Proteomics

Dataset Information

0

CENP-C-targeted PLK-1 regulates kinetochore function in C. elegans embryos


ABSTRACT: This project focused on the identification of phosphorylation sites on the C. elegans inner kinetochore protein CENP-C and the outer kinetochore complex MIS12. Phosphorylation was carried out in vitro using recombinant proteins. CENP-C was phosphorylated with Cdk1, PLK-1 or both; MIS12 complex components phosphorylation was performed using PLK-1.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Caenorhabditis Elegans

SUBMITTER: Douglas Lamont  

LAB HEAD: Dr Fede Pelisch

PROVIDER: PXD058379 | Pride | 2024-11-28

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
134_2024_DUN_FP-A.raw Raw
134_2024_DUN_FP-B.raw Raw
134_2024_DUN_FP-C.raw Raw
134_2024_DUN_FP-D.raw Raw
177_2024-FP-F.raw Raw
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Publications

CENP-C-targeted PLK-1 regulates kinetochore function in C. elegans embryos.

Bel Borja Laura L   Taylor Samuel J P SJP   Soubigou Flavie F   Pelisch Federico F  

Journal of cell science 20241128 22


Polo-like kinase 1 (PLK-1) is present in centrosomes, the nuclear envelope and kinetochores and plays a significant role in meiosis and mitosis. PLK-1 depletion or inhibition has severe consequences for spindle assembly, spindle assembly checkpoint (SAC) activation, chromosome segregation and cytokinesis. BUB-1 targets PLK-1 to the outer kinetochore and, in mammals, the inner kinetochore PLK1 targeting is mediated by the constitutive centromere associated network (CCAN). BUB-1-targeted PLK-1 pla  ...[more]

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