Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization.

Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Research Abstract Details 

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Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Abstract Text:

Chuanhai Fu,Feng Yan,Fang Wu,Quan Wu,Joseph Whittaker,Haiying Hu,Renming Hu,Xuebiao Yao,

During cell division, chromosome segregation is orchestrated by the interaction of spindle microtubules with the centromere. A dramatic remodeling of interpolar microtubules into an organized central spindle between the separating chromatids is required for the initiation and execution of cytokinesis. Central spindle organization requires mitotic kinesins, the chromosomal passenger protein complex, and microtubule bundling protein PRC1. PRC1 is phosphorylated by Cdc2 at Thr470 and Thr481 during mitosis. However, the functional relevance of PRC1 phosphorylation at Thr470 has remained elusive. Here we show that expression of the non-phosphorylatable mutant PRC1(T470A) but not the phospho-mimicking mutant PRC1(T470E) causes aberrant organization of the central spindle. Immunoprecipitation experiment indicates that both PRC1(T470A) and PRC1(T470E) mutant proteins associate with wild-type PRC1, suggesting that phosphorylation of Thr470 does not alter PRC1 self-association. In addition, in vitro co-sedimentation experiment showed that PRC1 binds to microtubule independent of the phosphorylation state of Thr470. Gel-filtration experiment suggested that phosphorylation of Thr470 promotes oligomerization of PRC1. Given the fact that prevention of the Thr470 phosphorylation inhibits PRC1 oligomerization in vitro and causes an aberrant organization of central spindle in vivo, we propose that this phosphorylation-dependent PRC1 oligomerization ensures that central spindle assembly occurs at the appropriate time in the cell cycle.

Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Publishing Authors By Initials

C Fu,F Yan,F Wu,Q Wu,J Whittaker,H Hu,R Hu,X Yao,

For similar amino acids, peptides, and proteins: amino acids: amino acids, essential: threonine research abstracts see: amino acids, peptides, and proteins: amino acids: amino acids, essential: threonine research

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Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Cell research

VOLUME: 17

Page Numbers: 449-57

Journal Abbreviation: Cell Res.

ISSN: 1748-7838

DAY: 3

MONTH: May

YEAR: 2007

Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9425763

Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Keywords Mesh Terms:

KEYWORDS: Threonine

MESH TERMS: metabolism

Chemical & Substance for Abstract: Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization. Information

Substance Name: Threonine

Registry Number: 72-19-5

Grant and Affiliation Information for Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization and proper central spindle organization.

AFFILIATION: Laboratory of Cellular Dynamics, Hefei National Laboratory and the University of Science and Technology of China, Hefei 230027, China.

Country: China

AGENCY: United States NINDS

GRANT: NS36194

ACRONYM: NS

MEDLINETA: Cell Res

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