Linked Life Data

20665223

Source:http://linkedlifedata.com/resource/pubmed/id/20665223

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2011-2-18
pubmed:abstractText
The attachment of O-linked ?-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 ?- and ?-tubulin. Further analysis of ?- and ?-tubulin revealed that O-GlcNAcylated peptides mapped between residues 173 and 185 of ?-tubulin and between residues 216 and 238 of ?-tubulin, respectively. We found that an increase in ?-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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1438-2199
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
809-18
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
O-GlcNAcylation of tubulin inhibits its polymerization.
pubmed:affiliation
Department of Biology, Yonsei University, Seoul, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't