Cargando…

ADAM10 sheddase activation is controlled by cell membrane asymmetry

Dysregulation of the disintegrin-metalloproteinase ADAM10 may contribute to the development of diseases including tumorigenesis and Alzheimer’s disease. The mechanisms underlying ADAM10 sheddase activation are incompletely understood. Here, we show that transient exposure of the negatively charged p...

Descripción completa

Detalles Bibliográficos
Autores principales:	Bleibaum, Florian, Sommer, Anselm, Veit, Martin, Rabe, Björn, Andrä, Jörg, Kunzelmann, Karl, Nehls, Christian, Correa, Wilmar, Gutsmann, Thomas, Grötzinger, Joachim, Bhakdi, Sucharit, Reiss, Karina
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Oxford University Press 2019
Materias:	Original Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6927242/ https://www.ncbi.nlm.nih.gov/pubmed/30753537 http://dx.doi.org/10.1093/jmcb/mjz008

Ejemplares similares

How membrane asymmetry regulates ADAM17 sheddase function
por: Sommer, Anselm, et al.
Publicado: (2016)

Phosphatidylserine exposure is required for ADAM17 sheddase function
por: Sommer, Anselm, et al.
Publicado: (2016)

Influence of Anoctamin-4 and -9 on ADAM10 and ADAM17 Sheddase Function
por: Leitzke, Sinje, et al.
Publicado: (2022)

Mutagenesis of the ADAM17-phosphatidylserine–binding motif leads to embryonic lethality in mice
por: Veit, Martin, et al.
Publicado: (2019)

Role of ADAM10 and ADAM17 in Regulating CD137 Function
por: Seidel, Jana, et al.
Publicado: (2021)

Scramblases as Regulators of Proteolytic ADAM Function
por: Reiss, Karina, et al.
Publicado: (2022)

Extracellular sphingomyelinase activity impairs TNF-α-induced endothelial cell death via ADAM17 activation and TNF receptor 1 shedding
por: Sommer, Anselm, et al.
Publicado: (2017)

Identification of ADAM12 as a Novel Basigin Sheddase
por: Albrechtsen, Reidar, et al.
Publicado: (2019)

The sheddase ADAM10 is a potent modulator of prion disease
por: Altmeppen, Hermann C, et al.
Publicado: (2015)

ADAM10 Sheddase Activity is a Potential Lung-Cancer Biomarker
por: Yoneyama, Toshie, et al.
Publicado: (2018)

Ephrin-A1 and the sheddase ADAM12 are upregulated in COVID-19
por: Mendoza, Rachelle, et al.
Publicado: (2021)

Regulation of A disintegrin and metalloproteinase (ADAM) family sheddases ADAM10 and ADAM17: The emerging role of tetraspanins and rhomboids
por: Matthews, Alexandra L., et al.
Publicado: (2017)

Role of ADAM10 as a CD30 Sheddase in Classical Hodgkin Lymphoma
por: Hansen, Hinrich P., et al.
Publicado: (2020)

CD9 regulates keratinocyte migration by negatively modulating the sheddase activity of ADAM17
por: Liu, Jie, et al.
Publicado: (2019)

Breakdown of Phospholipid Asymmetry Triggers ADAM17-Mediated Rescue Events in Cells Undergoing Apoptosis
por: Sperrhacke, Maria, et al.
Publicado: (2023)

Modification of proteolytic activity matrix analysis (PrAMA) to measure ADAM10 and ADAM17 sheddase activities in cell and tissue lysates
por: Yoneyama, Toshie, et al.
Publicado: (2017)

Cleavage Site Localization Differentially Controls Interleukin-6 Receptor Proteolysis by ADAM10 and ADAM17
por: Riethmueller, Steffen, et al.
Publicado: (2016)

How to exploit stress-related immunity against Hodgkin’s lymphoma: Targeting ERp5 and ADAM sheddases
por: Poggi, Alessandro, et al.
Publicado: (2013)

The ADAM17 sheddase complex regulator iTAP/Frmd8 modulates inflammation and tumor growth
por: Badenes, Marina, et al.
Publicado: (2023)

FRMD8 promotes inflammatory and growth factor signalling by stabilising the iRhom/ADAM17 sheddase complex
por: Künzel, Ulrike, et al.
Publicado: (2018)

A structural model of the iRhom–ADAM17 sheddase complex reveals functional insights into its trafficking and activity
por: Kahveci-Türköz, Selcan, et al.
Publicado: (2023)

Shear stress activates ADAM10 sheddase to regulate Notch1 via the Piezo1 force sensor in endothelial cells
por: Caolo, Vincenza, et al.
Publicado: (2020)

The matrix metalloproteinase ADAM10 supports hepatitis C virus entry and cell-to-cell spread via its sheddase activity
por: Carriquí-Madroñal, Belén, et al.
Publicado: (2023)

Molecular Identification of a Malaria Merozoite Surface Sheddase
por: Harris, Philippa K, et al.
Publicado: (2005)

Legumain Functions as a Transient TrkB Sheddase
por: Holzner, Christoph, et al.
Publicado: (2023)

Specific ADAM10 inhibitors localize in exosome-like vesicles released by Hodgkin lymphoma and stromal cells and prevent sheddase activity carried to bystander cells
por: Tosetti, Francesca, et al.
Publicado: (2018)

Identification and Characterization of an HtrA Sheddase Produced by Coxiella burnetii
por: Osman, Ikram Omar, et al.
Publicado: (2023)

Targeting the Sheddase Activity of ADAM17 by an Anti-ADAM17 Antibody D1(A12) Inhibits Head and Neck Squamous Cell Carcinoma Cell Proliferation and Motility via Blockage of Bradykinin Induced HERs Transactivation
por: Huang, Yanchao, et al.
Publicado: (2014)

LRP1 shedding in human brain: roles of ADAM10 and ADAM17
por: Liu, Qiang, et al.
Publicado: (2009)

Design of Membrane Active Peptides Considering Multi-Objective Optimization for Biomedical Application
por: Röckendorf, Niels, et al.
Publicado: (2022)

System-wide vitreous proteome dissection reveals impaired sheddase activity in diabetic retinopathy
por: Alli-Shaik, Asfa, et al.
Publicado: (2022)

Influence of Membrane Asymmetry on OmpF Insertion, Orientation and Function
por: Donoghue, Annemarie, et al.
Publicado: (2023)

Control of ADAM17 activity by regulation of its cellular localisation
por: Lorenzen, Inken, et al.
Publicado: (2016)

Erratum: Control of ADAM17 activity by regulation of its cellular localisation
por: Lorenzen, Inken, et al.
Publicado: (2016)

Cellular sheddases are induced by Merkel cell polyomavirus small tumour antigen to mediate cell dissociation and invasiveness
por: Nwogu, Nnenna, et al.
Publicado: (2018)

The malaria parasite sheddase SUB2 governs host red blood cell membrane sealing at invasion
por: Collins, Christine R, et al.
Publicado: (2020)

Correction for Substrate Selectivity of Epidermal Growth Factor-Receptor Ligand Sheddases and their Regulation by Phorbol Esters and Calcium Influx
Publicado: (2010)

Immunization against a merozoite sheddase promotes multiple invasion of red blood cells and attenuates Plasmodium infection in mice
por: Smith, Ryan C, et al.
Publicado: (2014)

ADAM17-dependent signaling is required for oncogenic human papillomavirus entry platform assembly
por: Mikuličić, Snježana, et al.
Publicado: (2019)

MUC1-C nuclear localization drives invasiveness of renal cancer cells through a sheddase/gamma secretase dependent pathway
por: Bouillez, Audrey, et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_8ueanlgu4fo7d92hin2doj3f0d