QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

Vol. 15, Issue 7, 3366-3378, July 2004

This Article Full Text Full Text (PDF) Supplemental Figure All Versions of this Article: E03-12-0887v1 15/7/3366    most recent Alert me when this article is cited Alert me if a correction is posted Services 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 Rodrigo-Brenni, M. C. Articles by Kaplan, K. B. Search for Related Content PubMed PubMed Citation Articles by Rodrigo-Brenni, M. C. Articles by Kaplan, K. B.

Sgt1p and Skp1p Modulate the Assembly and Turnover of CBF3 Complexes Required for Proper Kinetochore Function

Section of Molecular and Cellular Biology, University of California, Davis, Davis, California 95616

Submitted December 12, 2003; Revised March 1, 2004; Accepted April 7, 2004
Monitoring Editor: Douglas Koshland

Kinetochores are composed of a large number of protein complexes that must be properly assembled on DNA to attach chromosomes to the mitotic spindle and to coordinate their segregation with the advance of the cell cycle. CBF3 is an inner kinetochore complex in the budding yeast Saccharomyces cerevisiae that nucleates the recruitment of all other kinetochore proteins to centromeric DNA. Skp1p and Sgt1p act through the core CBF3 subunit, Ctf13p, and are required for CBF3 to associate with centromeric DNA. To investigate the contribution of Skp1p and Sgt1p to CBF3 function, we have used a combination of in vitro binding assays and a unique protocol for synchronizing the assembly of kinetochores in cells. We have found that the interaction between Skp1p and Sgt1p is critical for the assembly of CBF3 complexes. CBF3 assembly is not restricted during the cell cycle and occurs in discrete steps; Skp1p and Sgt1p contribute to a final, rate-limiting step in assembly, the binding of the core CBF3 subunit Ctf13p to Ndc10p. The assembly of CBF3 is opposed by its turnover and disruption of this balance compromises kinetochore function without affecting kinetochore formation on centromeric DNA.

^* Corresponding author. E-mail address: kbkaplan{at}ucdavis.edu.

This article has been cited by other articles:

				S. Thomas and K. B. Kaplan A Bir1p Sli15p Kinetochore Passenger Complex Regulates Septin Organization during Anaphase Mol. Biol. Cell, October 1, 2007; 18(10): 3820 - 3834. [Abstract] [Full Text] [PDF]

				K. L. Witkin, R. Prathapam, and K. Collins Positive and Negative Regulation of Tetrahymena Telomerase Holoenzyme Mol. Cell. Biol., March 15, 2007; 27(6): 2074 - 2083. [Abstract] [Full Text] [PDF]

				M. G. Catlett and K. B. Kaplan Sgt1p Is a Unique Co-chaperone That Acts as a Client Adaptor to Link Hsp90 to Skp1p J. Biol. Chem., November 3, 2006; 281(44): 33739 - 33748. [Abstract] [Full Text] [PDF]

				A. N. Gillis, S. Thomas, S. D. Hansen, and K. B. Kaplan A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis J. Cell Biol., December 5, 2005; 171(5): 773 - 784. [Abstract] [Full Text] [PDF]

				L. B. Lingelbach and K. B. Kaplan The Interaction between Sgt1p and Skp1p Is Regulated by HSP90 Chaperones and Is Required for Proper CBF3 Assembly Mol. Cell. Biol., October 15, 2004; 24(20): 8938 - 8950. [Abstract] [Full Text] [PDF]