The membrane‐proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin‐6 receptor and interleukin‐1 receptor II

IL‐6R physically interacts with ADAM17 by anti bait coimmunoprecipitation ( View interaction ) ADAM17 physically interacts with IL‐1RII by anti tag coimmunoprecipitation ( View interaction )

• Publication year

  2012

• Venue

  FEBS Letters

• Publication date

  2012-04-24

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/j.febslet.2012.03.012PMID 22575642
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• ADAM17: a molecular switch to control inflammation and tissue regeneration.

  2011cited by this paper
• Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain.

  2011cited by this paper
• A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17

  2011cited by this paper
• Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17.

  2011cited by this paper
• Cross-domain inhibition of TACE ectodomain

  2011cited by this paper
• Inhibitory role of TACE/ADAM17 cytotail in protein ectodomain shedding.

  2011cited by this paper
• Species Specificity of ADAM10 and ADAM17 Proteins in Interleukin-6 (IL-6) Trans-signaling and Novel Role of ADAM10 in Inducible IL-6 Receptor Shedding*

  2011cited by this paper
• Thiol isomerases negatively regulate the cellular shedding activity of ADAM17.

  2010cited by this paper
• Critical role of the disintegrin metalloprotease ADAM17 for intestinal inflammation and regeneration in mice

  2010cited by this paper
• Forced Homo- and Heterodimerization of All gp130-Type Receptor Complexes Leads to Constitutive Ligand-independent Signaling and Cytokine-independent Growth

  2010cited by this paper
• Three-dimensional domain architecture of the ADAM family proteinases.

  2009cited by this paper
• Cytoplasmic Relaxation of Active Eph Controls Ephrin Shedding by ADAM10

  2009cited by this paper
• Structural Characterization of the Ectodomain of a Disintegrin and Metalloproteinase-22 (ADAM22), a Neural Adhesion Receptor Instead of Metalloproteinase

  2009cited by this paper
• Regulation of Mature ADAM17 by Redox Agents for L-Selectin Shedding1

  2009cited by this paper
• Targeting ADAM10 to lipid rafts in neuroblastoma SH-SY5Y cells impairs amyloidogenic processing of the amyloid precursor protein.

  2009cited by this paper
• Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils.

  2007cited by this paper
• The transmembrane domain of TACE regulates protein ectodomain shedding

  2007cited by this paper
• The shedding activity of ADAM17 is sequestered in lipid rafts.

  2006cited by this paper
• Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold

  2006cited by this paper
• ERK-mediated phosphorylation of Thr735 in TNFα-converting enzyme and its potential role in TACE protein trafficking

  2005cited by this paper
• Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans.

  2005influential reference
• The tumor necrosis factor-alpha converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity.

  2002cited by this paper
• Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE).

  2000cited by this paper
• Shedding of interleukin-6 receptor and tumor necrosis factor alpha. Contribution of the stalk sequence to the cleavage pattern of transmembrane proteins.

  2000cited by this paper
• Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme.

  2000influential reference
• Cutting edge: a dominant negative form of TNF-alpha converting enzyme inhibits proTNF and TNFRII secretion.

  1999cited by this paper
• Specific Sequence Elements Are Required for the Expression of Functional Tumor Necrosis Factor-α-converting Enzyme (TACE)*

  1999cited by this paper
• An essential role for ectodomain shedding in mammalian development.

  1998cited by this paper
• A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

  1997cited by this paper
• Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

  1997cited by this paper
• A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells.

  1997cited by this paper
• Differential shedding of the two subunits of the interleukin‐6 receptor

  1993cited by this paper

• Critical Role of IL1R2‐ENO1 Interaction in Inhibiting Glycolysis‐Mediated Pyroptosis for Protection Against Lethal Sepsis

  2025cites this paper
• Progress of ADAM17 in Fibrosis-Related Diseases

  2025cites this paper
• Propolis Reduces Inflammation and Dyslipidemia Caused by High-Cholesterol Diet in Mice by Lowering ADAM10/17 Activities

  2024cites this paper
• S Protein, ACE2 and Host Cell Proteases in SARS-CoV-2 Cell Entry and Infectivity; Is Soluble ACE2 a Two Blade Sword? A Narrative Review

  2023cites this paper
• Diverse Control Mechanisms of the Interleukin-1 Cytokine Family

  2022influential citation
• A Disintegrin and Metalloproteinase (ADAM) Family—Novel Biomarkers of Selected Gastrointestinal (GI) Malignancies?

  2022cites this paper
• Identification of the extracellular metallo-endopeptidases ADAM and ADAMTS in the yellow fever mosquito Aedes aegypti.

  2022cites this paper
• Negative Regulation of the IL-1 System by IL-1R2 and IL-1R8: Relevance in Pathophysiology and Disease

  2022cites this paper
• IL-1α Processing, Signaling and Its Role in Cancer Progression

  2021cites this paper
• Lentiviral CRISPR-guided RNA library screening identified Adam17 as an upstream negative regulator of Procr in mammary epithelium

  2021cites this paper
• The role of ADAM17 during liver damage

  2021cites this paper
• Functionally confirmed compound heterozygous ADAM17 missense loss-of-function variants cause neonatal inflammatory skin and bowel disease 1

  2021cites this paper
• IL-1 Family Antagonists in Mouse and Human Skin Inflammation

  2021cites this paper
• ADAM-Mediated Signalling Pathways in Gastrointestinal Cancer Formation

  2020cites this paper
• Thiol switches in membrane proteins - Extracellular redox regulation in cell biology

  2020cites this paper
• Distance dependent shedding of IL-6R.

  2020cites this paper
• Follicular structures of cows with cystic ovarian disease present altered expression of cytokines

  2019cites this paper
• Functional Characterization of Colon Cancer-Associated Mutations in ADAM17: Modifications in the Pro-Domain Interfere with Trafficking and Maturation

  2019cites this paper
• The metalloprotease ADAM17 in inflammation and cancer.

  2019cites this paper
• A Disintegrin and Metalloproteinase 17 is required for ILC2 responses to IL-33.

  2019cites this paper
• Status update on iRhom and ADAM17: It's still complicated.

  2019cites this paper
• Could the inhibition of IL-17 or IL-18 be a potential therapeutic opportunity for gastric cancer?

  2018cites this paper
• Regulation of Immunity and Disease by the IL-1 Receptor Family Members IL-1R2 and IL-1R8

  2018cites this paper
• The EGFR-ADAM17 Axis in Chronic Obstructive Pulmonary Disease and Cystic Fibrosis Lung Pathology

  2018cites this paper
• Tuning inflammation and immunity by the negative regulators IL‐1R2 and IL‐1R8

  2018cites this paper
• The family of the interleukin‐1 receptors

  2018cites this paper
• Altered expression of IL-1β, IL-1RI, IL-1RII, IL-1RA and IL-4 could contribute to anovulation and follicular persistence in cattle.

  2018cites this paper
• Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17

  2018cites this paper
• Interleukin-1 Beta—A Friend or Foe in Malignancies?

  2018cites this paper
• GRP78 protects a disintegrin and metalloprotease 17 against protein‐disulfide isomerase A6 catalyzed inactivation

  2017cites this paper
• Molecular insights into the multilayered regulation of ADAM17: The role of the extracellular region.

  2017cites this paper
• Proteolytic Origin of the Soluble Human IL-6R In Vivo and a Decisive Role of N-Glycosylation

  2017cites this paper
• Cytokine Receptors and Their Ligands

  2016cites this paper
• The ADAMs family of proteases as targets for the treatment of cancer

  2016cites this paper
• Control of ADAM17 activity by regulation of its cellular localisation

  2016cites this paper
• ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview

  2016cites this paper
• Cytokine decoy and scavenger receptors as key regulators of immunity and inflammation.

  2016cites this paper
• Modulating Inflammatory Cytokines

  2016cites this paper
• Regulation und Transport der Disintegrin und Metalloproteinasen ADAM10 und ADAM17

  2016cites this paper
• Epigenetic and posttranslational regulation of the disintegrin and metalloproteases ADAM17 and ADAMTS-16

  2016cites this paper
• Staphylococcus aureus Induces Shedding of IL-1RII in Monocytes and Neutrophils

  2016cites this paper
• The interleukin (IL)-1 cytokine family--Balance between agonists and antagonists in inflammatory diseases.

  2015cites this paper
• 4. Metzincin Modulators

  2015cites this paper
• Secreted Frizzled-related protein 3 (sFRP3)-mediated suppression of interleukin-6 receptor release by A disintegrin and metalloprotease 17 (ADAM17) is abrogated in the osteoarthritis-associated rare double variant of sFRP3.

  2015cites this paper
• Meprin and ADAM Metalloproteases: Two Sides of the Same Coin?

  2015cites this paper
• Circulating ADAM17 Level Reflects Disease Activity in Proteinase-3 ANCA-Associated Vasculitis.

  2015cites this paper
• ADAM17 regulates IL-1 signaling by selectively releasing IL-1 receptor type 2 from the cell surface.

  2015cites this paper
• The IL-1 family in relation to psoriasis

  2014cites this paper
• A Disintegrin and Metalloprotease 17 Dynamic Interaction Sequence, the Sweet Tooth for the Human Interleukin 6 Receptor*

  2014cites this paper
• Compartimentation membranaire d’ADAM10 par les tétraspanines : conséquences pour la voie de signalisation NOTCH

  2014cites this paper
• T‐cell immunoglobulin and mucin domain 2 (TIM‐2) is a target of ADAM10‐mediated ectodomain shedding

  2014cites this paper
• IL-15.IL-15Rα complex shedding following trans-presentation is essential for the survival of IL-15 responding NK and T cells

  2014cites this paper
• Probiotic foods: Can their increasing use in India ameliorate the burden of chronic lifestyle disorders?

  2014cites this paper
• Interleukin-6: from basic biology to selective blockade of pro-inflammatory activities.

  2014cites this paper
• Differential Expression of Transcription Factors and Inflammation-, ROS-, and Cell Death-Related Genes in Organotypic Cultures in the Modiolus, the Organ of Corti and the Stria Vascularis of Newborn Rats

  2014cites this paper
• Interleukin-6 and its receptors: a highly regulated and dynamic system.

  2014cites this paper
• Die Rolle der Metalloprotease ADAM17 während der zellulären Seneszenz

  2014cites this paper
• The interleukin-1 receptor family.

  2013cites this paper
• The interleukin-1 family: back to the future.

  2013cites this paper
• ADAM17-overexpressing breast cancer cells selectively targeted by antibody–toxin conjugates

  2013cites this paper
• Negative regulatory receptors of the IL-1 family.

  2013cites this paper
• Minimal Interleukin 6 (IL-6) Receptor Stalk Composition for IL-6 Receptor Shedding and IL-6 Classic Signaling

  2013cites this paper
• Decoys and Regulatory “Receptors” of the IL-1/Toll-Like Receptor Superfamily

  2013cites this paper
• ADAM17, shedding, TACE as therapeutic targets.

  2013cites this paper
• The disintegrin domain of ADAM17 antagonises fibroblast‑carcinoma cell interactions.

  2013cites this paper
• Polo-like Kinase 2, a Novel ADAM17 Signaling Component, Regulates Tumor Necrosis Factor α Ectodomain Shedding*

  2013cites this paper
• Mouse neutrophils express the decoy type 2 interleukin‐1 receptor (IL‐1R2) constitutively and in acute inflammatory conditions

  2013cites this paper
• Polo-like kinase 2, a novel ADAM17 signaling component, regulates TNFα ectodomain shedding

  2013cites this paper
• Membrane-proximal domain of a disintegrin and metalloprotease-17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase.

  2013cites this paper
• The role of ADAM17 in metabolic inflammation.

  2013cites this paper
• Ectodomain shedding and ADAMs in development

  2012cites this paper
• A novel bispecific single-chain antibody for ADAM17 and CD3 induces T-cell-mediated lysis of prostate cancer cells.

  2012cites this paper