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Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation
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 α-Tubulin—reflect the different roles of Elongator in the cytosol and the nucleus....
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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Hindawi Publishing Corporation
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025403/ https://www.ncbi.nlm.nih.gov/pubmed/21274405 http://dx.doi.org/10.1155/2011/924898 |
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author | Creppe, Catherine Buschbeck, Marcus |
author_facet | Creppe, Catherine Buschbeck, Marcus |
author_sort | Creppe, Catherine |
collection | PubMed |
description | 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 α-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 α-Tubulin contributes to intracellular trafficking and cell migration. Defects in both functions of Elongator have been implicated in neurodegenerative disorders. |
format | Text |
id | pubmed-3025403 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Hindawi Publishing Corporation |
record_format | MEDLINE/PubMed |
spelling | pubmed-30254032011-01-27 Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation Creppe, Catherine Buschbeck, Marcus J Biomed Biotechnol Review Article 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 α-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 α-Tubulin contributes to intracellular trafficking and cell migration. Defects in both functions of Elongator have been implicated in neurodegenerative disorders. Hindawi Publishing Corporation 2011 2011-01-12 /pmc/articles/PMC3025403/ /pubmed/21274405 http://dx.doi.org/10.1155/2011/924898 Text en Copyright © 2011 C. Creppe and M. Buschbeck. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Creppe, Catherine Buschbeck, Marcus Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title | Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title_full | Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title_fullStr | Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title_full_unstemmed | Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title_short | Elongator: An Ancestral Complex Driving Transcription and Migration through Protein Acetylation |
title_sort | elongator: an ancestral complex driving transcription and migration through protein acetylation |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3025403/ https://www.ncbi.nlm.nih.gov/pubmed/21274405 http://dx.doi.org/10.1155/2011/924898 |
work_keys_str_mv | AT creppecatherine elongatoranancestralcomplexdrivingtranscriptionandmigrationthroughproteinacetylation AT buschbeckmarcus elongatoranancestralcomplexdrivingtranscriptionandmigrationthroughproteinacetylation |