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RXXPEG motif of MERIT40 is required to maintain spindle structure and function through its interaction with Tankyrase1
Author(s) -
Zheng Duo,
Xie Wangqing,
Li Li,
Jiang Wenqi,
Zou Yongdong,
Chiang Chengyao,
Shao Genze,
Yan Kaowen
Publication year - 2019
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.11086
Subject(s) - microbiology and biotechnology , motif (music) , deubiquitinating enzyme , mutant , mitosis , chemistry , biology , genetics , gene , physics , ubiquitin , acoustics
Deubiquitinase BRISC complex plays important role in the maintenance of spindle structure and function; however, the underlying mechanism remains largely undefined. Here we demonstrated that MERIT40, a core component of BRISC complex, directly interacts with the RXXPEG motif in the ARC‐V domain of Tankyrase1(TNKS1). Mutation of the RXXPEG motif in the MERIT40 (R28A) disrupted its interaction with TNKS1. Consistent with these data, R28A mutant cells displayed multiple mitotic defects including aberrant spindle assembly and chromosome misalignment. These results support a critical role of RXXPEG motif of MERIT40 in BRISC‐mediated regulation of TNKS1 function during spindle assembly.