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Journal Article | Research Support, Non-U.S. Gov't | Research Support, U.S. Gov't, P.H.S.

Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression.

X Zhu, M A Mancini, K H Chang, C Y Liu, C F Chen, B Shan, D Jones, T L Yang-Feng, W H Lee
X Zhu
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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M A Mancini
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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K H Chang
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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C Y Liu
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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C F Chen
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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B Shan
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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D Jones
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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T L Yang-Feng
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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W H Lee
Center for Molecular Medicine, University of Texas Health Science Center at San Antonio 78245, USA.
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DOI: 10.1128/MCB.15.9.5017
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ABSTRACT

A gene assigned to human chromosome 1q32-41 encodes a novel protein of 3,113 amino acids containing an internal tandem repeat of 177 amino acids. The protein, which we have named "mitosin," was identified by direct binding to purified retinoblastoma protein in vitro with a region distantly related to the retinoblastoma protein-binding site of E2F-1. Mitosin is expressed throughout S, G2, and M phases of the cell cycle but is absent in G1. Its localization is dramatically reorganized from a rather homogeneous nuclear distribution in S phase to paired dots at the kinetochore/centromere region, to the spindle apparatus, and then to the midbody during M-phase progression. This spatial reorganization coincides closely with the temporal phosphorylation patterns of mitosin. Overexpression of N-terminally truncated mutants blocks cell cycle progression mainly at G2/M. These results suggest that mitosin may play an important role in mitotic-phase progression.

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Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression.
X Zhu, M A Mancini, K H Chang, C Y Liu, C F Chen, B Shan, D Jones, T L Yang-Feng, W H Lee
Molecular and Cellular Biology Sep 1995, 15 (9) 5017-5029; DOI: 10.1128/MCB.15.9.5017

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Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression.
X Zhu, M A Mancini, K H Chang, C Y Liu, C F Chen, B Shan, D Jones, T L Yang-Feng, W H Lee
Molecular and Cellular Biology Sep 1995, 15 (9) 5017-5029; DOI: 10.1128/MCB.15.9.5017
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