Open AccessRole 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 of the united states of america
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) - ubiquitin ligase , microbiology and biotechnology , ubiquitin , mitosis , ubiquitin protein ligases , biology , chemistry , biochemistry , 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.