Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/18009
Title: The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock.
Authors: Coldwell, MJ
deSchoolmeester, ML
Fraser, GA
Pickering, BM
Packham, G
Willis, AE
First Published: 5-Jul-2001
Citation: ONCOGENE, 2001, 20 (30), pp. 4095-4100
Abstract: BAG-1 (also known as RAP46/HAP46) was originally identified as a 46 kDa protein that bound to and enhanced the anti-apoptotic properties of Bcl-2. BAG-1 exists as three major isoforms (designated p50, p46 and p36 or BAG-1L, BAG-1M and BAG-1S respectively) and one minor isoform (p29), which are translated from a common transcript. The differing amino terminus determines both the intracellular location and the repertoire of binding partners of the isoforms which play different roles in a variety of cellular processes including signal transduction, heat shock, apoptosis and transcription. Although in vitro data suggest that the four BAG-1 isoforms are translated by leaky scanning, the patterns of isoform expression in vivo, especially in transformed cells, do not support this hypothesis. We have performed in vivo analysis of the BAG-1 5' untranslated region and shown that translation initiation of the most highly expressed isoform (p36/BAG-1S) can occur by both internal ribosome entry and cap-dependent scanning. Following heat shock, when there is a downregulation of cap-dependent translation, the expression of the p36 isoform of BAG-1 is maintained by internal ribosome entry.
DOI Link: 10.1038/sj.onc.1204547
ISSN: 0950-9232
Links: http://hdl.handle.net/2381/18009
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.


Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.