Proteomics

Dataset Information

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O-linked and N-linked analysis of PTP69D (Drosophila melanogaster)

ABSTRACT: Identifying N-linked and O-linked sites of glycosylation on PTP69D (Drosophila melanogaster) by sHCD and CID neutral loss-trigged MS3.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Drosophila Melanogaster (fruit Fly)

SUBMITTER: Robert Bridger  

LAB HEAD: Robert Bridger

PROVIDER: PXD034563 | Pride | 2023-03-11

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
RB-Panin-OE-CIDtMS3-042222-_1_.pdResult Other
RB-Panin-OE-CIDtMS3-042222.pdResult Other
RB-Panin-OE-CIDtMS3-042222.raw.byspec2 Raw
RB-Panin-POMGNT1-sHCD.raw.byspec2 Raw
RB-VP-2ndRun-MT-030320-ptmRS.pdResult Other
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Publications

Protein tyrosine phosphatase 69D is a substrate of protein O-mannosyltransferases 1-2 that is required for the wiring of sensory axons in Drosophila.

Monagas-Valentin Pedro P   Bridger Robert R   Chandel Ishita I   Koff Melissa M   Novikov Boris B   Schroeder Patrick P   Wells Lance L   Panin Vladislav V  

The Journal of biological chemistry 20230110 3

Mutations in protein O-mannosyltransferases (POMTs) result in severe brain defects and congenital muscular dystrophies characterized by abnormal glycosylation of α-dystroglycan (α-Dg). However, neurological phenotypes of POMT mutants are not well understood, and the functional substrates of POMTs other than α-Dg remain unknown. Using a Drosophila model, here we reveal that Dg alone cannot account for the phenotypes of POMT mutants, and identify Protein tyrosine phosphatase 69D (PTP69D) as a gene  ...[more]

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