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The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock

The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock
The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock
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.
bag-1, ires, translation, internal ribosome entry, heat shock
0950-9232
4095-4100
Coldwell, Mark J.
485e308e-b1ac-4bd3-8cd3-542cf8ba05d8
deSchoolmeester, Matthew L.
81ba21ea-a99b-47c8-adcd-752a34b7bdce
Fraser, Graham A.
baa762aa-6899-4782-8d38-9f30c82e025b
Pickering, Becky M.
94be5c5d-f45f-4baf-a5e9-6b7bfc16be25
Packham, Graham
fdabe56f-2c58-469c-aadf-38878f233394
Willis, Anne E.
70657c98-607d-4626-8bdf-1468e8653f98
Coldwell, Mark J.
485e308e-b1ac-4bd3-8cd3-542cf8ba05d8
deSchoolmeester, Matthew L.
81ba21ea-a99b-47c8-adcd-752a34b7bdce
Fraser, Graham A.
baa762aa-6899-4782-8d38-9f30c82e025b
Pickering, Becky M.
94be5c5d-f45f-4baf-a5e9-6b7bfc16be25
Packham, Graham
fdabe56f-2c58-469c-aadf-38878f233394
Willis, Anne E.
70657c98-607d-4626-8bdf-1468e8653f98

Coldwell, Mark J., deSchoolmeester, Matthew L., Fraser, Graham A., Pickering, Becky M., Packham, Graham and Willis, Anne E. (2001) The p36 isoform of BAG-1 is translated by internal ribosome entry following heat shock. Oncogene, 20 (30), 4095-4100.

Record type: Article

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.

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More information

Published date: 2001
Keywords: bag-1, ires, translation, internal ribosome entry, heat shock

Identifiers

Local EPrints ID: 26253
URI: https://eprints.soton.ac.uk/id/eprint/26253
ISSN: 0950-9232
PURE UUID: c4400eb2-de3a-42d7-b15e-ea278a48e975
ORCID for Graham Packham: ORCID iD orcid.org/0000-0002-9232-5691

Catalogue record

Date deposited: 21 Apr 2006
Last modified: 17 Jul 2019 01:02

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