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PXD004341

DataSet Summary

  • HostingRepository: PRIDE
  • AnnounceDate: 2017-05-18
  • AnnouncementXML: Submission_2017-05-19_02:43:29.xml
  • DigitalObjectIdentifier:
  • ReviewLevel: Peer-reviewed dataset
  • DatasetOrigin: Original data
  • RepositorySupport: Unsupported dataset by repository
  • PrimarySubmitter: Adnan Halim
  • Title: CHO 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: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus); NCBI TaxID: 10029;
  • ModificationList: monohydroxylated residue; complex glycosylation; iodoacetamide derivatized residue
  • Instrument: LTQ Orbitrap Velos; Orbitrap Fusion ETD

Dataset History

VersionDatetimeStatusChangeLog Entry
02016-06-16 03:55:59ID requested
12017-05-19 02:43:30announced

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-mannosyltransferases 1 and 2. J Biol Chem, 292(27):11586-11598(2017) [pubmed]

Keyword List

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