PXD028612
PXD028612 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | PP2A/B55a substrate recruitment as defined by the retinoblastoma-related protein p107 |
| Description | Protein phosphorylation is a reversible post-translation modification essential in cell signaling. This study addresses a long-standing question as to how the most abundant serine/threonine Protein Phosphatase 2 (PP2A) holoenzyme, PP2A/B55a, specifically recognizes substrates and presents them to the enzyme active site. Here, we show how the PP2A regulatory subunit B55a recruits p107, a pRB-related tumor suppressor and B55a substrate. Using molecular and cellular approaches, we identified a conserved region 1 (R1, residues 615-626) encompassing the strongest p107 binding site. This enabled us to identify an "HxRVxxV619-625" short linear motif (SLiM) in p107 as necessary for B55a binding and dephosphorylation of the proximal pSer-615 in vitro and in cells. Numerous B55a/PP2A substrates, including TAU, contain a related SLiM C-terminal from a proximal phosphosite, "p[SSTT]-P--x(4,10)-[RK]-V-x-x-[VII]-R". Mutation of conserved SLiM residues in TAU dramatically inhibits dephosphorylation by PP2A/B55a, validating its generality. A data-guided computational model details the interaction of residues from the conserved p107 SLiM, the B55a groove, and phosphosite presentation. Altogether these data provide key insights into PP2A/B55a mechanisms of substrate recruitment and active site engagement, and also facilitate identification and validation of new substrates, a key step towards understanding PP2A/B55a role in multiple cellular processes. |
| HostingRepository | MassIVE |
| AnnounceDate | 2021-11-02 |
| AnnouncementXML | Submission_2021-11-02_08:46:36.081.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 | Carbamidomethyl; Oxidation |
| Instrument | Q Exactive Plus |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2021-09-17 07:03:36 | ID requested | |
| ⏵ 1 | 2021-11-02 08:46:36 | announced |
Publication List
| no publication |
Keyword List
| submitter keyword: phosphorylation, PP2A, p107, pRB, TAU, B55a |
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/MSV000088106/ |
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