4.6 Article

Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis

Journal

CELL CYCLE
Volume 13, Issue 18, Pages 2944-2951

Publisher

LANDES BIOSCIENCE
DOI: 10.4161/15384101.2014.947197

Keywords

BRCT domain; ECT2; mitosis; PAR; PAR binding

Categories

Funding

  1. National Institute of Health [CA132755, CA130899]
  2. University of Michigan Cancer Center
  3. GI Peptide Research Center
  4. Era of Hope Scholar Award from Department of Defense

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Poly(ADP-ribosyl)ation is an unique posttranslational modification and required for spindle assembly and function during mitosis. However, the molecular mechanism of poly(ADP-ribose) (PAR) in mitosis remains elusive. Here, we show the evidence that PAR is recognized by ECT2, a key guanine nucleotide exchange factor in mitosis. The BRCT domain of ECT2 directly binds to PAR both in vitro and in vivo. We further found that -tubulin is PARylated during mitosis. PARylation of -tubulin is recognized by ECT2 and recruits ECT2 to mitotic spindle for completing mitosis. Taken together, our study reveals a novel mechanism by which PAR regulates mitosis.

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