O-GlcNAc modification: A nutritional sensor that modulates proteasome function

Natasha E. Zachara; Gerald W. Hart

doi:10.1016/j.tcb.2004.03.005

O-GlcNAc modification: A nutritional sensor that modulates proteasome function

Natasha E. Zachara, Gerald W. Hart

School of Medicine

Research output: Contribution to journal › Short survey › peer-review

81 Scopus citations

Abstract

The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.

Original language	English (US)
Pages (from-to)	218-221
Number of pages	4
Journal	Trends in Cell Biology
Volume	14
Issue number	5
DOIs	https://doi.org/10.1016/j.tcb.2004.03.005
State	Published - May 2004

ASJC Scopus subject areas

Cell Biology

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title = "O-GlcNAc modification: A nutritional sensor that modulates proteasome function",

abstract = "The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.",

author = "Zachara, {Natasha E.} and Hart, {Gerald W.}",

note = "Funding Information: We thank Chad Slawson (The Johns Hopkins University) for critical reading of the manuscript. G.W.H. acknowledges the support of NIH grants DK 61671, HD13563, CA42486.",

year = "2004",

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doi = "10.1016/j.tcb.2004.03.005",

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T1 - O-GlcNAc modification

T2 - A nutritional sensor that modulates proteasome function

AU - Zachara, Natasha E.

AU - Hart, Gerald W.

N1 - Funding Information: We thank Chad Slawson (The Johns Hopkins University) for critical reading of the manuscript. G.W.H. acknowledges the support of NIH grants DK 61671, HD13563, CA42486.

PY - 2004/5

Y1 - 2004/5

N2 - The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.

AB - The addition of O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.

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DO - 10.1016/j.tcb.2004.03.005

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EP - 221

JO - Trends in Cell Biology

JF - Trends in Cell Biology

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O-GlcNAc modification: A nutritional sensor that modulates proteasome function

Abstract

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