The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells
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Title
The E3 ligase HOIL-1 catalyses ester bond formation between ubiquitin and components of the Myddosome in mammalian cells
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 116, Issue 27, Pages 13293-13298
Publisher
Proceedings of the National Academy of Sciences
Online
2019-06-18
DOI
10.1073/pnas.1905873116
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- RBR ligase–mediated ubiquitin transfer: a tale with many twists and turns
- (2018) Helen Walden et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
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- Cooperative Domain Formation by Homologous Motifs in HOIL-1L and SHARPIN Plays A Crucial Role in LUBAC Stabilization
- (2018) Hiroaki Fujita et al. Cell Reports
- LUBAC is essential for embryogenesis by preventing cell death and enabling haematopoiesis
- (2018) Nieves Peltzer et al. NATURE
- Coupled monoubiquitylation of the co–E3 ligase DCNL1 by Ariadne RBR E3 ubiquitin ligases promotes cullin-RING ligase complex remodeling
- (2018) Ian R. Kelsall et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Roles of the TRAF6 and Pellino E3 ligases in MyD88 and RANKL signaling
- (2017) Sam Strickson et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
- (2016) Daniel C. Scott et al. CELL
- The multifaceted role of the E3 ubiquitin ligase HOIL-1: beyond linear ubiquitination
- (2015) Lynn Elton et al. IMMUNOLOGICAL REVIEWS
- Linear ubiquitination in immunity
- (2015) Yutaka Shimizu et al. IMMUNOLOGICAL REVIEWS
- An unexpected twist to the activation of IKKβ: TAK1 primes IKKβ for activation by autophosphorylation
- (2014) Jiazhen Zhang et al. BIOCHEMICAL JOURNAL
- Protein kinase IKKβ-catalyzed phosphorylation of IRF5 at Ser462 induces its dimerization and nuclear translocation in myeloid cells
- (2014) Marta Lopez-Pelaez et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Screening of DUB activity and specificity by MALDI-TOF mass spectrometry
- (2014) Maria Stella Ritorto et al. Nature Communications
- OTULIN Antagonizes LUBAC Signaling by Specifically Hydrolyzing Met1-Linked Polyubiquitin
- (2013) Kirstin Keusekotten et al. CELL
- Non-canonical ubiquitylation: Mechanisms and consequences
- (2013) Gary S. McDowell et al. INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY
- Target Specificity of the E3 Ligase LUBAC for Ubiquitin and NEMO Relies on Different Minimal Requirements
- (2013) Judith J. Smit et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- OTULIN Restricts Met1-Linked Ubiquitination to Control Innate Immune Signaling
- (2013) Berthe Katrine Fiil et al. MOLECULAR CELL
- The linear ubiquitin-specific deubiquitinase gumby regulates angiogenesis
- (2013) Elena Rivkin et al. NATURE
- Activation of the canonical IKK complex by K63/M1-linked hybrid ubiquitin chains
- (2013) C. H. Emmerich et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- 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
- LUBAC synthesizes linear ubiquitin chains via a thioester intermediate
- (2012) Benjamin Stieglitz et al. EMBO REPORTS
- SHARPIN is a component of the NF-κB-activating linear ubiquitin chain assembly complex
- (2011) Fuminori Tokunaga et al. NATURE
- SHARPIN forms a linear ubiquitin ligase complex regulating NF-κB activity and apoptosis
- (2011) Fumiyo Ikeda et al. NATURE
- Linear ubiquitination prevents inflammation and regulates immune signalling
- (2011) Björn Gerlach et al. NATURE
- Ubiquitination of Substrates by Esterification
- (2011) Xiaoli Wang et al. TRAFFIC
- Helical assembly in the MyD88–IRAK4–IRAK2 complex in TLR/IL-1R signalling
- (2010) Su-Chang Lin et al. NATURE
- Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-κB Activation
- (2009) Simin Rahighi et al. CELL
- An Oligomeric Signaling Platform Formed by the Toll-like Receptor Signal Transducers MyD88 and IRAK-4
- (2009) Precious G. Motshwene et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural Basis for Recognition of Diubiquitins by NEMO
- (2009) Yu-Chih Lo et al. MOLECULAR CELL
- Direct activation of protein kinases by unanchored polyubiquitin chains
- (2009) Zong-Ping Xia et al. NATURE
- Involvement of linear polyubiquitylation of NEMO in NF-κB activation
- (2009) Fuminori Tokunaga et al. NATURE CELL BIOLOGY
- E2 interaction and dimerization in the crystal structure of TRAF6
- (2009) Qian Yin et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Identification of the phosphorylation sites on the E3 ubiquitin ligase Pellino that are critical for activation by IRAK1 and IRAK4
- (2009) H. Smith et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Identification of Ubiquitin Ligase Activity of RBCK1 and Its Inhibition by Splice Variant RBCK2 and Protein Kinase Cβ
- (2008) Kenji Tatematsu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The IRAK-catalysed activation of the E3 ligase function of Pellino isoforms induces the Lys63-linked polyubiquitination of IRAK1
- (2007) Alban Ordureau et al. BIOCHEMICAL JOURNAL
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