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Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Title
Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity
Authors
Han Y.Jeong H.M.Jin Y.-H.Kim Y.-J.Jeong H.G.Yeo C.-Y.Lee K.-Y.
Ewha Authors
여창열
SCOPUS Author ID
여창열scopus
Issue Date
2009
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 383, no. 1, pp. 88 - 92
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Protein acetyltransferases and deacetylases affect the activities of each other. This is well documented by the acetylation and inhibition of HDAC1 by p300, a transcriptional co-activator with protein acetyltransferase activity. However, the relationship between HDAC6 and p300 is poorly understood. HDAC6 is a class II histone deacetylase and differs from other members of HDAC family in that it contains two HDAC domains and an ubiquitin-binding motif. HDAC6 is a microtubule-associated deacetylase. It predominantly deacetylates non-histone proteins, including α-tubulin, and regulates cell motility. Here, we report that p300 interacts with and acetylates HDAC6 resulting down-regulation of HDAC6 deacetylase activity. Furthermore, we provide evidences that acetylation of HDAC6 by p300 inhibits tubulin deacetylation and suppression of Sp1 transcriptional activity by HDAC6. Our results demonstrate that p300 can inactivate HDAC6 by acetylation, and that p300 may regulate the activity of Sp1 indirectly through HDAC6 in addition to its direct modification of Sp1. © 2009 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2009.03.147
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자연과학대학 > 생명과학전공 > Journal papers
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