Publikation: The ubiquitin‐protein ligase E6‐associated protein (E6‐AP) serves as its own substrate
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Recognition of substrate proteins by the ubiquitin-conjugation system is a highly specific and regu- lated event and involves the action of ubiquitin-conjugating enzymes (E2) and ubiquitin-protein ligases (E3). However, the E2 and E3 involved in the recognition of particular substrates have been identified in only a few cases. The ubiquitin-protein ligase E6-associated protein (E6-AP) was originally identified as a protein involved in the human papillomavirus E6-oncoprotein-induced degradation of p53. The substrate proteins of E6-AP in the absence of the E6 oncoprotein, however, have not been identified. We show here that E6-AP can target itself for ubiquitination in vitro and provide evidence that, under conditions of overexpression, E6-AP efficiently promotes its own degradation in vivo. Autoubiquitination of E6-AP is mediated mainly by intermolecular transfer of ubiquitin. In addition, highly ubiquitinated forms of E6- AP cannot bind to p53 in the presence of the E6 oncoprotein and, conversely, binding of E6-AP to p53 interferes with ubiquitination of E6-AP. These results suggest that autoubiquitination and subsequent degradation of E6-AP represents a mechanism to control intracellular E6-AP levels by inactivating E6- AP molecules that are not bound to substrate proteins.
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NUBER, Ulrike, Sylvia E. SCHWARZ, Martin SCHEFFNER, 1998. The ubiquitin‐protein ligase E6‐associated protein (E6‐AP) serves as its own substrate. In: European Journal of Biochemistry. 1998, 254(3), pp. 643-649. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1046/j.1432-1327.1998.2540643.xBibTex
@article{Nuber1998-06-15ubiqu-42647, year={1998}, doi={10.1046/j.1432-1327.1998.2540643.x}, title={The ubiquitin‐protein ligase E6‐associated protein (E6‐AP) serves as its own substrate}, number={3}, volume={254}, issn={0014-2956}, journal={European Journal of Biochemistry}, pages={643--649}, author={Nuber, Ulrike and Schwarz, Sylvia E. and Scheffner, Martin} }
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