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Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery

John McCullough, Paula Row, Óscar Lorenzo, Mary Doherty, Robert Beynon, Michael J. Clague, Sylvie Urbé

Current Biology, Volume: 16, Issue: 2, Pages: 160 - 165

Swansea University Author: Paula Row

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DOI (Published version): 10.1016/j.cub.2005.11.073

Abstract

AMSH is an endosomal ubiquitin isopeptidase that can limit EGF receptor downregulation [1]. It directly binds to the SH3 domain of STAM, which is constitutively associated with Hrs, a component of clathrin-coated structures on endosomes. This clathrin coat has been implicated in the recruitment of u...

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Published in: Current Biology
Published: 2006
Online Access: http://ac.els-cdn.com/S0960982205015241/1-s2.0-S0960982205015241-main.pdf?_tid=48af539c-38ef-11e4-949d-00000aab0f6c&acdnat=1410356289_96c0ae8c70550570797a00a792ca4c8b
URI: https://cronfa.swan.ac.uk/Record/cronfa18382
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spelling 2019-06-24T15:11:25.2402100 v2 18382 2014-09-10 Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery 99bb528b2f8fb62aabbdad101d53ba96 Paula Row Paula Row true false 2014-09-10 BMS AMSH is an endosomal ubiquitin isopeptidase that can limit EGF receptor downregulation [1]. It directly binds to the SH3 domain of STAM, which is constitutively associated with Hrs, a component of clathrin-coated structures on endosomes. This clathrin coat has been implicated in the recruitment of ubiquitinated growth factor receptors prior to their incorporation into internal vesicles of the multivesicular body (MVB) 2 and 3, through the concerted action of ESCRT complexes I, II, and III [4]. We now show that AMSH is embedded within a network of interactions with components of the MVB-sorting machinery. AMSH and STAM, like Hrs [5], both bind directly to clathrin. AMSH also interacts with mVps24/CHMP3, a component of ESCRT III complex, and this interaction is reinforced through simultaneous STAM binding. We have explored the effect of interacting components on the in vitro enzymatic activity of AMSH. The enzyme shows specificity for K63- over K48-linked polyubiquitin chains in vitro and is markedly stimulated by coincubation with STAM, indicating that activation of AMSH is coupled to its association with the MVB-sorting machinery. Other interacting factors do not directly stimulate AMSH but may serve to orient the enzyme with respect to substrates on the endosomal membrane. Journal Article Current Biology 16 2 160 165 CELLBIO; PROTEINS 24 1 2006 2006-01-24 10.1016/j.cub.2005.11.073 http://ac.els-cdn.com/S0960982205015241/1-s2.0-S0960982205015241-main.pdf?_tid=48af539c-38ef-11e4-949d-00000aab0f6c&amp;acdnat=1410356289_96c0ae8c70550570797a00a792ca4c8b COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2019-06-24T15:11:25.2402100 2014-09-10T14:36:11.9154389 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine John McCullough 1 Paula Row 2 Óscar Lorenzo 3 Mary Doherty 4 Robert Beynon 5 Michael J. Clague 6 Sylvie Urbé 7
title Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
spellingShingle Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
Paula Row
title_short Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
title_full Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
title_fullStr Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
title_full_unstemmed Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
title_sort Activation of the Endosome-Associated Ubiquitin Isopeptidase AMSH by STAM, a Component of the Multivesicular Body-Sorting Machinery
author_id_str_mv 99bb528b2f8fb62aabbdad101d53ba96
author_id_fullname_str_mv 99bb528b2f8fb62aabbdad101d53ba96_***_Paula Row
author Paula Row
author2 John McCullough
Paula Row
Óscar Lorenzo
Mary Doherty
Robert Beynon
Michael J. Clague
Sylvie Urbé
format Journal article
container_title Current Biology
container_volume 16
container_issue 2
container_start_page 160
publishDate 2006
institution Swansea University
doi_str_mv 10.1016/j.cub.2005.11.073
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
url http://ac.els-cdn.com/S0960982205015241/1-s2.0-S0960982205015241-main.pdf?_tid=48af539c-38ef-11e4-949d-00000aab0f6c&amp;acdnat=1410356289_96c0ae8c70550570797a00a792ca4c8b
document_store_str 0
active_str 0
description AMSH is an endosomal ubiquitin isopeptidase that can limit EGF receptor downregulation [1]. It directly binds to the SH3 domain of STAM, which is constitutively associated with Hrs, a component of clathrin-coated structures on endosomes. This clathrin coat has been implicated in the recruitment of ubiquitinated growth factor receptors prior to their incorporation into internal vesicles of the multivesicular body (MVB) 2 and 3, through the concerted action of ESCRT complexes I, II, and III [4]. We now show that AMSH is embedded within a network of interactions with components of the MVB-sorting machinery. AMSH and STAM, like Hrs [5], both bind directly to clathrin. AMSH also interacts with mVps24/CHMP3, a component of ESCRT III complex, and this interaction is reinforced through simultaneous STAM binding. We have explored the effect of interacting components on the in vitro enzymatic activity of AMSH. The enzyme shows specificity for K63- over K48-linked polyubiquitin chains in vitro and is markedly stimulated by coincubation with STAM, indicating that activation of AMSH is coupled to its association with the MVB-sorting machinery. Other interacting factors do not directly stimulate AMSH but may serve to orient the enzyme with respect to substrates on the endosomal membrane.
published_date 2006-01-24T03:21:33Z
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score 11.013148

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