Format:
Online-Ressource
ISSN:
1460-2075
Content:
Transcriptional repression mediated through histone deacetylation is a critical component of eukaryotic gene regulation. Here we demonstrate that the class II histone deacetylase HDAC4 is covalently modified by the ubiquitin‐related SUMO‐1 modifier. A sumoylation‐deficient point mutant (HDAC4‐K559R) shows a slightly impaired ability to repress transcription as well as reduced histone deacetylase activity. The ability of HDAC4 to self‐aggregate is a prerequisite for proper sumoylation in vivo. Calcium/calmodulin‐dependent protein kinase (CaMK) signalling, which induces nuclear export, abrogates SUMO‐1 modification of HDAC4. Moreover, the modification depends on the presence of an intact nuclear localization signal and is catalysed by the nuclear pore complex (NPC) RanBP2 protein, a factor newly identified as a SUMO E3 ligase. These findings suggest that sumoylation of HDAC4 takes place at the NPC and is coupled to its nuclear import. Finally, modification experiments indicate that the MEF2‐interacting transcription repressor (MITR) as well as HDAC1 and ‐6 are similarly SUMO modified, indicating that sumoylation may be an important regulatory mechanism for the control of transcriptional repression mediated by both class I and II HDACs.
In:
volume:21
In:
number:11
In:
year:2002
In:
pages:2682-2691
In:
extent:10
In:
European Molecular Biology Organization, The EMBO journal, [London] : Nature Publishing Group UK, 1982-, 21, Heft 11 (2002), 2682-2691 (gesamt 10), 1460-2075
Language:
English
DOI:
10.1093/emboj/21.11.2682
URN:
urn:nbn:de:101:1-2023110304085293036538
URL:
https://doi.org/10.1093/emboj/21.11.2682
URL:
https://nbn-resolving.org/urn:nbn:de:101:1-2023110304085293036538
URL:
https://d-nb.info/1308422628/34
URL:
https://doi.org/10.1093/emboj/21.11.2682
Bookmarklink