HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions (Q24337173)

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23 December 2019

title

HD-PTP and Alix share some membrane-traffic related proteins that interact with their Bro1 domains or proline-rich regions (English)

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23 December 2019

5

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23 December 2019

author name string

Fumitaka Ichioka

1

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23 December 2019

Emi Takaya

2

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23 December 2019

Hironori Suzuki

3

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23 December 2019

Sachiko Kajigaya

4

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23 December 2019

Hideki Shibata

6

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23 December 2019

Masatoshi Maki

7

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23 December 2019

language of work or name

English

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publication date

17 November 2006

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Archives of Biochemistry and Biophysics

23 December 2019

published in

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23 December 2019

volume

457

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23 December 2019

page(s)

142-149

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23 December 2019

issue

2

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ALIX-ing phospholipids with endosome biogenesis

23 December 2019

cites work

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Expression analysis and modulation by HIV-Tat of the tyrosine phosphatase HD-PTP

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Cloning and characterization of a novel adaptor protein, CIN85, that interacts with c-Cbl

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HD-PTP: A novel protein tyrosine phosphatase gene on human chromosome 3p21.3

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ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner

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CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms

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Structural basis for endosomal targeting by the Bro1 domain

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Multiple domains of Ruk/CIN85/SETA/CD2BP3 are involved in interaction with p85alpha regulatory subunit of PI 3-kinase.

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Endosomal and non-endosomal functions of ESCRT proteins

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AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding

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The Protein Network of HIV Budding

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Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteins

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The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner

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Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors

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The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met

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A GTPase-activating protein controls Rab5 function in endocytic trafficking

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The biogenesis of multivesicular endosomes

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Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein

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Do Alix and ALG-2 really control endosomes for better or for worse?

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Cargo- and compartment-selective endocytic scaffold proteins

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The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4B

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

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A novel putative protein-tyrosine phosphatase contains a BRO1-like domain and suppresses Ha-ras-mediated transformation

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Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction

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7 January 2021

Peflin and ALG-2, members of the penta-EF-hand protein family, form a heterodimer that dissociates in a Ca2+-dependent manner

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7 January 2021

Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization

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7 January 2021

The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting

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7 January 2021

Identification of a novel proline-arginine motif involved in CIN85-dependent clustering of Cbl and down-regulation of epidermal growth factor receptors.

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Alix, a protein regulating endosomal trafficking, is involved in neuronal death.

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7 January 2021

Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities

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The glioma-associated protein SETA interacts with AIP1/Alix and ALG-2 and modulates apoptosis in astrocytes

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The penta-EF-hand protein ALG-2 interacts with a region containing PxY repeats in Alix/AIP1, which is required for the subcellular punctate distribution of the amino-terminal truncation form of Alix/AIP1

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Identifiers

DOI

2 references

Consolidated OpenCitations Corpus – April 2017

3865112

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17174262%20AND%20SRC:MED&resulttype=core&format=json

23 December 2019

3865112

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

2 references

3865112