regulators of the cell cycle. Here, we demonstrate that the essential and conserved eukaryotic phosducin-like protein 2 (PhLP2/PLP2) physically interacts with CCT and modulates its folding activity. Consistent with this functional interaction, temperature-sensitive alleles of S. cerevisiae PLP2 exhibit cytoskeletal and cell cycle defects. We uncovered several high-copy suppressors of the plp2 alleles, all of which are associated with G1/S cell cycle progression but which do not appreciably affect cytoskeletal protein function or fully rescue the growth defects. Our data support a model in which Plp2p modulates the biogenesis of several CCT substrates relating to cell cycle and cytoskeletal function, which together contribute to the essential function of PLP2.

Present addresses: {ddagger}Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 2E9; {sect}BC Cancer Research Centre, 675 West 10th Ave., Vancouver, British Columbia, Canada V5Z 1L3.

Address correspondence to: Michel R. Leroux (Leroux{at}sfu.ca)




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