Molecular Biology of the Cell click for ASCB 2009 Annual Meeting page

Home Help [Feedback] [For Subscribers] [Archive] [Search] --
QUICK SEARCH:   [advanced]


     

MBC in Press, published online ahead of print January 24, 2007
Mol. Biol. Cell 10.1091/mbc.E06-04-0360

A more recent version of this article appeared on April 1, 2007
This Article
Right arrow Full Text (PDF)
Right arrow Supplemental Material
Right arrow All Versions of this Article:
E06-04-0360v1
18/4/1187    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Moore, J. K.
Right arrow Articles by Miller, R. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Moore, J. K.
Right arrow Articles by Miller, R. K.

Submitted on April 27, 2006
Revised on January 11, 2007
Accepted on January 12, 2007

The CDK, Cdc28p, Regulates Multiple Aspects of Kar9p Function in Yeast

Jeffrey K. Moore and Rita K. Miller

Department of Biology, University of Rochester, Rochester, NY 14627

Monitoring Editor: Tim Stearns

During mitosis in the yeast S. cerevisiae, Kar9p directs one spindle pole body (SPB) toward the incipient daughter cell by linking the associated set of cytoplasmic microtubules (cMTs) to the polarized actin network on the bud cortex. The asymmetric localization of Kar9p to one SPB and attached cMTs is dependent on its interactions with microtubule-associated proteins and is regulated by the yeast Cdk1, Cdc28p. Liakopoulos et al. (2003) identified two phosphorylation sites in Kar9p. Here, we propose that the two sites are likely to govern Kar9p function through separate mechanisms, each involving a distinct cyclin. In the first mechanism, phosphorylation at serine 496 recruits Kar9p to one SPB. A phospho-mimetic mutation at serine 496 bypasses the requirement of BIK1 and CLB5 in generating Kar9p asymmetry. In the second mechanism, Clb4p may target serine 197 of Kar9p for phosphorylation. This modification is required for Kar9p to direct cMTs to the bud. Two-hybrid analysis suggests that this phosphorylation may attenuate the interaction between Kar9p and the XMAP215-homologue Stu2p. We propose that phosphorylation at serine 197 regulates the release of Kar9p from Stu2p at the SPB, either to clear it from the mother-SPB or to allow it to travel to the plus end.

Address correspondence to: Rita K. Miller (rmlr{at}mail.rochester.edu)




This article has been cited by other articles:


Home page
 GeneticsHome page
N. Meednu, H. Hoops, S. D'Silva, L. Pogorzala, S. Wood, D. Farkas, M. Sorrentino, E. Sia, P. Meluh, and R. K. Miller
The Spindle Positioning Protein Kar9p Interacts With the Sumoylation Machinery in Saccharomyces cerevisiae
Genetics, December 1, 2008; 180(4): 2033 - 2055.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] --
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.