Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 103, Issue 16, Pages 6196-6201Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0506926103
Keywords
Cdk phosphorylation; mitosis / cytokinesis; microtubule-associated proteins; microtubule bundling
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Funding
- NCI NIH HHS [2T32CA77109-06A2, T32 CA077109] Funding Source: Medline
- NIGMS NIH HHS [R01 GM067859, GM67859] Funding Source: Medline
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We have examined the role of PRC1, a micizone-associated, microtubule bundling, Cdk substrate protein, in regulating the spatio-temporal formation of the midzone in HeLa cells. Cdk-mediated phosphorylation of PRC1 in early mitosis holds PRC1 in an inactive monomeric state. During the metaphase-to-anaphase transition, PRC1 is dephosphorylated, promoting PRC1 oligomerization. Using time-lapse video microscopy, RNA interference, 3D immunofluorescence reconstruction imaging, and rescue experiments, we demonstrate that the dephosphorylated form of PRC1 is essential for bundling antiparallel, nonkinetochore, interdigitating microtubules to establish the midzone that is necessary for cytokinesis. Our results thus indicate that PRC1 is an essential factor in controlling the spatio-temporal formation of the midzone in human cells.
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