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PXD041196

PXD041196 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleUbiquitination of the actin polymerase VASP
DescriptionFilopodia are dynamic, actin-rich structures that extend outward from the cell to explore and respond to cues in the local environment. The actin polymerase VASP is a component of the filopodial tip complex, where it regulates actin polymerization and filopodial dynamics. Previously, we showed that VASP transiently co-localizes with the brain-enriched E3 ubiquitin ligase TRIM9 at the tips of neuronal filopodia. TRIM9 was required for the reversible, non-degradative ubiquitination of VASP and this modification was associated with decreased filopodia number and stability. Furthermore, the axon guidance cue netrin promoted deubiquitination of VASP. We hypothesize mono or multi-monoubiquitination of VASP is a mechanism to negatively regulate actin dynamics by blocking VASP and actin interactions. To determine the lysine residues that are ubiquitinated in VASP, we immunoprecipitated exogenously expressed human VASP from HEK293 cells. The immunopurified protein was analyzed by mass spectrometry to identify post-translational modifications. We identified numerous lysine residues that are ubiquitinated in VASP, including a high prevalence at K240 and K286.
HostingRepositoryPRIDE
AnnounceDate2024-01-17
AnnouncementXMLSubmission_2024-01-17_06:42:54.119.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAurora Cabrera
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListubiquitinylated lysine; phosphorylated residue
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-03-30 01:17:00ID requested
12024-01-17 06:42:54announced
Publication List
10.1242/JCS.261527;
Keyword List
submitter keyword: Actin
Ubiquitin
VASP
Post-translational modification
Contact List
Stephanie Gupton
contact affiliationUNC Chapel Hill
contact emailsgupton@email.unc.edu
lab head
Aurora Cabrera
contact affiliationDepartment of Pharmacology at UNC Chapel Hill
contact emailAurora_Cabrera@med.unc.edu
dataset submitter
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