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      BECLIN 1-VPS34 COMPLEX ARCHITECTURE: UNDERSTANDING THE NUTS AND BOLTS OF THERAPEUTIC TARGETS.

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          Abstract

          Autophagy is an important lysosomal degradation pathway that aids in the maintenance of cellular homeostasis by breaking down and recycling intracellular contents. Dysregulation of autophagy is linked to a growing number of human diseases. The Beclin 1-Vps34 protein-protein interaction network is critical for autophagy regulation and is therefore essential to cellular integrity. Manipulation of autophagy, in particular via modulation of the action of the Beclin 1-Vps34 complexes, is considered a promising route to combat autophagy-related diseases. Here we summarize recent findings on the core components and structural architecture of the Beclin 1-Vps34 complexes, and how these findings provide valuable insights into the molecular mechanisms that underlie the multiple functions of these complexes and for devising therapeutic strategies.

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          Author and article information

          Journal
          Front Biol (Beijing)
          Frontiers in biology
          Springer Nature
          1674-7984
          1674-7984
          Oct 2015
          : 10
          : 5
          Affiliations
          [1 ] Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536.
          [2 ] Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, BC, Canada V6T1Z3.
          [3 ] Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065.
          [4 ] Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536 ; Department of Toxicology and Cancer Biology, University of Kentucky, Lexington, KY 40536, USA ; Markey Cancer Center, University of Kentucky, Lexington, KY 40536, USA.
          Article
          NIHMS736419
          10.1007/s11515-015-1374-y
          4682202
          26692106
          7e062129-b51b-4ae2-9fa4-f92f00d1f09e

          Beclin 1, CX-MS, EM, Nrbf2, Vps34, complex, drug design, inhibitor, structure

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