PXD001672 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | SPPL3 cleavage of glycosyltransferases regulates their activity |
Description | The GxGD intramembrane-cleaving aspartylprotease signal peptide peptidase-like 3 (SPPL3) is a Golgi-resident, multi-pass membrane protein that is highly conserved among multicellular eukaryotes pointing to a pivotal physiological function in the Golgi network. Recently, the key branching enzyme N-acetylglucosaminyltransferase V (GnT-V) and other medial/trans Golgi glycosyltransferases were identified as first physiological SPPL3 substrates. SPPL3-mediated endoproteolysis releases these enzymes from their type II membrane anchors resulting in a subsequent secretion of the respective enzymes’ ectodomain. To systematically identify further SPPL3 substrates we used the secretome protein enrichment with click sugars (SPECS) method that makes secretomes of cultured cells accessible to mass spectrometric analyses. SPECS analyses of SPPL3-deficient and SPPL3-overexpression cell culture models revealed numerous additional SPPL3 candidate substrates and their subsequent biochemical validation underscores the role of SPPL3 in secretion of these proteins. In line with our previous observations, all novel SPPL3 substrates adopt a type II topology and the majority localizes to the Golgi network and is implicated in Golgi function. Importantly, most of the novel SPPL3 substrates catalyze the modification of N-linked glycans but also of O-glycans and glycosaminoglycans. Hence, SPPL3 emerges as a crucial player of Golgi function and the newly identified SPPL3 substrates will be instrumental to investigate the molecular mechanisms underlying the physiological function of SPPL3 in the Golgi network and in vivo. |
HostingRepository | PRIDE |
AnnounceDate | 2015-05-08 |
AnnouncementXML | Submission_2015-05-08_10:15:06.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Peer-Hendrik Kuhn |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | iodoacetamide derivatized residue |
Instrument | LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2015-01-13 03:39:55 | ID requested | |
⏵ 1 | 2015-05-08 10:15:08 | announced | |
Publication List
Kuhn PH, Voss M, Haug-Kr, ö, per M, Schr, ö, der B, Schepers U, Br, ä, se S, Haass C, Lichtenthaler SF, Fluhrer R, Secretome analysis identifies novel signal Peptide peptidase-like 3 (Sppl3) substrates and reveals a role of Sppl3 in multiple Golgi glycosylation pathways. Mol Cell Proteomics, 14(6):1584-98(2015) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: SPPL3, protease, substrates, SPECS |
Contact List
Prof. Dr. Stefan Lichtenthaler |
contact affiliation | DZNE Muenchen, Neuroproteomik |
contact email | Stefan.Lichtenthaler@dzne.de |
lab head | |
Peer-Hendrik Kuhn |
contact affiliation | DZNE München |
contact email | peerhendrik@gmx.net |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD001672
- Label: PRIDE project
- Name: SPPL3 cleavage of glycosyltransferases regulates their activity