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Regulated Intramembrane Cleavage of the EGF Receptor
Author(s) -
Liao HongJun,
Carpenter Graham
Publication year - 2012
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2012.01371.x
Subject(s) - proteases , biology , cleavage (geology) , ionomycin , protease , rhomboid , calpain , microbiology and biotechnology , receptor , protease activated receptor 2 , intracellular , biochemistry , 5 ht5a receptor , enzyme , paleontology , fracture (geology)
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.