Published January 16, 2009
| Version v1
Journal article
SUMOylation of RORα potentiates transcriptional activation function
Creators
- 1. Department of Biological Sciences, Research Center for Women's Disease, Sookmyung Women's University, 52 Hyochangwon-gil, Yongsan-gu, Seoul 140-742 (Korea, Republic of)
- 2. Department of Biological Sciences, Seoul National University, Seoul 151-742 (Korea, Republic of)
- 3. Department of Medical Sciences, Inha University, Incheon 402-751 (Korea, Republic of)
Description
SUMOylation regulates a variety of cellular processes, including control of transcriptional activities of nuclear receptors. Here, we present SUMOylation of orphan nuclear receptor, RORα by both SUMO-1 and SUMO-2. SUMOylation of RORα occurred on the 240th lysine residue at the hinge region of human protein. PIAS family members, PIASxα, PIAS3, and PIASy, increased SUMOylation of RORα, whereas SENP2 specifically removed SUMO from RORα. SUMOylation-defective mutant form of RORα exhibited decreased transcriptional activity on RORα-responsive promoters indicating that SUMOylation may positively regulate transcriptional function of RORα.
Availability note (English)
Available from http://dx.doi.org/10.1016/j.bbrc.2008.11.072Additional details
Identifiers
- DOI
- 10.1016/j.bbrc.2008.11.072;
- PII
- S0006-291X(08)02271-7;
Publishing Information
- Journal Title
- Biochemical and Biophysical Research Communications
- Journal Volume
- 378
- Journal Issue
- 3
- Journal Page Range
- p. 513-517
- ISSN
- 0006-291X
- CODEN
- BBRCA9
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 41006429
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- HUMAN POPULATIONS; LEUKEMIA; LYSINE; MUTANTS; PROMOTERS; RECEPTORS; RETINOIC ACID
- Descriptors DEC
- AMINO ACIDS; CARBOXYLIC ACID ESTERS; CARBOXYLIC ACIDS; DISEASES; ESTERS; IMMUNE SYSTEM DISEASES; MEMBRANE PROTEINS; NEOPLASMS; ORGANIC ACIDS; ORGANIC COMPOUNDS; POPULATIONS; PROTEINS
Optional Information
- Copyright
- Copyright (c) 2008 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.