The AAA+ ATPase TRIP13 remodels HORMA domains through N-terminal engagement and unfolding.
Ye, Qiaozhen; Kim, Dong Hyun; Dereli, Ihsan; Rosenberg, Scott C; Hagemann, Goetz; Herzog, Franz; Tóth, Attila; Cleveland, Don W; Corbett, Kevin D.
; 36(16): 2419-2434, 2017 08 15.
Artigo em Inglês | MEDLINE | ID: mdl-28659378
Mode of interaction of TRIP13 AAA-ATPase with the Mad2-binding protein p31comet and with mitotic checkpoint complexes.
Securin-independent regulation of separase by checkpoint-induced shugoshin-MAD2.
Mechanism for remodelling of the cell cycle checkpoint protein MAD2 by the ATPase TRIP13.
Thyroid hormone receptor interacting protein 13 (TRIP13) AAA-ATPase is a novel mitotic checkpoint-silencing protein.
Role of CCT chaperonin in the disassembly of mitotic checkpoint complexes.
Disassembly of mitotic checkpoint complexes by the joint action of the AAA-ATPase TRIP13 and p31(comet).
Nuclear pores set the speed limit for mitosis.
Insights into the mechanism and regulation of the CbbQO-type Rubisco activase, a MoxR AAA+ ATPase.
Nuclear pores protect genome integrity by assembling a premitotic and Mad1-dependent anaphase inhibitor.
Mechanochemical removal of ribosome biogenesis factors from nascent 60S ribosomal subunits.