PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression

J Cell Sci. 2003 Apr 15;116(Pt 8):1551-62. doi: 10.1242/jcs.00341.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • CHO Cells
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Division / drug effects
  • Cell Line
  • Cell Survival / drug effects
  • Cell Survival / genetics
  • Centrioles / metabolism*
  • Cricetinae
  • G1 Phase / drug effects
  • HeLa Cells
  • Humans
  • Hydroxyurea / pharmacology
  • In Situ Hybridization, Fluorescence / methods
  • Mice
  • Molecular Sequence Data
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Poly(ADP-ribose) Polymerases / genetics
  • Poly(ADP-ribose) Polymerases / metabolism*
  • S Phase / drug effects
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Cell Cycle Proteins
  • Poly(ADP-ribose) Polymerase Inhibitors
  • PARP3 protein, human
  • Poly(ADP-ribose) Polymerases
  • Hydroxyurea

Associated data

  • GENBANK/AY126341