Proteomics

Dataset Information

0

CK1 promotes double-strand break repair in fission yeast


ABSTRACT: CK1 enzymes are conserved, acidophilic serine/threonine kinases with a variety of critical cellular functions; their misregulation contributes to cancer, neurodegenerative diseases, and sleep phase disorders. The C-termini of these enzymes are thought to inhibit kinase activity by acting as pseudosubstrates. We were interested in identifying substrates of the fission yeast CK1 homologues Hhp1 and Hhp2, particularly substrates involved in DNA repair. We used quantitative phosphoproteomics to identify potential substrates of Hhp1 and Hhp2 in Schizosaccharomyces pombe and to compare between the full-length and C-terminally truncated forms.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Schizosaccharomyces Pombe

SUBMITTER: Jose Navarrete Perea  

LAB HEAD: Kathleen L. Gould, Ph.D.

PROVIDER: PXD033223 | Pride | 2025-05-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
CullatiS_GoudLab_Peptide.tsv Tabular
CullatiS_GoudLab_Phospho.csv Csv
CullatiS_GouldLab_Protein.tsv Tabular
Reporter_Ion_sample_order.xlsx Xlsx
checksum.txt Txt
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Publications

The DNA Damage Repair Function of Fission Yeast CK1 Involves Targeting Arp8, a Subunit of the INO80 Chromatin Remodeling Complex.

Cullati Sierra N SN   Akizuki Kazutoshi K   Shan Yufan Y   Zhang Eric E   Ren Liping L   Guillen Rodrigo X RX   Turner Lesley A LA   Chen Jun-Song JS   Navarrete-Perea Jose J   Elmore Zachary C ZC   Gygi Steven P SP   Gould Kathleen L KL  

Molecular and cellular biology 20241010 12


The CK1 family are conserved serine/threonine kinases with numerous substrates and cellular functions. The fission yeast CK1 orthologues Hhp1 and Hhp2 were first characterized as regulators of DNA repair, but the mechanism(s) by which CK1 activity promotes DNA repair had not been investigated. Here, we found that deleting Hhp1 and Hhp2 or inhibiting CK1 catalytic activities in yeast or in human cells increased double-strand breaks (DSBs). The primary pathways to repair DSBs, homologous recombina  ...[more]

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