PXD003964

PXD003964 is an original dataset announced via ProteomeXchange.

Title	hSSB1 DNA-binding is modulated by dynamic DNA-PK-mediated phosphorylation
Description	The maintenance of genomic stability is essential for cellular viability and the prevention of diseases such as cancer. Human single-stranded DNA binding protein 1 (hSSB1) is a protein with roles in the stabilisation and restart of stalled DNA replication forks, as well as in the repair of oxidative DNA lesions and double-strand DNA breaks. In the later process, phosphorylation of threonine 117 by the ATM kinase is required for hSSB1 stability and proper DNA repair. The regulation of hSSB1 in other DNA repair pathways has however remained unclear. Here we report that hSSB1 may also be directly phosphorylated by DNA-PK at serine residue 134. While this modification does occur in undamaged cells, it is largely suppressed by PPP-family protein phosphatases. Following the disruption of replication forks, S134 phosphorylation is however enhanced and promotes cellular survival. Interestingly, while hSSB1 is known to associate with replication forks following their disruption, we here find that S134 phosphorylation may limit binding to replication fork junctions. Together, these data represent a novel mechanism for hSSB1 regulation following the inhibition of replication.
HostingRepository	PRIDE
AnnounceDate	2018-02-07
AnnouncementXML	Submission_2018-02-07_11:49:37.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Catherine Botting
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	phosphorylated residue; monohydroxylated residue; deamidated residue; iodoacetamide derivatized residue
Instrument	TripleTOF 5600

Revision	Datetime	Status	ChangeLog Entry
0	2016-04-14 01:03:59	ID requested
⏵ 1	2018-02-07 11:49:38	announced

Ashton NW, Paquet N, Shirran SL, Bolderson E, Kariawasam R, Touma C, Fallahbaghery A, Gamsjaeger R, Cubeddu L, Botting C, Pollock PM, O'Byrne KJ, Richard DJ, hSSB1 phosphorylation is dynamically regulated by DNA-PK and PPP-family protein phosphatases. DNA Repair (Amst), 54():30-39(2017) [pubmed]

curator keyword: Biological, Biomedical

submitter keyword: human / hSSB1 / DNA-PK / PPP family phosphatase / replication stress / hydroxyurea / Sciex 5600

Catherine Helen Botting
contact affiliation	Biomedical Sciences Mass Spectrometry and Proteomics Facility, Biomedical Sciences Research Complex, University of St Andrews, St Andrews, Fife, KY16 9ST
contact email	cb2@st-andrews.ac.uk
lab head
Catherine Botting
contact affiliation	Biomedical Science Research Complex
contact email	cb2@st-andrews.ac.uk
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2018/02/PXD003964

PRIDE project URI

• PRIDE
  1. PXD003964
     1. Label: PRIDE project
     2. Name: hSSB1 DNA-binding is modulated by dynamic DNA-PK-mediated phosphorylation