Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins

Gerald W. Hart; Kenneth D. Greis; L. Y.Dennis Dong; Melissa A. Blomberg; Teh Ying Chou; Man Shiow Jiang; Elizabeth P. Roquemore; Doris M. Snow; Lisa K. Kreppel; Robert C. Cole; Bradley K. Hayes

doi:10.1351/pac199567101637

Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins

Gerald W. Hart, Kenneth D. Greis, L. Y.Dennis Dong, Melissa A. Blomberg, Teh Ying Chou, Man Shiow Jiang, Elizabeth P. Roquemore, Doris M. Snow, Lisa K. Kreppel, Robert C. Cole, Bradley K. Hayes

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

We have described a novel form of nuclear and cytoplasmic protein glycosylation (O-GlcNAc), which is as abundant and as transient on intracellular proteins as protein phosphorylation. O-GlcNAc consists of single, non-modified N~ acetylglucosamine residues O-glycosidically attached to Ser(Thr) hydroxyl moieties at sites similar to those used by growth-factor kinases. O-GlcNAc occurs on ‘hundreds’ of intracellular proteins in all eukaryotes. Proteins bearing O-GlcNAc include cytoskeletal-, viral-, nuclear pore-, heat shock-, and transcriptional regulatory proteins. Available data suggest that O-GlcNAc is a regulatory modification that mediates subunit-subunit interactions, and in many cases blocks phosphorylation.

Original language	English (US)
Pages (from-to)	1637-1645
Number of pages	9
Journal	Pure and Applied Chemistry
Volume	67
Issue number	10
DOIs	https://doi.org/10.1351/pac199567101637
State	Published - Jan 1 1995
Externally published	Yes

ASJC Scopus subject areas

General Chemistry
General Chemical Engineering

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title = "Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins",

abstract = "We have described a novel form of nuclear and cytoplasmic protein glycosylation (O-GlcNAc), which is as abundant and as transient on intracellular proteins as protein phosphorylation. O-GlcNAc consists of single, non-modified N~ acetylglucosamine residues O-glycosidically attached to Ser(Thr) hydroxyl moieties at sites similar to those used by growth-factor kinases. O-GlcNAc occurs on {\textquoteleft}hundreds{\textquoteright} of intracellular proteins in all eukaryotes. Proteins bearing O-GlcNAc include cytoskeletal-, viral-, nuclear pore-, heat shock-, and transcriptional regulatory proteins. Available data suggest that O-GlcNAc is a regulatory modification that mediates subunit-subunit interactions, and in many cases blocks phosphorylation.",

author = "Hart, {Gerald W.} and Greis, {Kenneth D.} and Dong, {L. Y.Dennis} and Blomberg, {Melissa A.} and Chou, {Teh Ying} and Jiang, {Man Shiow} and Roquemore, {Elizabeth P.} and Snow, {Doris M.} and Kreppel, {Lisa K.} and Cole, {Robert C.} and Hayes, {Bradley K.}",

year = "1995",

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doi = "10.1351/pac199567101637",

language = "English (US)",

volume = "67",

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journal = "Pure and Applied Chemistry",

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TY - JOUR

T1 - Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins

AU - Hart, Gerald W.

AU - Greis, Kenneth D.

AU - Dong, L. Y.Dennis

AU - Blomberg, Melissa A.

AU - Chou, Teh Ying

AU - Jiang, Man Shiow

AU - Roquemore, Elizabeth P.

AU - Snow, Doris M.

AU - Kreppel, Lisa K.

AU - Cole, Robert C.

AU - Hayes, Bradley K.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - We have described a novel form of nuclear and cytoplasmic protein glycosylation (O-GlcNAc), which is as abundant and as transient on intracellular proteins as protein phosphorylation. O-GlcNAc consists of single, non-modified N~ acetylglucosamine residues O-glycosidically attached to Ser(Thr) hydroxyl moieties at sites similar to those used by growth-factor kinases. O-GlcNAc occurs on ‘hundreds’ of intracellular proteins in all eukaryotes. Proteins bearing O-GlcNAc include cytoskeletal-, viral-, nuclear pore-, heat shock-, and transcriptional regulatory proteins. Available data suggest that O-GlcNAc is a regulatory modification that mediates subunit-subunit interactions, and in many cases blocks phosphorylation.

AB - We have described a novel form of nuclear and cytoplasmic protein glycosylation (O-GlcNAc), which is as abundant and as transient on intracellular proteins as protein phosphorylation. O-GlcNAc consists of single, non-modified N~ acetylglucosamine residues O-glycosidically attached to Ser(Thr) hydroxyl moieties at sites similar to those used by growth-factor kinases. O-GlcNAc occurs on ‘hundreds’ of intracellular proteins in all eukaryotes. Proteins bearing O-GlcNAc include cytoskeletal-, viral-, nuclear pore-, heat shock-, and transcriptional regulatory proteins. Available data suggest that O-GlcNAc is a regulatory modification that mediates subunit-subunit interactions, and in many cases blocks phosphorylation.

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JO - Pure and Applied Chemistry

JF - Pure and Applied Chemistry

IS - 10

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Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins

Abstract

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