Linear ubiquitination at a glance
Open accessAbstract
Ubiquitination (also known as ubiquitylation) is a post-translational modification that creates versatility in cell signalling and regulates a multitude of cellular processes. Its versatility lies in the capacity to form eight different inter-ubiquitin linkages through the seven lysine residues of ubiquitin and through its N-terminal methionine (M1). The latter, referred to as linear or M1 linkage, is created by the linear ubiquitin chain assembly complex (LUBAC), the only E3 ligase known to date that is capable of forming linear ubiquitin chains de novo. Linear ubiquitin chains are crucial modulators of innate and adaptive immune responses, and act by regulating inflammatory and cell death signalling. In this Cell Science at a Glance article and the accompanying poster, we review the current knowledge on the role of LUBAC and linear ubiquitination in immune signalling and human physiology. We specifically focus on the role for LUBAC in signalling that is induced by the cytokine tumour necrosis factor (TNF) and its role in inflammation, gene activation and cell death. Furthermore, we highlight the roles of deubiquitinases (DUBs) that cleave M1 linkages and add an additional layer in the control of LUBAC-mediated immune signalling.
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Two of the LUBAC's three complements are encoded by SHARPIN and RBCK1, and the LUBAC's function is directly regulated by OTULIN; SHARPIN, RBCK1 and OTULIN are new tier 1 prioritized genes in this study.
“Two of the LUBAC’s three complements are encoded by the new tier 1 prioritized genes SHARPIN and RBCK1, and the complex’s function is directly regulated by OTULIN (also a new tier 1 prioritized gene).”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [20]
The LUBAC has been studied as a regulator of TNF-α signaling.
“Lastly, the LUBAC has been studied as a regulator of TNF-α signaling in particular20.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [20]
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Self-citationOTULIN limits cell death and inflammation by deubiquitinating LUBAC
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Polyglucosan body myopathy caused by defective ubiquitin ligase RBCK1
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Self-citationStructures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity
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Self-citationMechanism Underlying IκB Kinase Activation Mediated by the Linear Ubiquitin Chain Assembly Complex
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SPATA2 promotes CYLD activity and regulates TNF‐induced NF‐κB signaling and cell death
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Self-citationActivation of p38mapk, MKK3, and MKK4 by TNF-alpha in mouse bone marrow-derived macrophages
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Self-citationHOIL-1L Interacting Protein (HOIP) Is Essential for CD40 Signaling
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A20: attractive without showing cleavage
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New insights into the genetic etiology of Alzheimer’s disease and related dementias
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K63 ubiquitination in immune signaling
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USP7 Is a Master Regulator of Genome Stability
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“Besides lysine residues, the N-terminal methionine of ubiquitin can also be ubiquitinated (Spit et al., 2019).”
BackgroundLinear Ubiquitin Chains: Cellular Functions and Strategies for Detection and Quantification
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The ubiquitin codes in cellular stress responses
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Insights in Post-Translational Modifications: Ubiquitin and SUMO
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The Role of Atypical Ubiquitin Chains in the Regulation of the Antiviral Innate Immune Response
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Non-proteolytic ubiquitylation in cellular signaling and human disease
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Specificity in Ubiquitination Triggered by Virus Infection
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The Molecular Basis of Ubiquitin-Conjugating Enzymes (E2s) as a Potential Target for Cancer Therapy
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RNF31 inhibition sensitizes tumors to bystander killing by innate and adaptive immune cells
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There is no gene for CVID — novel monogenetic causes for primary antibody deficiency
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The Ubiquitin Proteasome System in Genome Stability and Cancer
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Linear ubiquitination induces NEMO phase separation to activate NF-κB signaling
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K27-linked noncanonic ubiquitination in immune regulation
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Compound heterozygous variants in OTULIN are associated with fulminant atypical late‐onset ORAS
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Self-citationThe ubiquitin-proteasome system and learning-dependent synaptic plasticity – A 10 year update
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A Destiny for Degradation: Interplay between Cullin-RING E3 Ligases and Autophagy
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Activation and suppression of hematopoietic integrins in hemostasis and immunity
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Exploitation of the Host Ubiquitin System: Means by Legionella pneumophila
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Roles of Ubiquitination and Deubiquitination in Regulating Dendritic Cell Maturation and Function
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Regulation of FKBP51 and FKBP52 functions by post-translational modifications
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LUBAC-mediated linear ubiquitination in tissue homeostasis and disease
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Ubiquitin, SUMO, and Nedd8 as Therapeutic Targets in Cancer
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LUBAC enables tumor-promoting LTβ receptor signaling by activating canonical NF-κB
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Self-citationSex-Specific Linear Polyubiquitination Is a Critical Regulator of Contextual Fear Memory Formation
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The Impact of the Ubiquitin System in the Pathogenesis of Squamous Cell Carcinomas
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Fate of hematopoietic stem cells determined by Notch1 signaling (Review)
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Strategy for Development of Site-Specific Ubiquitin Antibodies
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SUMO conjugation regulates immune signalling
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Serine 165 phosphorylation of SHARPIN regulates the activation of NF-κB
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Repressive Control of Keratinocyte Cytoplasmic Inflammatory Signaling
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Emerging Roles of Non-proteolytic Ubiquitination in Tumorigenesis
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LUBAC: a new player in polyglucosan body disease
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Linear ubiquitination prevents lipodystrophy and obesity-associated metabolic syndrome
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Spatiotemporal Regulation of STING Activity by Linear Ubiquitination Governs Antiviral Immunity
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The Role of Protein Ubiquitination in the Onset and Progression of Sepsis
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- Authors
- Spit, M., Rieser, E., & Walczak, H.
- Affiliations
- University College London (GB)
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2019-01-15
- Volume
- 132
- Issue
- 2
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2910276590
- Cited by
- 94
- References
- 121
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 5 · 2023: 13 · 2022: 14 · 2021: 26 · 2020: 17 · 2019: 4
- FWCI
- 1.49
- Type
- journal article
- Language
- en
- Open access
- green
- discovery.ucl.ac.uk
- Locations
- Journal of Cell Science (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- Wellcome Trust (096831/Z/11/Z)
- European Research Council (294880)
- KWF Kankerbestrijding (BUIT 2015-7526)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Keywords
- linear ubiquitination, LUBAC, E3 ubiquitin ligase, deubiquitinase, inflammation, cell death signaling, innate immunity, adaptive immunity, gene activation
- MeSH terms
- Animals, Humans, Inflammation, Tumor Necrosis Factor-alpha, Signal Transduction, Cell Death, Ubiquitin, Ubiquitin-Protein Ligases, Ubiquitination
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