Poly(ADP-ribosyl)ation is recognized by ECT2 during mitosis.
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.
Mesh Terms:
Binding Sites, Cytokinesis, HeLa Cells, Humans, Mitosis, Models, Biological, Poly Adenosine Diphosphate Ribose, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins, Spindle Apparatus, Tankyrases, Tubulin
Binding Sites, Cytokinesis, HeLa Cells, Humans, Mitosis, Models, Biological, Poly Adenosine Diphosphate Ribose, Protein Binding, Protein Structure, Tertiary, Proto-Oncogene Proteins, Spindle Apparatus, Tankyrases, Tubulin
Cell Cycle
Date: Dec. 09, 2014
PubMed ID: 25486481
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