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PXD007214

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2017-11-14
  • AnnouncementXML: Submission_2017-11-14_08:21:56.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Martin Steger
  • Title: Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis
  • Description: We previously reported that Parkinson’s disease (PD) kinase LRRK2 phosphorylates a subset of Rab GTPases on a conserved residue in their switch-II domains (Steger, Tonelli et al., 2016) (PMID: 26824392). Here, we systematically analyzed the Rab protein family and found 14 of them (Rab3A/B/C/D, Rab5A/B/C, Rab8A/B, Rab10, Rab12, Rab29, Rab35 and Rab43) to be specifically phosphorylated by LRRK2, with evidence for endogenous phosphorylation for ten of them (Rab3A, Rab3B, Rab3C, Rab3D, Rab8A, Rab8B Rab10, Rab12, Rab35 and Rab43). Affinity enrichment mass spectrometry revealed that the primary ciliogenesis regulators RILPL1 specifically interacts with the LRRK2-phosphorylated forms of Rab8A and Rab10, whereas RILPL2 binds to phosphorylated Rab8A, Rab10, and Rab12. Induction of cilia formation by serum starvation led to a two-fold reduction in ciliogenesis in fibroblasts derived from pathogenic LRRK2-R1441G knock-in mice. These results implicate LRRK2 in primary cilia formation and suggest that Rab-mediated protein transport and/or signaling defects at cilia may contribute to LRRK2-dependent pathologies.
  • SpeciesList: scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
  • ModificationList: phosphorylated residue
  • Instrument: Q Exactive

Dataset History

VersionDatetimeStatusChangeLog Entry
02017-08-08 00:08:33ID requested
12017-11-14 08:21:57announced

Publication List

  1. Dataset with its publication pending

Keyword List

  1. curator keyword: Biomedical
  2. submitter keyword: LRRK2, proteomics, RabGTPases, Parkinson's disease

Contact List

    Matthias Mann
    • contact affiliation: Max Planck Institute of Biochemistry
    • contact email: mmann@biochem.mpg.de
    • lab head:
    Martin Steger
    • contact affiliation: Max Planck Institute of Biochemistry
    • contact email: steger@biochem.mpg.de
    • dataset submitter:

Full Dataset Link List

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  2. PRIDE project URI
Repository Record List
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