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O-GlcNAcylation of tubulin inhibits its polymerization.
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- Author(s): Ji, Suena; Kang, Jeong; Park, Sang; Lee, JooHun; Oh, Young; Cho, Jin
- Source:
Amino Acids; Mar2011, Vol. 40 Issue 3, p809-818, 10p, 1 Color Photograph, 5 Black and White Photographs, 1 Chart, 1 Graph
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- Additional Information
- Abstract:
The attachment of O-linked β- N-acetylglucosamine ( O-GlcNAc) to proteins is an abundant and reversible modification that involves many cellular processes including transcription, translation, cell proliferation, apoptosis, and signal transduction. Here, we found that the O-GlcNAc modification pattern was altered during all- trans retinoic acid (tRA)-induced neurite outgrowth in the MN9D neuronal cell line. We identified several O-GlcNAcylated proteins using mass spectrometric analysis, including α- and β-tubulin. Further analysis of α- and β-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of α-tubulin and between residues 216 and 238 of β-tubulin, respectively. We found that an increase in α-tubulin O-GlcNAcylation reduced heterodimerization and that O-GlcNAcylated tubulin did not polymerize into microtubules. Consequently, when O-GlcNAcase inhibitors were co-incubated with tRA, the extent of neurite outgrowth was decreased by 20% compared to control. Thus, our data indicate that the O-GlcNAcylation of tubulin negatively regulates microtubule formation. [ABSTRACT FROM AUTHOR]
- Abstract:
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