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Vol. 18, Issue 6, 2336-2345, June 2007

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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^,, Karam S. Takhar^*,, Andrei Pozniakovsky, Anthony A. Hyman, and Michel R. Leroux^*

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

Submitted January 26, 2007; Revised March 20, 2007; Accepted March 29, 2007
Monitoring Editor: Jonathan Weissman

The C haperonin Containing Tcp1 (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 Saccharomyces 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: Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada T6G 2E9;

BC Cancer Research Centre, Vancouver, British Columbia, Canada V5Z 1L3.

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

Abbreviations used: CCT, Chaperonin Containing Tcp1; DAPI, 4',6-diamidino-2-phenylindole; FACS, fluorescence activated cell sorting; PFD, prefoldin; PhLP, phosducin-like protein.

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