Literature DB >> 16212557

Regulation of mitosis by poly(ADP-ribosyl)ation.

Duane A Compton1.   

Abstract

The spindle is a dynamic, microtubule-based structure responsible for chromosome segregation during cell division. Spindles in mammalian cells contain several thousand microtubules that are arranged into highly symmetric bipolar arrays by the actions of numerous microtubule-associated motor and non-motor proteins. In addition to these protein constituents, recent work has demonstrated that poly(ADP-ribose) is a key spindle component. Of the multitude of poly(ADP-ribose) polymerase proteins encoded in the genome, tankyrase 1 appears to be the primary enzyme responsible for building poly(ADP-ribose) in spindles during mitosis. In this issue of the Biochemical Journal, Susan Smith and co-workers show that the primary target of tankyrase 1 in dividing cells is NuMA (nuclear mitotic apparatus protein), a protein that cross-links microtubule ends at spindle poles. The impact of poly(ADP-ribosyl)ation on the biochemical function of NuMA remains murky at this time, but these new results represent the first step to clearing the view as to how poly(ADP-ribosyl)ation regulates cell division.

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Year:  2005        PMID: 16212557      PMCID: PMC1276945          DOI: 10.1042/BJ20051437

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  14 in total

Review 1.  Spindle assembly in animal cells.

Authors:  D A Compton
Journal:  Annu Rev Biochem       Date:  2000       Impact factor: 23.643

Review 2.  Cell and molecular biology of spindle poles and NuMA.

Authors:  Xavier Fant; Andreas Merdes; Laurence Haren
Journal:  Int Rev Cytol       Date:  2004

3.  Resolution of sister telomere association is required for progression through mitosis.

Authors:  Jasmin N Dynek; Susan Smith
Journal:  Science       Date:  2004-04-02       Impact factor: 47.728

Review 4.  The world according to PARP.

Authors:  S Smith
Journal:  Trends Biochem Sci       Date:  2001-03       Impact factor: 13.807

5.  Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function.

Authors:  Paul Chang; Margaret Coughlin; Timothy J Mitchison
Journal:  Nat Cell Biol       Date:  2005-11       Impact factor: 28.824

6.  Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated.

Authors:  Alka Saxena; Richard Saffery; Lee H Wong; Paul Kalitsis; K H Andy Choo
Journal:  J Biol Chem       Date:  2002-05-13       Impact factor: 5.157

7.  Tankyrase promotes telomere elongation in human cells.

Authors:  S Smith; T de Lange
Journal:  Curr Biol       Date:  2000-10-19       Impact factor: 10.834

8.  Tankyrase, a poly(ADP-ribose) polymerase at human telomeres.

Authors:  S Smith; I Giriat; A Schmitt; T de Lange
Journal:  Science       Date:  1998-11-20       Impact factor: 47.728

9.  Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner.

Authors:  Juan I Sbodio; Nai-Wen Chi
Journal:  J Biol Chem       Date:  2002-06-21       Impact factor: 5.157

10.  Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes.

Authors:  S Smith; T de Lange
Journal:  J Cell Sci       Date:  1999-11       Impact factor: 5.285

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  3 in total

1.  Rae1 interaction with NuMA is required for bipolar spindle formation.

Authors:  Richard W Wong; Günter Blobel; Elias Coutavas
Journal:  Proc Natl Acad Sci U S A       Date:  2006-12-15       Impact factor: 11.205

2.  Tankyrase-1 function at telomeres and during mitosis is regulated by Polo-like kinase-1-mediated phosphorylation.

Authors:  G-H Ha; H-S Kim; H Go; H Lee; H Seimiya; D H Chung; C-W Lee
Journal:  Cell Death Differ       Date:  2011-08-05       Impact factor: 15.828

3.  The Poly(ADP-ribose) polymerase PARP-1 is required for oxidative stress-induced TRPM2 activation in lymphocytes.

Authors:  Ben Buelow; Yumei Song; Andrew M Scharenberg
Journal:  J Biol Chem       Date:  2008-07-03       Impact factor: 5.157

  3 in total

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