Cited by 223

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Modulation of type M 2 pyruvate kinase activity by the human papillomavirus type 16 E7 oncoprotein

Zwerschke, Werner, Mazurek, Sybille, Massimi, Paola, Banks, Lawrence, Eigenbrodt, Erich, Jansen-Dürr, Pidder·1999·Proceedings of the National Academy of Sciences

Abstract

We report here that the E7 oncoprotein encoded by the oncogenic human papillomavirus (HPV) type 16 binds to the glycolytic enzyme type M 2 pyruvate kinase (M2-PK). M2-PK occurs in a tetrameric form with a high affinity to its substrate phosphoenolpyruvate and a dimeric form with a low affinity to phosphoenolpyruvate, and the transition between both conformations regulates the glycolytic flux in tumor cells. The glycolytic intermediate fructose 1,6-bisphosphate induces the reassociation of the dimeric to the tetrameric form of M2-PK. The expression of E7 in an experimental cell line shifts the equilibrium to the dimeric state despite a significant increase in the fructose 1,6-bisphosphate levels. Investigations of HPV-16 E7 mutants and the nononcogenic HPV-11 subtype suggest that the interaction of HPV-16 E7 with M2-PK may be linked to the transforming potential of the viral oncoprotein.

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Crossref · 10.1073/pnas.96.4.1291

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Cited by

Metadata

Authors
Zwerschke, W., Mazurek, S., Massimi, P., Banks, L., Eigenbrodt, E., & Jansen-Dürr, P.
Affiliations
Deutsches Krebsforschungszentrum, Forschungsschwerpunkt Angewandte Tumorvirologie, Abt. F0301, INF 242, D-69120 Heidelberg, Germany; ScheBo Tech GmbH, Bahnhofstrasse 6, D-35435 Wettenberg, Germany; Institut für Biochemie and Endokrinologie, Fachbereich Veterinärmedizin, Universität Giessen, Frankfurter Strasse 100, D-35392 Giessen, Germany; and International Center for Genetic Engineering and Biotechnology, Padriciano 99, Trieste, Italy
Venue
Proceedings of the National Academy of Sciences
Published
1999-02-16
Volume
96
Issue
4
Pages
1291-1296
ISSN
  • 0027-8424
  • 1091-6490
Cited by
223
References
1
Language
en

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