PXD012695-1
PXD012695 is an original dataset announced via ProteomeXchange.
Dataset Summary
Title | A consensus binding motif for the PP4 protein phosphatase reveals its role as a regulator of cohesin release |
Description | Regulation of protein activities through phosphorylation is a fundamental regulatory mechanism in all organisms. Phosphoprotein phosphatase 4 (PP4) is a conserved and essential enzyme that dephosphorylates serine and threonine residues in substrates. Despite the importance of PP4 general principles of substrate selection are unknown hampering the study of signal regulation by this phosphatase. Here we identify and characterize a general PP4 consensus binding motif, the FxxP motif, that binds to the EVH1 domain of the PP4R3 subunit of the trimeric holoenzyme. We find that the FxxP motif is present in multiple PP4 interacting proteins and that PP4 binding to the FxxP motif can be negatively regulated by phosphorylation hereby providing a mechanism for feeding kinase information into the motif. We identify an uncharacterized FxxP motif in the cohesin release factor WAPL and show that direct binding between WAPL and PP4 is required for cohesin release. Collectively our work uncovers basic principles of PP4 specificity with broad implications for understanding phoshorylation-mediated signaling in cells. |
HostingRepository | MassIVE |
AnnounceDate | 2019-09-23 |
AnnouncementXML | Submission_2020-03-25_09:21:30.xml |
DigitalObjectIdentifier | |
ReviewLevel | Non peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Supported dataset by repository |
PrimarySubmitter | Mark Adamo |
SpeciesList | scientific name: Homo sapiens; common name: human; NCBI TaxID: 9606; |
ModificationList | Oxidation; Carbamidomethyl |
Instrument | Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
---|---|---|---|
0 | 2019-02-13 15:47:28 | ID requested | |
⏵ 1 | 2020-03-25 09:21:31 | announced |
Publication List
no publication |
Keyword List
submitter keyword: PP4, cohesin, phosphatase, EVH1, PP4R3, WAPL, phosphorylation |
Contact List
Arminja Kettenbach | |
---|---|
contact affiliation | The Geisel School of Medicine at Dartmouth |
contact email | arminja.n.kettenbach@dartmouth.edu |
lab head | |
Mark Adamo | |
contact affiliation | Dartmouth College |
contact email | mark.e.adamo@dartmouth.edu |
dataset submitter |
Full Dataset Link List
MassIVE dataset URI |
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://massive.ucsd.edu/MSV000083438/ |