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PXD004358

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2017-05-18
  • AnnouncementXML: Submission_2017-05-19_02:42:44.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Adnan Halim
  • Title: Human O-Mannosylation independent of POMT1/2
  • Description: Protein O-mannosylation is found in yeast and metazoans and a family of conserved orthologous polypeptide O-mannosyltransferases is believed to initiate this important posttranslational modification. We recently discovered that the large families of cadherins and protocadherins carry highly conserved O-Man glycans in specific EC domains, and it was suggested that the function of E-Cadherin was dependent on the O-Man glycans. Deficiencies in the two human polypeptide O-mannosyltransferases, POMT1 and T2, underlie a subgroup of congenital muscular dystrophies (CMD) designated α-dystroglycanopathies, because deficient O-Man glycans on -dystroglycan impair laminin interaction with -dystroglycan and the dystrophin complex. In order to explore the functions of O-Man glycans on cadherins and protocadherins we used a combinatorial gene editing strategy in multiple cell lines to evaluate to the role of the two POMTs initiation O-Man glycosylation and the major enzyme elongating O-Man glycans, the POMGNT1 2GlcNAc-transferase. Surprisingly, we discovered that O-Man glycans on cadherins and protocadherins do not appear to require POMT1 and T2 and moreover that the O-Man glycans on these proteins are not elongated in contrast to those on dystroglycan.
  • SpeciesList: scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
  • ModificationList: monohydroxylated residue; complex glycosylation; iodoacetamide derivatized residue
  • Instrument: LTQ Orbitrap Velos; Orbitrap Fusion ETD

Dataset History

VersionDatetimeStatusChangeLog Entry
02016-06-17 07:02:55ID requested
12017-05-19 02:42:45announced

Publication List

  1. Larsen ISB, Narimatsu Y, Joshi HJ, Yang Z, Harrison OJ, Brasch J, Shapiro L, Honig B, Vakhrushev SY, Clausen H, Halim A, Mammalian O-mannosylation of Cadherins and Plexins is Independent of Protein O-mannosyltransferase 1 and 2. J Biol Chem, ():(2017) [pubmed]

Keyword List

  1. curator keyword: Biological
  2. submitter keyword: O-Glycosylation, Glycoproteomics, O-Mannose, Mannosyltransferase

Contact List

    Henrik Clausen
    • contact affiliation: Copenhagen Center for Glycomics and Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, DK-2200 Copenhagen N, Denmark
    • contact email: hclau@sund.ku.dk
    • lab head:
    Adnan Halim
    • contact affiliation: University of Copenhagen
    • contact email: halim@sund.ku.dk
    • dataset submitter:

Full Dataset Link List

  1. Dataset FTP location
  2. PRIDE project URI
Repository Record List
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