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Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins

Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins

http://www.wikidata.org/entity/Q24658387

about

SERPINA2 is a novel gene with a divergent function from SERPINA1 Protein folding and quality control in the ER The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology New Concepts in Alpha-1 Antitrypsin Deficiency Disease Mechanisms.Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates.Neuroserpin polymers cause oxidative stress in a neuronal model of the dementia FENIB A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency.The endoplasmic reticulum (ER)-associated degradation system regulates aggregation and degradation of mutant neuroserpin.Tissue plasminogen activator-independent roles of neuroserpin in the central nervous system.Role of Drosophila EDEMs in the degradation of the alpha-1-antitrypsin Z variant.Therapeutic targeting of misfolding and conformational change in α1-antitrypsin deficiency.Why has it been so difficult to prove the efficacy of alpha-1-antitrypsin replacement therapy? Insights from the study of disease pathogenesis The aggregation-prone intracellular serpin SRP-2 fails to transit the ER in Caenorhabditis elegans.Activating transcription factor 6 limits intracellular accumulation of mutant α(1)-antitrypsin Z and mitochondrial damage in hepatoma cells.129-Derived Mouse Strains Express an Unstable but Catalytically Active DNA Polymerase Iota Variant A single-chain variable fragment intrabody prevents intracellular polymerization of Z α1-antitrypsin while allowing its antiproteinase activity SVIP regulates Z variant alpha-1 antitrypsin retro-translocation by inhibiting ubiquitin ligase gp78.Proteasomes, TAP, and endoplasmic reticulum-associated aminopeptidase associated with antigen processing control CD4+ Th cell responses by regulating indirect presentation of MHC class II-restricted cytoplasmic antigens Proteasome inhibition rescues clinically significant unstable variants of the mismatch repair protein Msh2.Interactions between N-linked glycosylation and polymerisation of neuroserpin within the endoplasmic reticulum UDP-glucose:glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum.The endoplasmic reticulum remains functionally connected by vesicular transport after its fragmentation in cells expressing Z-α1-antitrypsin.Endoplasmic reticulum polymers impair luminal protein mobility and sensitize to cellular stress in alpha1-antitrypsin deficiency An antibody that prevents serpin polymerisation acts by inducing a novel allosteric behaviour.Glycoprotein folding and quality-control mechanisms in protein-folding diseases α(1)-antitrypsin deficiency and inflammation.Unravelling the twists and turns of the serpinopathies.Aggrephagy: selective disposal of protein aggregates by macroautophagy.Endoplasmic reticulum and the unfolded protein response: dynamics and metabolic integration Serpins, immunity and autoimmunity: old molecules, new functions.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.Erdj3 Has an Essential Role for Z Variant Alpha-1-Antitrypsin Degradation.Aberrant disulphide bonding contributes to the ER retention of alpha1-antitrypsin deficiency variants.Increased ERK signalling promotes inflammatory signalling in primary airway epithelial cells expressing Z α1-antitrypsin Sterol metabolism regulates neuroserpin polymer degradation in the absence of the unfolded protein response in the dementia FENIB.Mechanisms underlying the cellular clearance of antitrypsin Z: lessons from yeast expression systems.A novel interaction between aging and ER overload in a protein conformational dementia.Proteostasis: a new therapeutic paradigm for pulmonary disease.Reactive centre loop mutants of α-1-antitrypsin reveal position-specific effects on intermediate formation along the polymerization pathway.Endoplasmic reticulum stress in the pathogenesis of fibrotic disease.

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P2860

Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins

http://www.wikidata.org/entity/Q24658387

description

2009 nî lūn-bûn

@nan

2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

name

Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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type

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

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JBC.M109.027102

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Journal of Biological Chemistry

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Endoplasmic reticulum-associat ...... e polymerogenic mutant serpins

@en

P2093

Damian C Crowther

http://www.w3.org/2001/XMLSchema#string

David A Lomas

http://www.w3.org/2001/XMLSchema#string

Heike Kroeger

http://www.w3.org/2001/XMLSchema#string

Ian MacLeod

http://www.w3.org/2001/XMLSchema#string

Juan Pérez

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of a serpin-protease complex shows inhibition by deformation

Characterization of an ERAD gene as VPS30/ATG6 reveals two alternative and functionally distinct protein quality control pathways: one for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ.

Alpha1-antitrypsin polymerization and the serpinopathies: pathobiology and prospects for therapy

Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

Signal integration in the endoplasmic reticulum unfolded protein response

ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly.

Familial dementia caused by polymerization of mutant neuroserpin

Conformational disease

Mutants of neuroserpin that cause dementia accumulate as polymers within the endoplasmic reticulum

ERAD: the long road to destruction

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22793-802

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scholarly article

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3660885

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10.1074/JBC.M109.027102

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34

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284

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Stefan J Marciniak

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2009-08-21T00:00:00Z

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26314238

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19549782

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endoplasmic reticulum

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2755687

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