Journal
TRAFFIC
Volume 13, Issue 8, Pages 1106-1112Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1600-0854.2012.01371.x
Keywords
calpain; epidermal growth factor receptor; intracellular domain; intramembrane proteolysis; ionomycin; nucleus; rhomboid protease
Categories
Funding
- NIH [RO1 CA 125649]
- Vanderbilt Ingram Cancer Center [P30 CA 068485]
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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 ?-secretase proteases, are identified as responsible for the cleavage event. Agonist-initiated cleavage occurs slowly over 324 h. Inhibition of calpain protease activity significantly increased the detectable level of ICD fragment.
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