Analysis of the Conditions That Affect the Selective Processing of Endogenous Notch1 by ADAM10 and ADAM17.


Journal

International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791

Informations de publication

Date de publication:
12 Feb 2021
Historique:
received: 21 01 2021
revised: 10 02 2021
accepted: 10 02 2021
entrez: 6 3 2021
pubmed: 7 3 2021
medline: 16 4 2021
Statut: epublish

Résumé

Notch signaling is critical for controlling a variety of cell fate decisions during metazoan development and homeostasis. This unique, highly conserved signaling pathway relies on cell-to-cell contact, which triggers the proteolytic release of the cytoplasmic domain of the membrane-anchored transcription factor Notch from the membrane. A disintegrin and metalloproteinase (ADAM) proteins are crucial for Notch activation by processing its S2 site. While ADAM10 cleaves Notch1 under physiological, ligand-dependent conditions, ADAM17 mainly cleaves Notch1 under ligand-independent conditions. However, the mechanism(s) that regulate the distinct contributions of these ADAMs in Notch processing remain unclear. Using cell-based assays in mouse embryonic fibroblasts (mEFs) lacking ADAM10 and/or ADAM17, we aimed to clarify what determines the relative contributions of ADAM10 and ADAM17 to ligand-dependent or ligand-independent Notch processing. We found that EDTA-stimulated ADAM17-dependent Notch1 processing is rapid and requires the ADAM17-regulators iRhom1 and iRhom2, whereas the Delta-like 4-induced ligand-dependent Notch1 processing is slower and requires ADAM10. The selectivity of ADAM17 for EDTA-induced Notch1 processing can most likely be explained by a preference for ADAM17 over ADAM10 for the Notch1 cleavage site and by the stronger inhibition of ADAM10 by EDTA. The physiological ADAM10-dependent processing of Notch1 cannot be compensated for by ADAM17 in

Identifiants

pubmed: 33673337
pii: ijms22041846
doi: 10.3390/ijms22041846
pmc: PMC7918056
pii:
doi:

Substances chimiques

Membrane Proteins 0
Notch1 protein, mouse 0
Receptor, Notch1 0
Amyloid Precursor Protein Secretases EC 3.4.-
ADAM10 Protein EC 3.4.24.81
Adam10 protein, mouse EC 3.4.24.81
ADAM17 Protein EC 3.4.24.86
Adam17 protein, mouse EC 3.4.24.86

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NIH HHS
ID : R01 GM64750
Pays : United States
Organisme : NIH HHS
ID : T32 GM007739
Pays : United States
Organisme : NIH HHS
ID : T32EY00713820
Pays : United States
Organisme : NIH HHS
ID : T32HD606006
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM134907
Pays : United States
Organisme : NIH HHS
ID : F31 GM136144
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008539
Pays : United States
Organisme : NIH HHS
ID : T32 GM008539
Pays : United States
Organisme : NIH HHS
ID : R35 GM134907
Pays : United States

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Auteurs

Rolake O Alabi (RO)

Tri-Institutional MD/PhD Program, Memorial Sloan-Kettering Cancer Center, Weill Cornell Medicine, Rockefeller University, New York, NY 10021, USA.
Arthritis and Tissue Degeneration Program, Hospital for Special Surgery, New York, NY 10021, USA.

Jose Lora (J)

Arthritis and Tissue Degeneration Program, Hospital for Special Surgery, New York, NY 10021, USA.
Department of Physiology, Biophysics and Systems Biology, Weill Cornell Medicine, New York, NY 10021, USA.

Arda B Celen (AB)

Arthritis and Tissue Degeneration Program, Hospital for Special Surgery, New York, NY 10021, USA.

Thorsten Maretzky (T)

Inflammation Program and Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.

Carl P Blobel (CP)

Tri-Institutional MD/PhD Program, Memorial Sloan-Kettering Cancer Center, Weill Cornell Medicine, Rockefeller University, New York, NY 10021, USA.
Arthritis and Tissue Degeneration Program, Hospital for Special Surgery, New York, NY 10021, USA.
Department of Physiology, Biophysics and Systems Biology, Weill Cornell Medicine, New York, NY 10021, USA.
Department of Medicine, Weill Cornell Medicine, New York, NY 10021, USA.

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