Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3. - Wikidata - awgldk - TriplyDB

Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3.

Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3.

http://www.wikidata.org/entity/Q40393907

about

Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3 Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3 Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3 Efficient protection and isolation of ubiquitylated proteins using tandem ubiquitin-binding entities Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation Ataxin-3 is a multivalent ligand for the parkin Ubl domain The ubiquitin proteasome system in neuropathology Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein Trinucleotide repeats: a structural perspective Histone acetylation, acetyltransferases, and ataxia--alteration of histone acetylation and chromatin dynamics is implicated in the pathogenesis of polyglutamine-expansion disorders Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila.Allele-specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado-Joseph disease.Ataxin-3 promotes genome integrity by stabilizing Chk1.Ataxin-3 plays a role in mouse myogenic differentiation through regulation of integrin subunit levels Structural transformation of the tandem ubiquitin-interacting motifs in ataxin-3 and their cooperative interactions with ubiquitin chains.Splice isoforms of the polyglutamine disease protein ataxin-3 exhibit similar enzymatic yet different aggregation properties.Axonal inclusions in spinocerebellar ataxia type 3.Trehalose improves human fibroblast deficits in a new CHIP-mutation related ataxia.Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117.Ubiquitin-binding site 2 of ataxin-3 prevents its proteasomal degradation by interacting with Rad23 Dominant negative effect of polyglutamine expansion perturbs normal function of ataxin-3 in neuronal cells.Toward understanding Machado-Joseph disease Ataxin-3 regulates aggresome formation of copper-zinc superoxide dismutase (SOD1) by editing K63-linked polyubiquitin chains.Ataxin-3 phosphorylation decreases neuronal defects in spinocerebellar ataxia type 3 models Machado-Joseph disease/spinocerebellar ataxia type 3.JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis Strategies for the identification of novel inhibitors of deubiquitinating enzymes.Aggregation of polyglutamine-expanded ataxin-3 sequesters its specific interacting partners into inclusions: implication in a loss-of-function pathology.Regulation of proteolysis by human deubiquitinating enzymes.Ataxin-3 protein and RNA toxicity in spinocerebellar ataxia type 3: current insights and emerging therapeutic strategies.Polyglutamine (PolyQ) diseases: genetics to treatments.The UBA-UIM domains of the USP25 regulate the enzyme ubiquitination state and modulate substrate recognition.The deubiquitinating enzyme ataxin-3, a polyglutamine disease protein, edits Lys63 linkages in mixed linkage ubiquitin chains.Striatal and nigral pathology in a lentiviral rat model of Machado-Joseph disease.Cellular turnover of the polyglutamine disease protein ataxin-3 is regulated by its catalytic activity.p45, an ATPase subunit of the 19S proteasome, targets the polyglutamine disease protein ataxin-3 to the proteasome.Ataxin-3 consolidates the MDC1-dependent DNA double-strand break response by counteracting the SUMO-targeted ubiquitin ligase RNF4.Deregulation of autophagy in postmortem brains of Machado-Joseph disease patients.Identification of a novel site of interaction between ataxin-3 and the amyloid aggregation inhibitor polyglutamine binding peptide 1.

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P2860

Defining the role of ubiquitin-interacting motifs in the polyglutamine disease protein, ataxin-3.

http://www.wikidata.org/entity/Q40393907

description

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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Defining the role of ubiquitin ...... ine disease protein, ataxin-3.

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Defining the role of ubiquitin ...... ine disease protein, ataxin-3.

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Defining the role of ubiquitin ...... ine disease protein, ataxin-3.

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Ginger L Marrs

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Henry L Paulson

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Hsiang Wen

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Sarah J Shoesmith Berke

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Yaohui Chai

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P2860

The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis

Structure and ubiquitin binding of the ubiquitin-interacting motif

Non-traditional functions of ubiquitin and ubiquitin-binding proteins

Deubiquitinating enzymes--the importance of driving in reverse along the ubiquitin-proteasome pathway

Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities

Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature

Themes and variations on ubiquitylation

Structural modeling of ataxin-3 reveals distant homology to adaptins

CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1

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32026-32034

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10.1074/JBC.M506084200

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36

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280

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