TY - JOUR
T1 - O-GlcNAc signalling
T2 - Implications for cancer cell biology
AU - Slawson, Chad
AU - Hart, Gerald Warren
PY - 2011/9
Y1 - 2011/9
N2 - O-GlcNAcylation is the covalent attachment of Î 2-D-N- acetylglucosamine (GlcNAc) sugars to serine or threonine residues of nuclear and cytoplasmic proteins, and it is involved in extensive crosstalk with other post-translational modifications, such as phosphorylation. O-GlcNAcylation is becoming increasing realized as having important roles in cancer-relevant processes, such as cell signalling, transcription, cell division, metabolism and cytoskeletal regulation. However, currently little is known about the specific roles of aberrant O-GlcNAcylation in cancer. In this Opinion article, we summarize the current understanding of O-GlcNAcylation in cancer and its emerging functions in transcriptional regulation at the level of chromatin and transcription factors.
AB - O-GlcNAcylation is the covalent attachment of Î 2-D-N- acetylglucosamine (GlcNAc) sugars to serine or threonine residues of nuclear and cytoplasmic proteins, and it is involved in extensive crosstalk with other post-translational modifications, such as phosphorylation. O-GlcNAcylation is becoming increasing realized as having important roles in cancer-relevant processes, such as cell signalling, transcription, cell division, metabolism and cytoskeletal regulation. However, currently little is known about the specific roles of aberrant O-GlcNAcylation in cancer. In this Opinion article, we summarize the current understanding of O-GlcNAcylation in cancer and its emerging functions in transcriptional regulation at the level of chromatin and transcription factors.
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U2 - 10.1038/nrc3114
DO - 10.1038/nrc3114
M3 - Article
C2 - 21850036
AN - SCOPUS:80052068559
VL - 11
SP - 678
EP - 684
JO - Nature Reviews Cancer
JF - Nature Reviews Cancer
SN - 1474-175X
IS - 9
ER -