Regulated intramembrane cleavage of the EGF receptor.

Liao HJ, Carpenter G
Traffic. 2012 13 (8): 1106-12

PMID: 22531034 · DOI:10.1111/j.1600-0854.2012.01371.x

Following the addition of EGF or ionomycin to A431 cells, protease activity mediates cleavage of the EGF receptor producing a 60 kDa fragment that includes the intracellular domain (ICD). This fragment is located in both membrane and nuclear fractions. On the basis of sensitivity to chemical inhibitors and overexpression of cDNAs, the rhomboid intramembrane proteases, not γ-secretase proteases, are identified as responsible for the cleavage event. Agonist-initiated cleavage occurs slowly over 3-24 h. Inhibition of calpain protease activity significantly increased the detectable level of ICD fragment.

© 2012 John Wiley & Sons A/S.

MeSH Terms (17)

Amyloid Precursor Protein Secretases Calpain Cell Line, Tumor Cell Membrane Cell Nucleus Epidermal Growth Factor ErbB Receptors Gene Expression Glycoproteins HEK293 Cells Humans Ionomycin Proteolysis Quinazolines Serine Endopeptidases Serine Proteinase Inhibitors Tyrphostins

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