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We have found that treatment of A431 cells with tumor necrosis factor\u2010\u03b1 in the presence of cycloheximide resulted in the cleavage of epidermal growth factor receptor (EGFR) as well as the activation of caspase\u20103. Among various caspases, caspase\u20101, caspase\u20103 and caspase\u20107 were most potent in the cleavage of EGFR in vitro. Proteolytic cleavage of EGFR was inhibited by both YVAD\u2010cmk and DEVD\u2010fmk in vitro. We also investigated the effect of caspase\u2010dependent cleavage of EGFR upon the mediation of signals to downstream signaling molecules such as PLC\u2010\u03b31. Cleavage of EGFR by caspase\u20103 significantly impaired the tyrosine phosphorylation of PLC\u2010\u03b31 in vitro. Given these results, we suggest that apoptotic protease specifically cleaves and inactivates EGFR, which plays crucial roles in anti\u2010apoptotic signaling, to abrogate the activation of EGFR\u2010dependent downstream survival signaling molecules.<\/jats:p>","DOI":"10.1016\/s0014-5793(01)02167-6","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T19:52:46Z","timestamp":1027626766000},"page":"16-20","source":"Crossref","is-referenced-by-count":38,"title":["Proteolytic cleavage of epidermal growth factor receptor by caspases"],"prefix":"10.1002","volume":"491","author":[{"given":"Sun Sik","family":"Bae","sequence":"first","affiliation":[]},{"given":"Jang Hyun","family":"Choi","sequence":"additional","affiliation":[]},{"given":"Yong Seok","family":"Oh","sequence":"additional","affiliation":[]},{"given":"David K.","family":"Perry","sequence":"additional","affiliation":[]},{"given":"Sung Ho","family":"Ryu","sequence":"additional","affiliation":[]},{"given":"Pann-Ghill","family":"Suh","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2001,2,20]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.39.25436"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.12.8817"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80405-5"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.282.5392.1318"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.7878463"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81334-3"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81265-9"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)81589-5"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80501-2"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80434-1"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.278.5345.1966"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1096\/fasebj.14.9.1083"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.273.12.7141"},{"key":"e_1_2_6_15_1","unstructured":"Harlow E. and Lane D. 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