Parkin–phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity
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Title
Parkin–phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity
Authors
Keywords
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Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 24, Issue 5, Pages 475-483
Publisher
Springer Nature
Online
2017-04-17
DOI
10.1038/nsmb.3400
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Related references
Note: Only part of the references are listed.- Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
- (2016) Daniel C. Scott et al. CELL
- Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms
- (2016) Katja K Dove et al. EMBO REPORTS
- MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes
- (2016) Syed Arif Abdul Rehman et al. MOLECULAR CELL
- Structure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation
- (2016) Bernhard C. Lechtenberg et al. NATURE
- Structure of phosphorylated UBL domain and insights into PINK1-orchestrated parkin activation
- (2016) Jacob D. Aguirre et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Noncovalent Ubiquitin Interactions Regulate the Catalytic Activity of Ubiquitin Writers
- (2016) Joshua D. Wright et al. TRENDS IN BIOCHEMICAL SCIENCES
- Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin
- (2016) Eunju Im et al. Open Biology
- Parkin and PINK1 Patient iPSC-Derived Midbrain Dopamine Neurons Exhibit Mitochondrial Dysfunction and α-Synuclein Accumulation
- (2016) Sun Young Chung et al. Stem Cell Reports
- Activation of the E3 ubiquitin ligase Parkin
- (2015) Thomas R. Caulfield et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis
- (2015) A. Kumar et al. EMBO JOURNAL
- A Ubl/ubiquitin switch in the activation of Parkin
- (2015) V. Sauve et al. EMBO JOURNAL
- Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation
- (2015) A. Kazlauskaite et al. EMBO REPORTS
- Interaction between RING1 (R1) and the Ubiquitin-like (UBL) Domains Is Critical for the Regulation of Parkin Activity
- (2015) Su Jin Ham et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mechanism of phospho-ubiquitin-induced PARKIN activation
- (2015) Tobias Wauer et al. NATURE
- The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
- (2015) Michael Lazarou et al. NATURE
- Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy
- (2015) Alban Ordureau et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- RBR E3 ubiquitin ligases: new structures, new insights, new questions
- (2014) Donald E. Spratt et al. BIOCHEMICAL JOURNAL
- Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
- (2014) Agne Kazlauskaite et al. BIOCHEMICAL JOURNAL
- Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis
- (2014) T. Wauer et al. EMBO JOURNAL
- PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
- (2014) Lesley A. Kane et al. JOURNAL OF CELL BIOLOGY
- Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis
- (2014) Alban Ordureau et al. MOLECULAR CELL
- Ubiquitin is phosphorylated by PINK1 to activate parkin
- (2014) Fumika Koyano et al. NATURE
- Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin
- (2014) Thomas R. Caulfield et al. PLoS Computational Biology
- Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
- (2013) Xinde Zheng et al. CELL RESEARCH
- TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes
- (2013) Ian R Kelsall et al. EMBO JOURNAL
- Structure of the human Parkin ligase domain in an autoinhibited state
- (2013) Tobias Wauer et al. EMBO JOURNAL
- PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
- (2013) Michael Lazarou et al. JOURNAL OF CELL BIOLOGY
- The E3 Ligase Parkin Maintains Mitochondrial Integrity by Increasing Linear Ubiquitination of NEMO
- (2013) Anne Kathrin Müller-Rischart et al. MOLECULAR CELL
- Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP
- (2013) Benjamin Stieglitz et al. NATURE
- Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
- (2013) J.-F. Trempe et al. SCIENCE
- Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation Mechanism
- (2013) David M. Duda et al. STRUCTURE
- A molecular explanation for the recessive nature of parkin-linked Parkinson’s disease
- (2013) Donald E. Spratt et al. Nature Communications
- Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
- (2013) B.E. Riley et al. Nature Communications
- Regulation of Parkin E3 ubiquitin ligase activity
- (2012) Helen Walden et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
- (2012) Judith J Smit et al. EMBO JOURNAL
- Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences
- (2012) Nicole Exner et al. EMBO JOURNAL
- LUBAC synthesizes linear ubiquitin chains via a thioester intermediate
- (2012) Benjamin Stieglitz et al. EMBO REPORTS
- Mitochondrial Quality Control Mediated by PINK1 and Parkin: Links to Parkinsonism
- (2012) D. Narendra et al. Cold Spring Harbor Perspectives in Biology
- PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
- (2012) Kei Okatsu et al. Nature Communications
- PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
- (2012) Kahori Shiba-Fukushima et al. Scientific Reports
- PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
- (2012) C. Kondapalli et al. Open Biology
- Recent Advances in the Genetics of Parkinson's Disease
- (2011) Ian Martin et al. Annual Review of Genomics and Human Genetics
- Autoregulation of Parkin activity through its ubiquitin-like domain
- (2011) Viduth K Chaugule et al. EMBO JOURNAL
- SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
- (2011) Fuminori Tokunaga et al. NATURE
- UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
- (2011) Dawn M. Wenzel et al. NATURE
- Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations
- (2011) H. I. Woodroof et al. Open Biology
- The role of parkin in familial and sporadic Parkinson's disease
- (2010) Ted M. Dawson et al. MOVEMENT DISORDERS
- MolProbity: all-atom structure validation for macromolecular crystallography
- (2009) Vincent B. Chen et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Identification of a Novel Zn2+-binding Domain in the Autosomal Recessive Juvenile Parkinson-related E3 Ligase Parkin
- (2009) Ventzislava A. Hristova et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Involvement of linear polyubiquitylation of NEMO in NF-κB activation
- (2009) Fuminori Tokunaga et al. NATURE CELL BIOLOGY
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