PXD013782 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphoproteomics of DNA repair in Saccharomyces cerevisisae |
Description | The role of Rad53 in response to a DNA lesion is central for the accurate orchestration of the DNA damage response. Rad53 activation relies on its phosphorylation by the Mec1 kinase and its own autophosphorylation in a manner dependent on the adaptor Rad9. While the mechanism behind Rad53 phosphorylation and activation has been well documented, less is known about the processes that counteract its kinase activity during the response to a DNA break. Here, we describe that PP4 dephosphorylates Rad53 during the repair of a DNA lesion, a process that affects the phosphorylation status of multiple factors involved in the DNA damage response. PP4-dependent Rad53 dephosphorylation stimulates DNA end resection in a process that relies mainly on Sgs1/Dna2. Consequently, elimination of PP4 activity affects DNA resection and repair by single-strand annealing, defects that are bypassed by reducing the hyper-phosphorylation state of Rad53 observed in the absence of the phosphatase. These results confirms that Rad53 is one of the principal targets of PP4 during the repair of a DNA lesion and demonstrate that the attenuation of its kinase activity during the initial steps of the repair process is essential to efficiently enhance recombinational repair pathways that depend on long-range resection for its execution. |
HostingRepository | PRIDE |
AnnounceDate | 2019-09-12 |
AnnouncementXML | Submission_2019-10-25_05:10:53.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Holger Kramer |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | phosphorylated residue; monohydroxylated residue; N-acetylated residue; iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap Velos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-05-09 01:47:42 | ID requested | |
1 | 2019-09-12 05:29:13 | announced | |
⏵ 2 | 2019-10-25 05:10:55 | announced | 2019-10-25: Updated publication reference for PubMed record(s): 31544936. |
3 | 2024-10-22 04:15:26 | announced | 2024-10-22: Updated project metadata. |
Publication List
Villoria MT, Guti, é, rrez-Escribano P, Alonso-Rodr, í, guez E, Ramos F, Merino E, Campos A, Montoya A, Kramer H, Arag, ó, n L, Clemente-Blanco A, PP4 phosphatase cooperates in recombinational DNA repair by enhancing double-strand break end resection. Nucleic Acids Res, 47(20):10706-10727(2019) [pubmed] |
Keyword List
submitter keyword: DNA repair/Double-strand break |
Homologous recombination |
PP4 |
resection |
phosphoproteomics |
Contact List
Andrés Clemente Blanco |
contact affiliation | Cell Cycle and Genome Stability Group. Institute of Functional Biology and Genomics (IBFG). Spanish National Research Council (CSIC). University of Salamanca (USAL). C/ Zacarías González 2. Salamanca 37007. SPAIN |
contact email | andresclemente@usal.es |
lab head | |
Holger Kramer |
contact affiliation | MRC London Institute of Medical Sciences |
contact email | h.kramer@lms.mrc.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD013782
- Label: PRIDE project
- Name: Phosphoproteomics of DNA repair in Saccharomyces cerevisisae