Published February 11, 2005
| Version v1
Journal article
E1AF degradation by a ubiquitin-proteasome pathway
Creators
- 1. Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, North 13 West 7, Kita-ku 060-8586, Sapporo (Japan)
- 2. Department of Biology, Sapporo Medical University School of Medicine, South 1 West 17, Chuo-ku 060-8556, Sapporo (Japan)
- 3. Division of Cancer Pathobiology, Institute for Genetic Medicine, Hokkaido University, North 15 West 7, Kita-ku 060-0815, Sapporo (Japan)
Description
E1AF is a member of the ETS family of transcription factors. In mammary tumors, overexpression of E1AF is associated with tumorigenesis, but E1AF protein has hardly been detected and its degradation mechanism is not yet clear. Here we show that E1AF protein is stabilized by treatment with the 26S protease inhibitor MG132. We found that E1AF was modified by ubiquitin through the C-terminal region and ubiquitinated E1AF aggregated in nuclear dots, and that the inhibition of proteasome-activated transcription from E1AF target promoters. These results suggest that E1AF is degraded via the ubiquitin-proteasome pathway, which has some effect on E1AF function
Additional details
Identifiers
- DOI
- 10.1016/j.bbrc.2004.12.045;
- PII
- S0006-291X(04)02813-X;
Publishing Information
- Journal Title
- Biochemical and Biophysical Research Communications
- Journal Volume
- 327
- Journal Issue
- 2
- Journal Page Range
- p. 575-580
- ISSN
- 0006-291X
- CODEN
- BBRCA9
INIS
- Country of Publication
- United States
- Country of Input or Organization
- International Atomic Energy Agency (IAEA)
- INIS RN
- 36062887
- Subject category
- S60: APPLIED LIFE SCIENCES;
- Descriptors DEI
- BIOLOGICAL PATHWAYS; INHIBITION; NEOPLASMS; TRANSCRIPTION; TRANSCRIPTION FACTORS
- Descriptors DEC
- DISEASES; ORGANIC COMPOUNDS; PROTEINS
Optional Information
- Copyright
- Copyright (c) 2004 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.