Proteolytic cleavage of epidermal growth factor receptor by caspases
SCIE
SCOPUS
- Title
- Proteolytic cleavage of epidermal growth factor receptor by caspases
- Authors
- Bae, SS; Choi, JH; Oh, YS; Perry, DK; Ryu, SH; Suh, PG
- Date Issued
- 2001-02-23
- Publisher
- ELSEVIER SCIENCE BV
- Abstract
- Apoptotic proteases cleave and inactivate survival signaling molecules such as Akt/PKB, phospholipase C (PLC)-gamma1, and Bcl-2. We have found that treatment of A431 cells with tumor necrosis factor-alpha in the presence of cycloheximide resulted in the cleavage of epidermal growth factor receptor (EGFR) as well as the activation of caspase-3. Among various caspases, caspase-1, caspase-3 and caspase-7 were most potent in the cleavage of EGFR in vitro. Proteolytic cleavage of EGFR was inhibited by both YVAD-cmk and DEVD-fmk in vitro. We also investigated the effect of caspase-dependent cleavage of EGFR upon the mediation of signals to downstream signaling molecules such as PLC-gamma1. Cleavage of EGFR by caspase-3 significantly impaired the tyrosine phosphorylation of PLC-gamma1 in vitro. Given these results, we suggest that apoptotic protease specifically cleaves and inactivates EGFR, which plays crucial roles in anti-apoptotic signaling, to abrogate the activation of EGFR-dependent downstream survival signaling molecules, (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
- Keywords
- apoptosis; proteolysis; receptor; CYTOCHROME-C; EGF RECEPTOR; DEATH; APOPTOSIS; PHOSPHORYLATION; PROTEASE; ACTIVATION; SIGNALS; BCL-2; SITE
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/19652
- DOI
- 10.1016/S0014-5793(01)02167-6
- ISSN
- 0014-5793
- Article Type
- Article
- Citation
- FEBS LETTERS, vol. 491, no. 1-2, page. 16 - 20, 2001-02-23
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