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Originally published In Press as doi:10.1074/jbc.M208058200 on October 28, 2002
J. Biol. Chem., Vol. 278, Issue 1, 147-153, January 3, 2003
Pho85 Phosphorylates the Glc7 Protein Phosphatase Regulator
Glc8 in Vivo*
Yves S. H.
Tan ,
Paul A.
Morcos§, and
John F.
Cannon¶
From the Department of Molecular Microbiology and Immunology,
University of Missouri, Columbia, Missouri 65212
The budding yeast Glc7 serine/threonine protein
phosphatase-1 is regulated by Glc8, the yeast ortholog of mammalian
phosphatase inhibitor-2. In this work, we demonstrated that similarly
to inhibitor-2, Glc8 function is regulated by phosphorylation. The
cyclin-dependent protein kinase, Pho85, in conjunction with
the related cyclins Pcl6 and Pcl7 comprise the major Glc8 kinase
in vivo and in vitro. Several glc7
mutations are dependent on the presence of Glc8 for viability. For
example, glc7 alleles R121K, R142H,
and R198D are lethal in combination with a glc8
deletion. We found that glc7-R121K is lethal in combination
with a pho85 deletion. This finding indicates that Pho85 is
the sole Glc8 kinase in vivo. Furthermore,
glc7-R121K is also lethal when combined with deletions of
pcl6, plc7, pcl8, and
pcl10, indicating that these related cyclins redundantly
activate Pho85 for Glc8 phosphorylation in vivo. In
vitro kinase assays and genetic results indicate that Pho85
cyclins Pcl6 and Pcl7 comprise the predominant Glc8 kinase.
*
This work was supported by the National Science Foundation,
the University of Missouri Molecular Biology Program, and the Department of Molecular Microbiology and Immunology.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address: Div. of Hematology/Oncology, Children's Hospital
Los Angeles, 4650 Sunset Blvd., Los Angeles, CA 90027.
§
Present address: Gene Tools LLC, 2680 SW 3rd St.,
Corvallis, OR 97333.
¶
To whom correspondence should be addressed: Dept. of Molecular
Microbiology and Immunology, 1 Hospital Dr., University of Missouri,
Columbia, MO 65212. Tel.: 573-882-2780; Fax: 573-882-4287; E-mail: CannonJ@missouri.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

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