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PXD030448

PXD030448 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleA systematic screening pipeline identifies a new regulator of tyrosinated microtubule dynamics
DescriptionTubulin detyrosination is a reversible post-translational modification thought to be important for processes including the generation of cell polarity and cell division. The Y/ΔY cycle does not affect the intrinsic properties of microtubules per se, but rather influences the cohort of microtubule-associated proteins (MAPs) and motor proteins that associate with microtubules. Here we present a screening pipeline to identify proteins that bind microtubules in a manner that depends on the Y versus ΔY state.
HostingRepositoryPRIDE
AnnounceDate2022-08-16
AnnouncementXMLSubmission_2022-08-15_19:56:00.844.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterSarah Haynes
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListTMT6plex-126 reporter+balance reagent acylated residue; monohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-12-16 11:17:19ID requested
12022-08-15 19:56:02announced
Publication List
Hotta T, McAlear TS, Yue Y, Higaki T, Haynes SE, Nesvizhskii AI, Sept D, Verhey KJ, Bechstedt S, Ohi R, EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules. Curr Biol, 32(18):3898-3910.e14(2022) [pubmed]
Keyword List
submitter keyword: microtubule, tyrosination, detyrosination, TMT6, LC-MS/MS, human
Contact List
Alexey Nesvizhskii
contact affiliationDepartment of Pathology, University of Michigan, USA
contact emailnesvi@med.umich.edu
lab head
Sarah Haynes
contact affiliationUniversity of Michigan
contact emailhayse@umich.edu
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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