⮝ Full datasets listing
PXD073461
PXD073461 is an original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Characterization of Protein Phosphatase 1b substrate specificity |
| Description | Phosphoprotein phosphatase 1 (PP1) is a heterodimeric holoenzyme consisting of a catalytic subunit (PP1c) and one of over 200 regulatory subunits (PP1R). The interaction between catalytic and regulatory subunits is mediated by short linear motifs (SLiMs). The human genome encodes four highly conserved PP1c isoforms, PP1ca, PP1cb, and splice variants PP1cc1 and PP1cc2. Using affinity purification mass spectrometry (AP-MS), we identify PP1c isoform-specific interactors and confirm that myosin phosphatase N-terminal element (MyPhoNE) motif-containing PP1R are significantly enriched in binding to the PP1cb compared to the PP1ca and PP1cc isoforms. To uncover the key binding determinants of PP1cb binding to MyPhoNE-containing PP1Rs, we created chimeric mutants of PP1cb and PP1cc. We employed CRISPR-Cas9-mediated editing of the PP1cb locus to generate a Thr197Gln mutant that mimics the amino acid found in PP1cc. We find that the Thr197 residue, as well as carboxyl-terminal residues of PP1cb, coordinate binding to MyPhoNE-PP1Rs. Additionally, quantitative phosphoproteomics of the homozygous knock-in PP1cb Thr197Gln cells identifies a phosphorylation site in the activation loop of Polo-like kinase 1 (PLK1) as a potential PP1cb substrate. We validate this finding by immunofluorescence and add to the current understanding of the critical role of the PP1cb-MYPT1 holoenzyme in controlling PLK1 activity in early mitosis. |
| HostingRepository | MassIVE |
| AnnounceDate | 2026-08-20 |
| AnnouncementXML | Submission_2026-08-20_14:06:46.095.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Non peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Supported dataset by repository |
| PrimarySubmitter | Arminja Nadine Kettenbach |
| SpeciesList | scientific name: Homo sapiens; common name: human; NCBI TaxID: 9606; |
| ModificationList | Phospho |
| Instrument | Orbitrap Fusion; Orbitrap Fusion Lumos; Q Exactive Plus |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
|---|---|---|---|
| 0 | 2026-01-23 09:02:07 | ID requested | |
| ⏵ 1 | 2026-08-20 14:06:46 | announced |
Publication List
| no publication |
Keyword List
| submitter keyword: phosphoprotein phosphatase 1 (PP1), substrate specificity, MyPhoNE motif, protein chimera, phosphorylation, phosphoproteomics, mitosis, DatasetType:Proteomics |
Contact List
| Arminja Kettenbach | |
|---|---|
| contact affiliation | The Geisel School of Medicine at Dartmouth |
| contact email | arminja.n.kettenbach@dartmouth.edu |
| lab head | |
| Arminja Nadine Kettenbach | |
| contact affiliation | Dartmouth |
| contact email | Arminja.N.Kettenbach@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-ftp.ucsd.edu/v12/MSV000100567/ |
