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Article

Rhbdf2 mutations increase its protein stability and drive EGFR hyperactivation through enhanced secretion of amphiregulin.

Proceedings of the National Academy of Sciences of the United States of America - 27 May 2014

Hosur Vishnu, Johnson Kenneth R, Burzenski Lisa M, Stearns Timothy M, Maser Richard S, Shultz Leonard D

Abstract excerpt

The rhomboid 5 homolog 2 (Rhbdf2) gene encodes an inactive rhomboid (iRhom) protease, iRhom2, one of a family of enzymes containing a long cytosolic N terminus and a dormant peptidase domain of unknown function. iRhom2 has been implicated in epithelial regeneration and cancer growth through constitutive activation of epidermal growth factor receptor (EGFR) signaling. However, little is known about the...

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Identifiers

PMID: 24825892
DOI: 10.1073/pnas.1323908111
PMCID: PMC4040562

Genes

EGFR
ADAM17
EGF

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Rhbdf2 mutations increase its protein stability and drive EGFR hyperactivation through enhanced secretion of amphiregulin.PMID 24825892Read ↗

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A sterol-binding pocket in iRhom1 underlies paralog-specific regulation of the sheddase ADAM17Semantic proximity Read ↗

Substrate-selective protein ectodomain shedding by ADAM17 and iRhom2 depends on their juxtamembrane and transmembrane domains.Semantic proximity Read ↗

iRHOM2: A Regulator of Palmoplantar Biology, Inflammation, and Viral Susceptibility.Semantic proximity Read ↗

Deletions in the cytoplasmic domain of iRhom1 and iRhom2 promote shedding of the TNF receptor by the protease ADAM17.Semantic proximity Read ↗

Pathological mutations reveal the key role of the cytosolic iRhom2 N-terminus for phosphorylation-independent 14-3-3 interaction and ADAM17 binding, stability, and activity.Semantic proximity Read ↗

Pathological mutations reveal the key role of the cytosolic iRhom2 N-terminus for phosphorylation-independent 14-3-3 interaction and ADAM17 binding, stability, and activitySemantic proximity Read ↗

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