PXD010173-2

PXD010173 is an original dataset announced via ProteomeXchange.

Title	O-GlcNAc pattern of sOGT regulates its substrate selectivity and function
Description	O-GlcNAcylation occurs on thousands of proteins involved in various cellular events. O-GlcNAc transferase (OGT), one of the enzymes responsible for protein O-GlcNAcylation, is known to be auto-O-GlcNAcylated at multiple sites. However, the role of O-GlcNAcylation on OGT is still unknown. Here, we report the role of O-GlcNAcylation on short form OGT (sOGT). By LC-ETD-MS analysis and western blot, we show that sOGT was mainly O-GlcNAcylated in the tetratricopeptide repeat (TPR) motifs with T12 and S56 being two “key” sites. T12 was a predominant O-GlcNAcylation site and the absence of S56 O-GlcNAcylation enhanced sOGT O-GlcNAcylation level. We found that O-GlcNAcylation of sOGT did not affect the enzyme activity but increased its binding to substrate proteins. S56A bound to and hence glycosylated more proteins, while T12A associated with fewer substrates. Proteomic studies combined with cell proliferation/cell cycle analyses indicated that S56A substantially enhanced cell proliferation, while T12A reduced it, and T12A led to a G2/M cell cycle arrest, due to O-GlcNAcylation of diverse proteins. These findings demonstrate that the O-GlcNAc pattern on sOGT modulates its function in cells by targeting different proteins.
HostingRepository	PRIDE
AnnounceDate	2019-09-16
AnnouncementXML	Submission_2019-09-25_02:49:15.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Yong Zhang
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	O-(N-acetylamino)glucosyl-L-threonine; O-(N-acetylamino)glucosyl-L-serine; monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue; deamidated residue
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2018-06-20 07:27:09	ID requested
1	2019-09-16 00:40:53	announced
⏵ 2	2019-09-25 02:49:17	announced	2019-09-25: Updated publication reference for PubMed record(s): 31527085.

Liu L, Li L, Ma C, Shi Y, Liu C, Xiao Z, Zhang Y, Tian F, Gao Y, Zhang J, Ying W, Wang PG, Zhang L, -GlcNAc transferase (sOGT) regulates its substrate selectivity. J Biol Chem, 294(45):16620-16633(2019) [pubmed]

curator keyword: Biological

submitter keyword: O-GlcNAc pattern;sOGT;site mapping;functional regulation

Lianwen Zhang
contact affiliation	college of pharmacy, Nankai university,Tianjin, 300353, China
contact email	lianwen@nankai.edu.cn
lab head
Yong Zhang
contact affiliation	Beijing Proteome Research Center
contact email	nankai1989@foxmail.com
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD010173
     1. Label: PRIDE project
     2. Name: O-GlcNAc pattern of sOGT regulates its substrate selectivity and function