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Insights into the activation mechanism of class I HDAC complexes by inositol phosphates

Abstract:

Histone deacetylases (HDACs) 1, 2 and 3 form the catalytic subunit of several large transcriptional repression complexes. Unexpectedly, the enzymatic activity of HDACs in these complexes has been shown to be regulated by inositol phosphates, which bind in a pocket sandwiched between the HDAC and co-repressor proteins. However, the actual mechanism of activation remains poorly understood. Here we have elucidated the stereochemical requirements for binding and activation by inositol phosphates,...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/ncomms11262

Authors


More from this funder
Name:
Wellcome Trust
Funding agency for:
Potter, B
Grant:
WT101010
WT085408
WT100237toJ.W.R.S.,WT082837toA.M.R
B.V.L.P
WT101010toB.V.L.P
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
BB/N002954/1toS.M.C
BB/J009598/1
Publisher:
Nature Publishing Group
Journal:
Nature Communications More from this journal
Volume:
7
Article number:
11262
Publication date:
2016-01-01
Acceptance date:
2016-03-07
DOI:
ISSN:
2041-1723
Pubs id:
pubs:613760
UUID:
uuid:f405c161-59a6-4617-a956-46e3933d2936
Local pid:
pubs:613760
Source identifiers:
613760
Deposit date:
2016-04-05

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