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PXD065711

PXD065711 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleDisruption of the Golgi-based deacetylase alters the quality of the secretome and neuronal activity
DescriptionThe lysine acetylation status of modified proteins depends on acetyltransferases and deacetylases, which often coexist within the same cellular organelle or compartment. An exception is the conventional protein secretion pathway, where acetylation occurs in the lumen of the endoplasmic reticulum (ER) while deacetylation occurs in the lumen of the Golgi apparatus. Here, we provide in vitro and in vivo evidence that C6orf89, a Golgi-based type II membrane protein, has deacetylase activity and behaves as a Zn+2-dependent deacetylase. Furthermore, genetic disruption of C6orf89 in the mouse almost abolished the endogenous Golgi-based deacetylase activity supporting the argument that C6orf89 is a Golgi-based deacetylase (GDAC). Deletion of C6orf89 in the mouse resulted in behavioral defects, expansion of the dendritic spine network, and altered neuronal spontaneous firing. Mechanistically, the mice displayed expansion of the Golgi network with altered N-glycosylation of trafficking glycoproteins. In conclusion, our findings suggest that Golgi deacetylation of transiting N-glycoproteins is required to ensure the quality of the secretome within the conventional protein secretion pathway.
HostingRepositoryMassIVE
AnnounceDate2026-04-11
AnnouncementXMLSubmission_2026-04-11_11:08:27.728.xml
DigitalObjectIdentifier
ReviewLevelNon peer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFeixuan
SpeciesList scientific name: Mus musculus; common name: house mouse; NCBI TaxID: 10090;
ModificationListunknown modification
InstrumentOrbitrap Fusion Lumos
Dataset History
RevisionDatetimeStatusChangeLog Entry
02025-07-02 21:12:49ID requested
12026-04-11 11:08:28announced
Publication List
no publication
Keyword List
submitter keyword: Acetyl-CoA, C6orf89, Deacetylase, Golgi apparatus, N-glycosylation, DatasetType:Proteomics, DatasetType:Other (Glycoproteomics)
Contact List
Luigi Puglielli
contact affiliationUniversity of Wisconsin - Madison
contact emaillp1@medicine.wisc.edu
lab head
Feixuan
contact affiliationUniversity of Wisconsin-Madison
contact emailfwu76@wisc.edu
dataset submitter
Full Dataset Link List
MassIVE dataset URI
Dataset FTP location
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