Acetylation of histone deacetylase 6 by p300 attenuates its deacetylase activity

Younho Han, Hyung Min Jeong, Yun Hye Jin, Yeon Jin Kim, Hye Gwang Jeong, Chang Yeol Yeo, Kwang Youl Lee

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42 Scopus citations


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.

Original languageEnglish
Pages (from-to)88-92
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - 22 May 2009

Bibliographical note

Funding Information:
This work was supported by a grant from the Korea Research Foundation Grant funded by the Korean Government (MOEHRD, Basic Research Promotion Fund; KRF-2006-311-E00120) to K.-Y. Lee. Y.-J. K is supported by the second stage of Brain Korea 21 Project.


  • Acetylation
  • HDAC6
  • Sp1
  • Tubulin
  • p300


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