Role of ubiquitin-protein ligase UBR5 in the disassembly of mitotic checkpoint complexes | Zendy

Sharon Kaisari | Zendy; Shirly Miniowitz-Shemtov | Zendy; Danielle Sitry-Shevah | Zendy; Pnina Shomer | Zendy; Guennadi Kozlov | Zendy; Kalle Gehring | Zendy; Avram Hershko | Zendy

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Role of ubiquitin-protein ligase UBR5 in the disassembly of mitotic checkpoint complexes

Author(s) -

Sharon Kaisari,

Shirly Miniowitz-Shemtov,

Danielle Sitry-Shevah,

Pnina Shomer,

Guennadi Kozlov,

Kalle Gehring,

Avram Hershko

Publication year - 2022

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.2121478119

Subject(s) - anaphase promoting complex , microbiology and biotechnology , spindle checkpoint , mad2 , mitosis , mitotic exit , biology , ubiquitin ligase , cdc20 , anaphase , cell cycle checkpoint , securin , chemistry , ubiquitin , spindle apparatus , cell cycle , biochemistry , cell division , cell , gene

Significance The mitotic checkpoint system is essential for the prevention of mistakes in the segregation of chromosomes in mitosis. As long as chromosomes are not attached correctly to the mitotic spindle, a mitotic checkpoint complex (MCC) is assembled and inhibits the action of ubiquitin ligase APC/C (anaphase-promoting complex/cyclosome) to initiate anaphase. When the checkpoint is turned off, MCC is disassembled, allowing anaphase initiation. The mechanisms of MCC disassembly have been studied, but the regulation of this process remained obscure. We found that a second ubiquitin ligase, UBR5 (ubiquitin-protein ligaseN -recognin 5), ubiquitylates MCC components and stimulates the disassembly of MCC from APC/C, as well as the dissociation of a subcomplex of MCC.

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