Next Article in Journal
Protective Effects of Liquiritigenin against Citrinin-Triggered, Oxidative-Stress-Mediated Apoptosis and Disruption of Embryonic Development in Mouse Blastocysts
Next Article in Special Issue
The E3 Ubiquitin Ligase RNF7 Negatively Regulates CARD14/CARMA2sh Signaling
Previous Article in Journal
RNA Chaperone Function of a Universal Stress Protein in Arabidopsis Confers Enhanced Cold Stress Tolerance in Plants
Previous Article in Special Issue
The Relevance of the UPS in Fatty Liver Graft Preservation: A New Approach for IGL-1 and HTK Solutions
Article Menu
Issue 12 (December) cover image

Export Article

Open AccessReview
Int. J. Mol. Sci. 2017, 18(12), 2541;

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

Biochemie Intrazellulärer Transportprozesse, Ruhr-Universität Bochum, 44801 Bochum, Germany
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)
Full-Text   |   PDF [1397 KB, uploaded 27 November 2017]   |  


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

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

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.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top