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2 results on '"compensatory autophagy"'

1. Hsp83 loss suppresses proteasomal activity resulting in an upregulation of caspase-dependent compensatory autophagy.

Author

Choutka, Courtney, DeVorkin, Lindsay, Go, Nancy Erro, Hou, Ying-Chen Claire, Moradian, Annie, Morin, Gregg B., and Gorski, Sharon M.

Abstract

The 2 main degradative pathways that contribute to proteostasis are the ubiquitin-proteasome system and autophagy but how they are molecularly coordinated is not well understood. Here, we demonstrate an essential role for an effector caspase in the activation of compensatory autophagy when proteasomal activity is compromised. Functional loss of Hsp83, theDrosophilaortholog of human HSP90 (heat shock protein 90), resulted in reduced proteasomal activity and elevated levels of the effector caspase Dcp-1. Surprisingly, genetic analyses showed that the caspase was not required for cell death in this context, but instead was essential for the ensuing compensatory autophagy, female fertility, and organism viability. The zymogen pro-Dcp-1 was found to interact with Hsp83 and undergo proteasomal regulation in an Hsp83-dependent manner. Our work not only reveals unappreciated roles for Hsp83 in proteasomal activity and regulation of Dcp-1, but identifies an effector caspase as a key regulatory factor for sustaining adaptation to cell stress in vivo. [ABSTRACT FROM PUBLISHER]

Published
2017
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2. Hsp83 loss suppresses proteasomal activity resulting in an upregulation of caspase-dependent compensatory autophagy

Author

Gregg B. Morin, Sharon M. Gorski, Lindsay DeVorkin, Ying-Chen Claire Hou, Courtney Choutka, Nancy Erro Go, and Annie Moradian

Subjects
Proteomics, 0301 basic medicine, Proteasome Endopeptidase Complex, Programmed cell death, caspase, Mass Spectrometry, 03 medical and health sciences, Downregulation and upregulation, compensatory autophagy, Heat shock protein, Autophagy, In Situ Nick-End Labeling, Animals, Drosophila Proteins, Molecular Biology, Heat-Shock Proteins, Caspase, Ovum, biology, Effector, apoptosis, Cell Biology, heat-shock protein, Hsp83, Basic Research Paper, Up-Regulation, Cell biology, Protein Subunits, Drosophila melanogaster, Fertility, 030104 developmental biology, Proteostasis, Proteasome, Caspases, Larva, Mutation, Dcp-1, Cancer research, biology.protein, Drosophila, Female, Mutant Proteins, RNA Interference, ubiquitin-proteasome system, Protein Binding
Abstract

The 2 main degradative pathways that contribute to proteostasis are the ubiquitin-proteasome system and autophagy but how they are molecularly coordinated is not well understood. Here, we demonstrate an essential role for an effector caspase in the activation of compensatory autophagy when proteasomal activity is compromised. Functional loss of Hsp83, the Drosophila ortholog of human HSP90 (heat shock protein 90), resulted in reduced proteasomal activity and elevated levels of the effector caspase Dcp-1. Surprisingly, genetic analyses showed that the caspase was not required for cell death in this context, but instead was essential for the ensuing compensatory autophagy, female fertility, and organism viability. The zymogen pro-Dcp-1 was found to interact with Hsp83 and undergo proteasomal regulation in an Hsp83-dependent manner. Our work not only reveals unappreciated roles for Hsp83 in proteasomal activity and regulation of Dcp-1, but identifies an effector caspase as a key regulatory factor for sustaining adaptation to cell stress in vivo.

Published
2017

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