Journal
CELL CYCLE
Volume 13, Issue 18, Pages 2944-2951Publisher
LANDES BIOSCIENCE
DOI: 10.4161/15384101.2014.947197
Keywords
BRCT domain; ECT2; mitosis; PAR; PAR binding
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Funding
- National Institute of Health [CA132755, CA130899]
- University of Michigan Cancer Center
- GI Peptide Research Center
- 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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