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Journal article 1409 views

Control of growth factor receptor dynamics by reversible ubiquitination

J. McCullough, S. Urbé, P. Row, I.A. Prior, R. Welchman, M.J. Clague, Paula Row

Biochemical Society Transactions, Volume: 34, Issue: 5, Start page: 754

Swansea University Author: Paula Row

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DOI (Published version): 10.1042/BST0340754

Abstract

Activated tyrosine kinase receptors acquire ubiquitin tags. Ubiquitination governs receptor down-regulation through interaction with components of the endosomal ESCRT (endosomal sorting complexes required for transport) machinery that shepherds receptors into luminal vesicles of multivesicular bodie...

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Published in: Biochemical Society Transactions
Published: 2006
URI: https://cronfa.swan.ac.uk/Record/cronfa18385
first_indexed 2014-09-11T01:59:11Z
last_indexed 2018-02-09T04:52:57Z
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spelling 2014-09-10T14:47:51.9823595 v2 18385 2014-09-10 Control of growth factor receptor dynamics by reversible ubiquitination 99bb528b2f8fb62aabbdad101d53ba96 Paula Row Paula Row true false 2014-09-10 MEDS Activated tyrosine kinase receptors acquire ubiquitin tags. Ubiquitination governs receptor down-regulation through interaction with components of the endosomal ESCRT (endosomal sorting complexes required for transport) machinery that shepherds receptors into luminal vesicles of multivesicular bodies en route to the lysosome. We have characterized two de-ubiquitinating enzymes that interact with components of this machinery. AMSH [associated molecule with the SH3 domain (Src homology 3 domain) of STAM (signal transducing adapter molecule)] shows specificity for Lys63- over Lys48-linked ubiquitin and may act to rescue receptors from taking the lysosomal pathway. In contrast, UBPY (ubiquitin-specific processing protease Y) does not discriminate between Lys48 and Lys63-linked chains and is required for lysosomal sorting. Journal Article Biochemical Society Transactions 34 5 754 31 12 2006 2006-12-31 10.1042/BST0340754 COLLEGE NANME Medical School COLLEGE CODE MEDS Swansea University 2014-09-10T14:47:51.9823595 2014-09-10T14:47:51.9823595 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine J. McCullough 1 S. Urbé 2 P. Row 3 I.A. Prior 4 R. Welchman 5 M.J. Clague 6 Paula Row 7
title Control of growth factor receptor dynamics by reversible ubiquitination
spellingShingle Control of growth factor receptor dynamics by reversible ubiquitination
Paula Row
title_short Control of growth factor receptor dynamics by reversible ubiquitination
title_full Control of growth factor receptor dynamics by reversible ubiquitination
title_fullStr Control of growth factor receptor dynamics by reversible ubiquitination
title_full_unstemmed Control of growth factor receptor dynamics by reversible ubiquitination
title_sort Control of growth factor receptor dynamics by reversible ubiquitination
author_id_str_mv 99bb528b2f8fb62aabbdad101d53ba96
author_id_fullname_str_mv 99bb528b2f8fb62aabbdad101d53ba96_***_Paula Row
author Paula Row
author2 J. McCullough
S. Urbé
P. Row
I.A. Prior
R. Welchman
M.J. Clague
Paula Row
format Journal article
container_title Biochemical Society Transactions
container_volume 34
container_issue 5
container_start_page 754
publishDate 2006
institution Swansea University
doi_str_mv 10.1042/BST0340754
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
document_store_str 0
active_str 0
description Activated tyrosine kinase receptors acquire ubiquitin tags. Ubiquitination governs receptor down-regulation through interaction with components of the endosomal ESCRT (endosomal sorting complexes required for transport) machinery that shepherds receptors into luminal vesicles of multivesicular bodies en route to the lysosome. We have characterized two de-ubiquitinating enzymes that interact with components of this machinery. AMSH [associated molecule with the SH3 domain (Src homology 3 domain) of STAM (signal transducing adapter molecule)] shows specificity for Lys63- over Lys48-linked ubiquitin and may act to rescue receptors from taking the lysosomal pathway. In contrast, UBPY (ubiquitin-specific processing protease Y) does not discriminate between Lys48 and Lys63-linked chains and is required for lysosomal sorting.
published_date 2006-12-31T18:35:01Z
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score 11.04748

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