Structure of parkin reveals mechanisms for ubiquitin ligase activation - Test2 - elhamkhani - TriplyDB

Structure of parkin reveals mechanisms for ubiquitin ligase activation

Structure of parkin reveals mechanisms for ubiquitin ligase activation

http://www.wikidata.org/entity/Q27684576

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Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65 Ubiquitin is phosphorylated by PINK1 to activate parkin Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis Hexokinase activity is required for recruitment of parkin to depolarized mitochondria Ataxin-3 is a multivalent ligand for the parkin Ubl domain TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes Ubiquitin modifications Linking F-box protein 7 and parkin to neuronal degeneration in Parkinson's disease (PD)Cross Talk of Proteostasis and Mitostasis in Cellular Homeodynamics, Ageing, and Disease Ubiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatment Parkin Regulation and Neurodegenerative Disorders Expanding the ubiquitin code through post-translational modification Regulating the Regulators: Recent Revelations in the Control of E3 Ubiquitin Ligases RBR E3 ubiquitin ligases: new structures, new insights, new questions The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications PINK1 and Parkin – mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease Parkin structure and function Pathologic and therapeutic implications for the cell biology of parkin Self and nonself: how autophagy targets mitochondria and bacteria Parkin Regulates Mitosis and Genomic Stability through Cdc20/Cdh1.Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering Cell-permeable parkin proteins suppress Parkinson disease-associated phenotypes in cultured cells and animals Phosphorylation by PINK1 releases the UBL domain and initializes the conformational opening of the E3 ubiquitin ligase Parkin Activation of the E3 ubiquitin ligase Parkin.Structure of the human Parkin ligase domain in an autoinhibited state Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP Mechanism and disease association of E2-conjugating enzymes: lessons from UBE2T and UBE2L3 Molecular basis for specificity of the Met1-linked polyubiquitin signal Targeting Pink1-Parkin-mediated mitophagy for treating liver injury Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control Perilous journey: a tour of the ubiquitin-proteasome system Probes of ubiquitin E3 ligases enable systematic dissection of parkin activation Structural insights into Parkin substrate lysine targeting from minimal Miro substrates PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity Incorporating modeling and simulations in undergraduate biophysical chemistry course to promote understanding of structure-dynamics-function relationships in proteins.Site-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation.Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation.Quantitative proteomic analysis of Parkin substrates in Drosophila neurons.Structural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.

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P2860

Structure of parkin reveals mechanisms for ubiquitin ligase activation

http://www.wikidata.org/entity/Q27684576

description

2013 nî lūn-bûn

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2013 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2013 թվականի հունիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Structure of parkin reveals mechanisms for ubiquitin ligase activation

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type

label

Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Structure of parkin reveals mechanisms for ubiquitin ligase activation

@en

Structure of parkin reveals mechanisms for ubiquitin ligase activation

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prefLabel

Structure of parkin reveals mechanisms for ubiquitin ligase activation

@ast

Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Structure of parkin reveals mechanisms for ubiquitin ligase activation

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Bhushan Nagar

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Jean-François Trempe

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Jonathan Krett

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Karl Grenier

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Kathy Wong

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Marie Ménade

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Marjan Seirafi

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Matthew Y Tang

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Sameer Al-Abdul-Wahid

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Véronique Sauvé

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P2860

PINK1 is selectively stabilized on impaired mitochondria to activate Parkin

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

LUBAC synthesizes linear ubiquitin chains via a thioester intermediate

PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

Phosphorylation by the c-Abl protein tyrosine kinase inhibits parkin's ubiquitination and protective function

UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids

Autoregulation of Parkin activity through its ubiquitin-like domain

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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6139

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340

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Guennadi Kozlov

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236675747

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