NDLI: SUMOylation regulates polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis.

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SUMOylation regulates polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis.

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SUMOylation regulates polo-like kinase 1-interacting checkpoint helicase (PICH) during mitosis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sridharan, Vinidhra Ryu, Hyunju Park, Hyewon Azuma, Yoshiaki
Description	Author Affiliation: Sridharan V ( From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.); Park H ( From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.); Ryu H ( From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.); Azuma Y ( From the Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045 azumay@ku.edu.)
Abstract	Mitotic SUMOylation has an essential role in faithful chromosome segregation in eukaryotes, although its molecular consequences are not yet fully understood. In Xenopus egg extract assays, we showed that poly(ADP-ribose) polymerase 1 (PARP1) is modified by SUMO2/3 at mitotic centromeres and that its enzymatic activity could be regulated by SUMOylation. To determine the molecular consequence of mitotic SUMOylation, we analyzed SUMOylated PARP1-specific binding proteins. We identified Polo-like kinase 1-interacting checkpoint helicase (PICH) as an interaction partner of SUMOylated PARP1 in Xenopus egg extract. Interestingly, PICH also bound to SUMOylated topoisomerase II (TopoII ), a major centromeric small ubiquitin-like modifier (SUMO) substrate. Purified recombinant human PICH interacted with SUMOylated substrates, indicating that PICH directly interacts with SUMO, and this interaction is conserved among species. Further analysis of mitotic chromosomes revealed that PICH localized to the centromere independent of mitotic SUMOylation. Additionally, we found that PICH is modified by SUMO2/3 on mitotic chromosomes and in vitro. PICH SUMOylation is highly dependent on protein inhibitor of activated STAT, PIASy, consistent with other mitotic chromosomal SUMO substrates. Finally, the SUMOylation of PICH significantly reduced its DNA binding capability, indicating that SUMOylation might regulate its DNA-dependent ATPase activity. Collectively, our findings suggest a novel SUMO-mediated regulation of the function of PICH at mitotic centromeres.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	6
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-02-06
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA Helicases Metabolism Mitosis Sumoylation Animals Antigens, Neoplasm Centromere DNA Topoisomerases, Type II DNA-Binding Proteins Poly(ADP-ribose) Polymerases Protein Binding Protein Inhibitors Of Activated STAT Protein Transport Small Ubiquitin-Related Modifier Proteins Ubiquitins Xenopus Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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