Kinetochore-bound Mps1 regulates kinetochore-microtubule attachments via Ndc80 phosphorylation.
Adenosine Triphosphate
/ metabolism
Kinetochores
/ chemistry
M Phase Cell Cycle Checkpoints
Microtubules
/ metabolism
Nuclear Proteins
/ chemistry
Phosphorylation
Protein Binding
Protein Serine-Threonine Kinases
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ chemistry
Signal Transduction
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
06 12 2021
06 12 2021
Historique:
received:
24
06
2021
revised:
03
08
2021
accepted:
09
09
2021
entrez:
14
10
2021
pubmed:
15
10
2021
medline:
24
12
2021
Statut:
ppublish
Résumé
Dividing cells detect and correct erroneous kinetochore-microtubule attachments during mitosis, thereby avoiding chromosome missegregation. The Aurora B kinase phosphorylates microtubule-binding elements specifically at incorrectly attached kinetochores, promoting their release and providing another chance for proper attachments to form. However, growing evidence suggests that the Mps1 kinase is also required for error correction. Here we directly examine how Mps1 activity affects kinetochore-microtubule attachments using a reconstitution-based approach that allows us to separate its effects from Aurora B activity. When endogenous Mps1 that copurifies with kinetochores is activated in vitro, it weakens their attachments to microtubules via phosphorylation of Ndc80, a major microtubule-binding protein. This phosphorylation contributes to error correction because phospho-deficient Ndc80 mutants exhibit genetic interactions and segregation defects when combined with mutants in other error correction pathways. In addition, Mps1 phosphorylation of Ndc80 is stimulated on kinetochores lacking tension. These data suggest that Mps1 provides an additional mechanism for correcting erroneous kinetochore-microtubule attachments, complementing the well-known activity of Aurora B.
Identifiants
pubmed: 34647959
pii: 212702
doi: 10.1083/jcb.202106130
pmc: PMC8641409
pii:
doi:
Substances chimiques
NDC80 protein, S cerevisiae
0
Nuclear Proteins
0
Saccharomyces cerevisiae Proteins
0
Adenosine Triphosphate
8L70Q75FXE
Protein Serine-Threonine Kinases
EC 2.7.11.1
MPS1 protein, S cerevisiae
EC 2.7.12.2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : P01 GM105537
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA015704
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM079373
Pays : United States
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM064386
Pays : United States
Organisme : NIH HHS
ID : R01GM079373
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134842
Pays : United States
Informations de copyright
© 2021 Sarangapani et al.
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