PMID- 27048592
OWN - NLM
STAT- MEDLINE
DCOM- 20170515
LR  - 20181113
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Print)
IS  - 0264-6021 (Linking)
VI  - 473
IP  - 12
DP  - 2016 Jun 15
TI  - Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of 
      mitochondrial proteins.
PG  - 1693-702
LID - 10.1042/BCJ20160092 [doi]
AB  - O-linked N-acetylglucosamine modification (O-GlcNAcylation) is a 
      nutrient-dependent protein post-translational modification (PTM), dynamically and 
      reversibly driven by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase 
      (OGA) that catalyse the addition and the removal of the O-GlcNAc moieties to/from 
      serine and threonine residues of target proteins respectively. Increasing 
      evidence suggests involvement of O-GlcNAcylation in many biological processes, 
      including transcription, signalling, neuronal development and mitochondrial 
      function. The presence of a mitochondrial O-GlcNAc proteome and a mitochondrial 
      OGT (mOGT) isoform has been reported. We explored the presence of mOGT in human 
      cell lines and mouse tissues. Surprisingly, analysis of genomic sequences 
      indicates that this isoform cannot be expressed in most of the species analysed, 
      except some primates. In addition, we were not able to detect endogenous mOGT in 
      a range of human cell lines. Knockdown experiments and Western blot analysis of 
      all the predicted OGT isoforms suggested the expression of only a single OGT 
      isoform. In agreement with this, we demonstrate that overexpression of the 
      nucleocytoplasmic OGT (ncOGT) isoform leads to increased O-GlcNAcylation of 
      mitochondrial proteins, suggesting that ncOGT is necessary and sufficient for the 
      generation of the O-GlcNAc mitochondrial proteome.
CI  - (c) 2016 The Author(s).
FAU - Trapannone, Riccardo
AU  - Trapannone R
AD  - School of Life Sciences, University of Dundee, Dundee DD1 4HN, U.K.
FAU - Mariappa, Daniel
AU  - Mariappa D
AD  - School of Life Sciences, University of Dundee, Dundee DD1 4HN, U.K.
FAU - Ferenbach, Andrew T
AU  - Ferenbach AT
AD  - School of Life Sciences, University of Dundee, Dundee DD1 4HN, U.K.
FAU - van Aalten, Daan M F
AU  - van Aalten DM
AD  - School of Life Sciences, University of Dundee, Dundee DD1 4HN, U.K. Division of 
      Molecular Microbiology, College of Life Sciences, University of Dundee, Dundee 
      DD1 4HN, U.K. d.m.f.vanaalten@dundee.ac.uk.
LA  - eng
GR  - WT087590MA/Wellcome Trust/United Kingdom
GR  - WT097459/Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20160405
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Protein Isoforms)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.- (O-GlcNAc transferase)
RN  - EC 3.2.1.50 (hexosaminidase C)
RN  - EC 3.2.1.52 (beta-N-Acetylhexosaminidases)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Western
MH  - Cell Line
MH  - Cell Nucleus/*enzymology
MH  - Cytoplasm/*enzymology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - HEK293 Cells
MH  - HeLa Cells
MH  - Humans
MH  - Immunoprecipitation
MH  - Mice
MH  - Mitochondrial Proteins/genetics/*metabolism
MH  - Molecular Sequence Data
MH  - N-Acetylglucosaminyltransferases/genetics/*metabolism
MH  - Open Reading Frames/genetics
MH  - Protein Isoforms/genetics/metabolism
MH  - beta-N-Acetylhexosaminidases/genetics/metabolism
PMC - PMC4901358
OTO - NOTNLM
OT  - O-GlcNAc transferase (OGT)
OT  - O-linked N-acetylglucosamine (O-GlcNAc)
OT  - alternative splicing
OT  - glycobiology
OT  - mitochondria
OT  - post-translational modification (PTM)
EDAT- 2016/04/07 06:00
MHDA- 2017/05/16 06:00
PMCR- 2016/06/10
CRDT- 2016/04/07 06:00
PHST- 2015/09/01 00:00 [received]
PHST- 2016/04/05 00:00 [accepted]
PHST- 2016/04/07 06:00 [entrez]
PHST- 2016/04/07 06:00 [pubmed]
PHST- 2017/05/16 06:00 [medline]
PHST- 2016/06/10 00:00 [pmc-release]
AID - BCJ20160092 [pii]
AID - 10.1042/BCJ20160092 [doi]
PST - ppublish
SO  - Biochem J. 2016 Jun 15;473(12):1693-702. doi: 10.1042/BCJ20160092. Epub 2016 Apr 
      5.