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Papers In Press, published online ahead of print December 29, 2003
J. Biol. Chem, 10.1074/jbc.M310224200
Submitted on September 15, 2003
Revised on December 29, 2003
Accepted on December 29, 2003
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9041
Corresponding Author: hongtao.yu{at}utsouthwestern.edu
Proper kinetochore function is essential for the accurate segregation of chromosomes during mitosis. Kinetochores provide the attachment sites for spindle microtubules and are required for the alignment of chromosomes at the metaphase plate (chromosome congression). Components of the conserved Ndc80 complex are required for chromosome congression and their disruption results in mitotic arrest accompanied by multiple spindle aberrations. To better understand the function of the Ndc80 complex, we have identified two novel subunits of the human Ndc80 complex, termed human Spc25 (hSpc25) and human Spc24 (hSpc24), using an immuno-affinity approach. Human Spc25 interacts with Ndc80 throughout the cell cycle and localizes to kinetochores during mitosis. RNAi-mediated depletion of hSpc25 in HeLa cells causes aberrant mitosis followed by cell death, a phenotype similar to that of cells depleted for Hec1. Loss of hSpc25 also causes multiple spindle aberrations, including elongated, multipolar, and fractured spindles. In the absence of hSpc25, Mad1 and Hec1 fail to localize to kinetochores during mitosis whereas the kinetochore localization of Bub1 and BubR1 is largely unaffected. Interestingly, the kinetochore localization of Mad1 in cells with a compromised Ndc80 function is restored upon microtubule depolymerization. Thus, hSpc25 is an essential kinetochore component that plays a significant role in proper execution of mitotic events.
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