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Liao H , Winkfein RJ , Mack G , Rattner JB , Yen TJ
Cenp-F Is a Protein of the Nuclear Matrix That Assembles onto Kinetochores at Late G2 and Is Rapidly Degraded after Mitosis
Journal of Cell Biology. 1995 Aug;130(3) :507-518
PMID: ISI:A1995RL49600002   
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Abstract
Centromere protein-F (CENP-F) is a mammalian kinetochore protein that was recently identified by an autoimmune serum (Rattner, J. B., A. Rao, M. J. Fritzler, D. W. Valencia, and T. J. Yen. Cell Motil. Cytoskeleton. 26:214-226). We report here the human cDNA sequence of CENP-F, along with its expression and localization patterns at different stages of the HeLa cell cycle. CENP-F is a protein of the nuclear matrix that gradually accumulates during the cell cycle until it reaches peak levels in G2 and M phase cells and is rapidly degraded upon completion of mitosis. CENP-F is first detected at the prekinetochore complex during late G2, and is clearly detectable as paired foci that correspond to all the centromeres by prophase. During mitosis, CENP-F is associated with kinetochores from prometaphase until early anaphase and is then detected at the spindle midzone throughout the remainder of anaphase. By telophase, CENP-F is concentrated within the intracellular bridge at either side of the mid-body. The predicted structure of the 367-kD CENP-F protein consists of two 1,600-amino acid- long coil domains that flank a central flexible core, A putative P-loop nucleotide binding site (ADIPTGKT) is located within the globular carboxy terminus, The structural features deduced from our sequence studies and the spatial and temperal distribution of CENP-F revealed in our cytological and biochemical studies suggest that it may play a role in several mitotic events.
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Times Cited: 99 Article RL496 J CELL BIOL