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MBC in Press, published online ahead of print January 2, 2008
Mol. Biol. Cell 10.1091/mbc.E07-05-0499

A more recent version of this article appeared on March 1, 2008
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Submitted on May 25, 2007
Revised on November 21, 2007
Accepted on December 20, 2007

Ypi1, a Positive Regulator of Nuclear Protein Phosphatase Type 1 Activity in Saccharomyces cerevisiae

Jennifer P. Bharucha,* Jennifer R. Larson, Lu Gao, Lisa K. Daves, and Kelly Tatchell

Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130

Monitoring Editor: Charles Boone

The catalytic subunit of protein phosphatase type 1 (PP1) has an essential role in mitosis, acting in opposition to the Ipl1/Aurora B protein kinase to ensure proper kinetochore-microtubule interactions. However, the regulatory subunit(s) that completes the PP1 holoenzyme that functions in this capacity is not known. We show here that the budding yeast Ypi1 protein is a nuclear protein that functions with PP1 (Glc7) in this mitotic role. Depletion of cellular Ypi1 induces mitotic arrest due to activation of the spindle checkpoint. Ypi1 depletion is accompanied by a reduction of nuclear PP1 and by loss of nuclear Sds22, a Glc7 binding partner that is found in a ternary complex with Ypi1 and Glc7. Expression of a Ypi1 variant that binds weakly to PP1 also activates the spindle checkpoint and suppresses the temperature sensitivity of an ipl1–2 mutant. These results, together with genetic interactions among YPI1, GLC7, and SDS22 mutants, indicate that Ypi1 and Sds22 are positive regulators of the nuclear Glc7 activity that is required for mitosis.

*Present address: Laboratory of Human Retrovirology, Clinical Services Program, Applied and Developmental Research Support Program, Science Application International Corporation (SAIC)-Frederick Inc., National Cancer Institute at Frederick, Frederick, MD 21702.

Address correspondence to: Kelly Tatchell (ktatch{at}lsuhsc.edu)




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