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PXD013886-1

PXD013886 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleA dynamic charge:charge interaction modulates PP2A:B56 interactions
DescriptionThe recruitment of specific substrates by ser/thr protein phosphatase 2A (PP2A) regulatory B-subunits is poorly understood, limiting our understanding of PP2A-regulated signaling. Recently, the first PP2A:B56 consensus binding motif, LxxIxE, which confers substrate specificity to PP2A:B56 holoenzymes, was identified. However, most validated LxxIxE motifs interact with PP2A:B56 with low micromolar affinities, suggesting that additional recognition motifs exist that function cooperatively to enhance PP2A:B56 binding. Here, we report the requirement of a positively charged motif in a subset of PP2A:B56 interactors that facilitates B56 binding via dynamic charge:charge interactions. Using molecular and cellular approaches, we show that a highly conserved, negatively charged groove on B56 mediates this dynamic interaction. We also show that this motif is required for efficient binding and dephosphorylation of KIF4A in cells, confirming the functional relevance of this motif for PP2A:B56 dephosphorylation. Collectively our results provide an important framework for understanding PP2A regulation of cellular signaling.
HostingRepositoryMassIVE
AnnounceDate2020-03-16
AnnouncementXMLSubmission_2020-03-25_09:18:04.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;
ModificationListOxidation; Carbamidomethyl
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-05-16 09:01:06ID requested
12020-03-25 09:18:05announced
Publication List
no publication
Keyword List
submitter keyword: PP2A, B56, phosphatase, LxxIxE, motif, charge, interaction, KIF4A, cellular signaling, holoenzyme
Contact List
Arminja Kettenbach
contact affiliationThe Geisel School of Medicine at Dartmouth
contact emailarminja.n.kettenbach@dartmouth.edu
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
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