Document Detail

PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression.
MedLine Citation:
PMID:  12640039     Owner:  NLM     Status:  MEDLINE    
A novel member of the poly(ADP-ribose) polymerase (PARP) family, hPARP-3, is identified here as a core component of the centrosome. hPARP-3 is preferentially localized to the daughter centriole throughout the cell cycle. The N-terminal domain (54 amino acids) of hPARP-3 is responsible for its centrosomal localization. Full-length hPAPR-3 (540 amino acids, with an apparent mass of 67 kDa) synthesizes ADP-ribose polymers during its automodification. Overexpression of hPARP-3 or its N-terminal domain does not influence centrosomal duplication or amplification but interferes with the G1/S cell cycle progression. PARP-1 also resides for part of the cell cycle in the centrosome and interacts with hPARP-3. The presence of both PARP-1 and PARP-3 at the centrosome may link the DNA damage surveillance network to the mitotic fidelity checkpoint.
Angélique Augustin; Catherine Spenlehauer; Hélène Dumond; Josiane Ménissier-De Murcia; Matthieu Piel; Anne-Catherine Schmit; Françoise Apiou; Jean-Luc Vonesch; Michael Kock; Michel Bornens; Gilbert De Murcia
Related Documents :
19034829 - Maillard reaction involved in the steaming process of the root of polygonum multiflorum.
12269 - The granulation of binary mixtures: the effects of the properties of the component powd...
18468889 - Solubilization of morocco phosphorite by aspergillus niger.
8115279 - Isocitric and citric acid in human prostatic and seminal fluid: implications for prosta...
20333539 - Fabrication of calcium phosphate-calcium sulfate injectable bone substitute using hydro...
6820329 - Production of kojic acid by resuspended mycelia of aspergillus flavus.
2829239 - Fatty acid modification of cultured neuroblastoma cells by gamma linolenic acid relevan...
15884659 - Enterobacterial responses to external protons, including responses that involve early w...
5472179 - The synthesis of bile acids in perfused rat liver subjected to chronic biliary drainage.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of cell science     Volume:  116     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2003 Apr 
Date Detail:
Created Date:  2003-03-17     Completed Date:  2004-01-30     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1551-62     Citation Subset:  IM    
Unité 9003 du CNRS, Ecole Supérieure de Biotechnologie de Strasbourg, Boulevard Sébastien Brant, 67400 Illkirch, France.
Data Bank Information
Bank Name/Acc. No.:
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
3T3 Cells
Amino Acid Sequence
Base Sequence
CHO Cells
Cell Cycle Proteins / genetics,  metabolism*
Cell Division / drug effects
Cell Line
Cell Survival / drug effects,  genetics
Centrioles / metabolism*
G1 Phase / drug effects
Hela Cells
Hydroxyurea / pharmacology
In Situ Hybridization, Fluorescence / methods
Molecular Sequence Data
Poly(ADP-ribose) Polymerases / antagonists & inhibitors,  genetics,  metabolism*
S Phase / drug effects
Sequence Alignment
Sequence Homology, Amino Acid
Reg. No./Substance:
0/Cell Cycle Proteins; 127-07-1/Hydroxyurea; EC protein, human; EC Polymerases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Expression in Xenopus oocytes shows that WT1 binds transcripts in vivo, with a central role for zinc...
Next Document:  Genome-wide expression screens indicate a global role for protein kinase CK2 in chromatin remodeling...