The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation (Q24337922)

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English	The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation	scientific article

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scholarly article

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The MIT domain of UBPY constitutes a CHMP binding and endosomal localization signal required for efficient epidermal growth factor receptor degradation (English)

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object named as

Han Liu

2

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object named as

Sylvie Urbé

9

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Michael J. Clague

object named as

Michael J Clague

7

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author name string

Paula E Row

1

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Sebastian Hayes

3

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Rebecca Welchman

4

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Panagoula Charalabous

5

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Kay Hofmann

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Christopher M Sanderson

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language of work or name

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publication date

19 October 2007

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Journal of Biological Chemistry

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282

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42

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30929-37

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The role of ubiquitylation in signaling by growth factors: implications to cancer

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Endocytosis and cancer.

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Regulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins

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Ubiquitin and endocytic protein sorting

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Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins

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Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes

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Bilayered clathrin coats on endosomal vacuoles are involved in protein sorting toward lysosomes

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Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes

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CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and functions in the endosomal sorting pathway

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A family of small coiled-coil-forming proteins functioning at the late endosome in yeast

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A genomic and functional inventory of deubiquitinating enzymes

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A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP

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AMSH is an endosome-associated ubiquitin isopeptidase

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Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII

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The ubiquitin isopeptidase UBPY regulates endosomal ubiquitin dynamics and is essential for receptor down-regulation

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https://api.crossref.org/works/10.1074%2FJBC.M704009200

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A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes

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UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation

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The mouse SKD1, a homologue of yeast Vps4p, is required for normal endosomal trafficking and morphology in mammalian cells

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Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates

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The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function

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A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex

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Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo

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Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.

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The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia

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Identification of mammalian Vps24p as an effector of phosphatidylinositol 3,5-bisphosphate-dependent endosome compartmentalization

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A protein interaction framework for human mRNA degradation

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Growth factors induce differential phosphorylation profiles of the Hrs-STAM complex: a common node in signalling networks with signal-specific properties

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Endosomal dynamics of Met determine signaling output

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Activation of the endosome-associated ubiquitin isopeptidase AMSH by STAM, a component of the multivesicular body-sorting machinery

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Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes

1 reference

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The hereditary spastic paraplegia protein spastin interacts with the ESCRT-III complex-associated endosomal protein CHMP1B.

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AMSH, an ESCRT-III associated enzyme, deubiquitinates cargo on MVB/late endosomes

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UBPY: a growth-regulated human ubiquitin isopeptidase.

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A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function

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Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies

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Membrane Transport: A Coat for Ubiquitin

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The Vps27p Hse1p complex binds ubiquitin and mediates endosomal protein sorting.

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7 January 2021

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Identifiers

10.1074/JBC.M704009200

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Consolidated OpenCitations Corpus – April 2017

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1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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