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Vol. 18, Issue 10, 3800-3809, October 2007

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A Protein Interaction Map of the Mitotic Spindle

Jonathan Wong^*, Yuko Nakajima^*, Stefan Westermann, Ching Shang^*, Jung-seog Kang, Crystal Goodner, Pantea Houshmand^*, Stanley Fields, Clarence S.M. Chan, David Drubin^*, Georjana Barnes^*, and Tony Hazbun^||

*Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720; Research Institute of Molecular Pathology, 1030 Vienna, Austria; Section of Molecular Genetics and Microbiology and Institute for Cellular and Molecular Biology, The University of Texas, Austin, TX 78712; Howard Hughes Medical Institute, Departments of Genome Sciences and Medicine, University of Washington, Seattle, WA 98195-5065; and ^||Department of Medicinal Chemistry and Molecular Pharmacology, Bindley Bioscience Center and Purdue Cancer Center, Purdue University, West Lafayette, IN 47907

Submitted June 6, 2007; Revised July 2, 2007; Accepted July 6, 2007
Monitoring Editor: Sandra Schmid

The mitotic spindle consists of a complex network of proteins that segregates chromosomes in eukaryotes. To strengthen our understanding of the molecular composition, organization, and regulation of the mitotic spindle, we performed a system-wide two-hybrid screen on 94 proteins implicated in spindle function in Saccharomyces cerevisiae. We report 604 predominantly novel interactions that were detected in multiple screens, involving 303 distinct prey proteins. We uncovered a pattern of extensive interactions between spindle proteins reflecting the intricate organization of the spindle. Furthermore, we observed novel connections between kinetochore complexes and chromatin-modifying proteins and used phosphorylation site mutants of NDC80/TID3 to gain insights into possible phospho-regulation mechanisms. We also present analyses of She1p, a novel spindle protein that interacts with the Dam1 kinetochore/spindle complex. The wealth of protein interactions presented here highlights the extent to which mitotic spindle protein functions and regulation are integrated with each other and with other cellular activities.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Address correspondence to: Georjana Barnes (gbarnes{at}berkeley.edu)

Abbreviations used: AD, activation domain; DBD, DNA-binding domain; MAP, microtubule-associated protein.

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