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Int. J. Mol. Sci. 2017, 18(12), 2541; https://doi.org/10.3390/ijms18122541

Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades

1
Biochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, 44801 Bochum, Germany
2
Biomedizinische Forschung, Leibniz-Institut für Analytische Wissenschaften-ISAS-e.V. 44139 Dortmund, Germany
*
Author to whom correspondence should be addressed.
Received: 3 November 2017 / Revised: 22 November 2017 / Accepted: 24 November 2017 / Published: 27 November 2017
(This article belongs to the Special Issue Ubiquitin System)
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Abstract

Autophagy contributes to cellular homeostasis through the degradation of various intracellular targets such as proteins, organelles and microbes. This relates autophagy to various diseases such as infections, neurodegenerative diseases and cancer. A central component of the autophagy machinery is the class III phosphatidylinositol 3-kinase (PI3K-III) complex, which generates the signaling lipid phosphatidylinositol 3-phosphate (PtdIns3P). The catalytic subunit of this complex is the lipid-kinase VPS34, which associates with the membrane-targeting factor VPS15 as well as the multivalent adaptor protein BECLIN 1. A growing list of regulatory proteins binds to BECLIN 1 and modulates the activity of the PI3K-III complex. Here we discuss the regulation of BECLIN 1 by several different types of ubiquitination, resulting in distinct polyubiquitin chain linkages catalyzed by a set of E3 ligases. This contribution is part of the Special Issue “Ubiquitin System”. View Full-Text
Keywords: BECLIN 1; VPS34; AMBRA 1; ubiquitin; autophagy; tumor suppressor BECLIN 1; VPS34; AMBRA 1; ubiquitin; autophagy; tumor suppressor
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Boutouja, F.; Brinkmeier, R.; Mastalski, T.; El Magraoui, F.; Platta, H.W. Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades. Int. J. Mol. Sci. 2017, 18, 2541.

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