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The Drosophila effector caspase Dcp-1 regulates mitochondrial dynamics and autophagic flux via SesB. | LitMetric

The Drosophila effector caspase Dcp-1 regulates mitochondrial dynamics and autophagic flux via SesB.

J Cell Biol

The Genome Sciences Centre, British Columbia Cancer Agency, Vancouver, British Columbia V5Z 1L3, Canada Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada

Published: May 2014

AI Article Synopsis

  • The study investigates the role of Drosophila caspase 1 (Dcp-1) in linking autophagy and apoptosis, revealing its presence in mitochondria and its impact on mitochondrial structure and autophagy levels.
  • Loss of Dcp-1 results in elongated mitochondria and increased ATP production, but also lowers autophagic activity, indicating a complex relationship between these cellular processes.
  • The research identifies stress-sensitive B (SesB) as a negative regulator of autophagy during midoogenesis and shows that Dcp-1 helps maintain autophagic flux by stabilizing SesB and controlling ATP levels.

Article Abstract

Increasing evidence reveals that a subset of proteins participates in both the autophagy and apoptosis pathways, and this intersection is important in normal physiological contexts and in pathological settings. In this paper, we show that the Drosophila effector caspase, Drosophila caspase 1 (Dcp-1), localizes within mitochondria and regulates mitochondrial morphology and autophagic flux. Loss of Dcp-1 led to mitochondrial elongation, increased levels of the mitochondrial adenine nucleotide translocase stress-sensitive B (SesB), increased adenosine triphosphate (ATP), and a reduction in autophagic flux. Moreover, we find that SesB suppresses autophagic flux during midoogenesis, identifying a novel negative regulator of autophagy. Reduced SesB activity or depletion of ATP by oligomycin A could rescue the autophagic defect in Dcp-1 loss-of-function flies, demonstrating that Dcp-1 promotes autophagy by negatively regulating SesB and ATP levels. Furthermore, we find that pro-Dcp-1 interacts with SesB in a nonproteolytic manner to regulate its stability. These data reveal a new mitochondrial-associated molecular link between nonapoptotic caspase function and autophagy regulation in vivo.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4033768PMC
http://dx.doi.org/10.1083/jcb.201303144DOI Listing

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