Proteomics

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Phosphorylation of iRhom2 controls stimulated proteolytic shedding by the metalloprotease ADAM17/TACE

ABSTRACT: TACE (TNFa Converting Enzyme), is responsible for cleavage (‘shedding’) of membrane-tethered signaling molecules such as TNF of EGFR ligands. TACE interacts with iRhom2, which mediates the exit of TACE from the endoplasmic reticulum. In this study we analyze a new role for iRHOM2, where a fraction of the protein remains in the membrane and the phosphorylation of different residues in its cytoplasmatic tail is necessary for TACE shedding function.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Alfonso Bolado  

LAB HEAD: Alexander von Kriegsheim

PROVIDER: PXD007763 | Pride | 2021-11-03

REPOSITORIES: Pride

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Publications

Cell surface metalloproteases coordinate signaling during development, tissue homeostasis, and disease. TACE (TNF-α-converting enzyme), is responsible for cleavage ("shedding") of membrane-tethered signaling molecules, including the cytokine TNF, and activating ligands of the EGFR. The trafficking of TACE within the secretory pathway requires its binding to iRhom2, which mediates the exit of TACE from the endoplasmic reticulum. An important, but mechanistically unclear, feature of TACE biology i  ...[more]

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