Article (Scientific journals)
Elongator: an ancestral complex driving transcription and migration through protein acetylation.
Creppe, Catherine; Buschbeck, Marcus
2011In Journal of Biomedicine and Biotechnology, 2011, p. 924898
Peer Reviewed verified by ORBi
 

Files


Full Text
Creppe and Buschbeck 2011.pdf
Publisher postprint (1.19 MB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Acetylation; Animals; Cell Movement/physiology; Histone Acetyltransferases/genetics/metabolism/physiology; Histones/metabolism; Humans; Mice; Nerve Tissue Proteins/genetics/metabolism/physiology; Neurodegenerative Diseases/genetics/metabolism; Transcription, Genetic; Tubulin/metabolism
Abstract :
[en] Elongator is an evolutionary highly conserved complex. At least two of its cellular functions rely on the intrinsic lysine acetyl-transferase activity of the elongator complex. Its two known substrates--histone H3 and alpha-tubulin--reflect the different roles of elongator in the cytosol and the nucleus. A picture seems to emerge in which nuclear elongator could regulate the transcriptional elongation of a subset of stress-inducible genes through acetylation of histone H3 in the promoter-distal gene body. In the cytosol, elongator-mediated acetylation of alpha-tubulin contributes to intracellular trafficking and cell migration. Defects in both functions of elongator have been implicated in neurodegenerative disorders.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Creppe, Catherine ;  Université de Liège - ULiège
Buschbeck, Marcus
Language :
English
Title :
Elongator: an ancestral complex driving transcription and migration through protein acetylation.
Publication date :
12 January 2011
Journal title :
Journal of Biomedicine and Biotechnology
ISSN :
1110-7243
eISSN :
1110-7251
Publisher :
Hindawi Publishing Corporation, Egypt
Volume :
2011
Pages :
924898
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 26 January 2016

Statistics


Number of views
49 (0 by ULiège)
Number of downloads
113 (1 by ULiège)

Scopus citations®
 
19
Scopus citations®
without self-citations
19
OpenCitations
 
13

Bibliography


Similar publications



Contact ORBi