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Article

Targeted truncation of the ADAM17 cytoplasmic domain in mice results in protein destabilization and a hypomorphic phenotype.

The Journal of biological chemistry - 1 Jan 2000

Lora Jose, Weskamp Gisela, Li Thomas M, Maretzky Thorsten, Shola Dorjee T N, Monette Sébastien, Lichtenthaler Stefan F, Lu Theresa T, Yang Chingwen, Blobel Carl P

Abstract excerpt

A disintegrin and metalloprotease 17 (ADAM17) is a cell-surface metalloprotease that serves as the principle sheddase for tumor necrosis factor α (TNFα), interleukin-6 receptor (IL-6R), and several ligands of the epidermal growth factor receptor (EGFR), regulating these crucial signaling pathways. ADAM17 activation requires its transmembrane domain, but not its cytoplasmic domain, and little is known about the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33957124
DOI: 10.1016/j.jbc.2021.100733
PMCID: PMC8191336

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