HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 15, 14591-14596, April 15, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/15/14591    most recent M500560200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ren, L. Articles by Gould, K. L. Search for Related Content PubMed PubMed Citation Articles by Ren, L. Articles by Gould, K. L. Social Bookmarking                      What's this?

Analysis of the Role of Phosphorylation in Fission Yeast Cdc13p/CyclinB Function^*

Liping Ren, Anna Feoktistova, W. Hayes McDonald, Greg Den Haese, Jennifer L. Morrell, and Kathleen L. Gould

From the Howard Hughes Medical Institute and Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

The Cdk1p-cyclin B complex drives entry into mitosis in all eukaryotes. Cdc13p is the single essential cyclin in Schizosaccharomyces pombe and a member of the cyclin B family. Cdc13p abundance rises during G₂-phase and falls as cells progress through mitosis and G₁. Cdc13p degradation, mediated by the anaphase-promoting complex, is an important mechanism of Cdk1p inhibition and mitotic exit. Cdk1p-cyclin B1 complexes shuttle between the nucleus and cytoplasm, and preventing nuclear accumulation of Cdk1p-cyclin B1 in mammalian cells appears to be one mechanism of preventing entry into mitosis during a DNA damage-induced checkpoint delay. In vertebrates, phosphorylation plays a key role in regulating the intracellular distribution of cyclins. Previous mass spectrometric analysis identified sites of Cdc13p phosphorylation. Here, we have confirmed that these sites are the sole in vivo Cdc13p phosphorylation sites and have studied the role that phosphorylation plays in Cdc13p localization and function. Our data indicate that Cdc13p accumulates in the nucleolus in response to G₂ checkpoint delays, rather than in the cytoplasm, and that phosphorylation plays no role in Cdc13p localization or function.

Received for publication, January 18, 2005

^* This work was supported by National Institutes of Health Grant GM47728. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. This work was supported by National Institutes of Health Grant GM47728.

To whom correspondence should be addressed: HHMI and Dept. of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232. Tel.: 615-343-9502; Fax: 615-343-0723; E-mail: Kathy.gould{at}vanderbilt.edu.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. D. Unwin, J. R. Griffiths, M. K. Leverentz, A. Grallert, I. M. Hagan, and A. D. Whetton Multiple Reaction Monitoring to Identify Sites of Protein Phosphorylation with High Sensitivity Mol. Cell. Proteomics, August 1, 2005; 4(8): 1134 - 1144. [Abstract] [Full Text] [PDF]