<<< Full experiment listing

PXD002609

PXD002609 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleQuantitative Phosphoproteomics reveals new roles for PP6 in chromosome condensation and segregation
DescriptionProtein phosphorylation by protein kinases and phosphatases is an important regulatory mechanism that controls mitotic progression. Protein Phosphatase 6 (PP6) is an essential enzyme with conserved roles in chromosome segregation and spindle assembly from yeast to humans. Here, we develop a baculovirus-mediated gene silencing approach and combine it with mass spectrometry-based quantitative phosphoproteomics to overcome the lack of PP6-specific inhibitors and comprehensively determine changes in phosphorylation and protein abundance upon depletion of the catalytic subunit of PP6 (PP6c). We identify 400 phosphopeptides on 267 proteins that increase in phosphorylation occupancy upon PP6c depletion in mitosis and reveal new PP6c-dependent regulatory pathways. We demonstrate that PP6c directly opposes casein kinase 2-dependent phosphorylation of the condensin I subunit NCAP-G and show that depletion of PP6c results in defects in chromosome and condensation and segregation in anaphase, consistent with deregulation of condensin I function.
HostingRepositoryMassIVE
AnnounceDate2015-09-22
AnnouncementXMLSubmission_2015-09-22_13:33:25.xml
DigitalObjectIdentifier
ReviewLevelNon peer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportSupported dataset by repository
PrimarySubmitterMark Adamo
SpeciesList scientific name: Homo sapiens; common name: human; NCBI TaxID: 9606;
ModificationListCarbamidomethyl; Oxidation; Phospho; Dimethyl; Dimethyl:2H(6)13C(2); TMT6plex
InstrumentOrbitrap Fusion; instrument model: Q Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02015-07-27 12:59:53ID requested
12015-09-22 13:33:25announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Mitosis, Protein Phosphatase 6, PP6, Phosphoproteomics
Contact List
Arminja Kettenbach
lab head
Mark Adamo
contact affiliationDartmouth College
contact emailmark.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/MSV000079201