Cell cycle-dependent association of polo kinase Cdc5 with CENP-A contributes to faithful chromosome segregation in budding yeast.
Cell Cycle Proteins
/ metabolism
Centromere
/ metabolism
Centromere Protein A
/ physiology
Chromatin
/ metabolism
Chromosomal Proteins, Non-Histone
/ metabolism
Chromosome Segregation
/ physiology
DNA-Binding Proteins
/ metabolism
Histones
/ metabolism
Kinetochores
/ metabolism
Mitosis
Nuclear Proteins
/ metabolism
Phosphorylation
Protein Serine-Threonine Kinases
/ metabolism
Saccharomyces
/ metabolism
Saccharomyces cerevisiae
/ metabolism
Saccharomyces cerevisiae Proteins
/ metabolism
Saccharomycetales
/ metabolism
Schizosaccharomyces pombe Proteins
/ metabolism
Journal
Molecular biology of the cell
ISSN: 1939-4586
Titre abrégé: Mol Biol Cell
Pays: United States
ID NLM: 9201390
Informations de publication
Date de publication:
01 04 2019
01 04 2019
Historique:
pubmed:
7
2
2019
medline:
1
8
2019
entrez:
7
2
2019
Statut:
ppublish
Résumé
Evolutionarily conserved polo-like kinase, Cdc5 (Plk1 in humans), associates with kinetochores during mitosis; however, the role of cell cycle-dependent centromeric ( CEN) association of Cdc5 and its substrates that exclusively localize to the kinetochore have not been characterized. Here we report that evolutionarily conserved CEN histone H3 variant, Cse4 (CENP-A in humans), is a substrate of Cdc5, and that the cell cycle-regulated association of Cse4 with Cdc5 is required for cell growth. Cdc5 contributes to Cse4 phosphorylation in vivo and interacts with Cse4 in mitotic cells. Mass spectrometry analysis of in vitro kinase assays showed that Cdc5 phosphorylates nine serine residues clustered within the N-terminus of Cse4. Strains with cse4-9SA exhibit increased errors in chromosome segregation, reduced levels of CEN-associated Mif2 and Mcd1/Scc1 when combined with a deletion of MCM21. Moreover, the loss of Cdc5 from the CEN chromatin contributes to defects in kinetochore integrity and reduction in CEN-associated Cse4. The cell cycle-regulated association of Cdc5 with Cse4 is essential for cell viability as constitutive association of Cdc5 with Cse4 at the kinetochore leads to growth defects. In summary, our results have defined a role for Cdc5-mediated Cse4 phosphorylation in faithful chromosome segregation.
Identifiants
pubmed: 30726152
doi: 10.1091/mbc.E18-09-0584
pmc: PMC6589903
doi:
Substances chimiques
Cell Cycle Proteins
0
Centromere Protein A
0
Chromatin
0
Chromosomal Proteins, Non-Histone
0
DNA-Binding Proteins
0
Histones
0
Nuclear Proteins
0
Saccharomyces cerevisiae Proteins
0
Schizosaccharomyces pombe Proteins
0
Plo1 protein, S pombe
EC 2.7.11.1
Protein Serine-Threonine Kinases
EC 2.7.11.1
CDC5 protein, S cerevisiae
EC 2.7.11.21
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Langues
eng
Pagination
1020-1036Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UP_A252_1027
Pays : United Kingdom
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