RT Journal Article
SR Electronic
T1 SUMOylation targets shugoshin to stabilize sister kinetochore biorientation
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 840157
DO 10.1101/840157
A1 Xue Bessie Su
A1 Menglu Wang
A1 Claudia Schaffner
A1 Dean Clift
A1 Olga O. Nerusheva
A1 Triin Tammasalu
A1 Andreas Wallek
A1 Yehui Wu
A1 David A. Kelly
A1 A. Arockia Jeyaprakash
A1 Zuzana Storchova
A1 Ronald Hay
A1 Adèle L. Marston
YR 2019
UL http://biorxiv.org/content/early/2019/11/13/840157.abstract
AB The accurate segregation of chromosomes during mitosis relies on the attachment of sister chromatids to microtubules from opposite poles, called biorientation. Sister chromatid cohesion resists microtubule forces, generating tension which provides the signal that biorientation has occurred. How tension silences the surveillance pathways that prevent cell cycle progression and correct erroneous kinetochore-microtubule remains unclear. Here we identify SUMOylation as a mechanism that promotes anaphase onset upon biorientation. SUMO ligases modify the tension-sensing pericentromere-localized chromatin protein, shugoshin, to stabilize bioriented sister kinetochore-microtubule attachments. In the absence of SUMOylation, Aurora B kinase removal from kinetochores is delayed. Shugoshin SUMOylation prevents its binding to protein phosphatase 2A (PP2A) and release of this interaction is important for stabilizing sister kinetochore biorientation. We propose that SUMOylation modulates the kinase-phosphatase balance within pericentromeres to inactivate the error correction machinery, thereby allowing anaphase entry in response to biorientation.