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Updated: Feb 22, 2026

In Vivo Biosensor Tracks Non-apoptotic Caspase Activity in Drosophila
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Tango7 regulates cortical activity of caspases during reaper-triggered changes in tissue elasticity

Yunsik Kang1,2,3, Sarah D Neuman1,4, Arash Bashirullah5,6,7

  • 1Division of Pharmaceutical Sciences, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI, 53705-2222, USA.

Nature Communications
|September 21, 2017
PubMed

Insights

Caspase activity in living cells was uncovered. Specific adaptor proteins, tango7 and dark, control caspase functions in distinct cellular locations, enabling physiological processes without cell death.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Developmental biology

Background:

  • Caspases are crucial enzymes involved in both cell death and physiological processes.
  • The mechanisms by which caspases execute non-lethal functions remain largely unknown.
  • Understanding caspase regulation is key to deciphering cellular homeostasis and disease.

Purpose of the Study:

  • To identify novel physiological roles of caspases in living cells.
  • To elucidate the regulatory mechanisms governing caspase activity in specific subcellular compartments.
  • To differentiate between lethal and non-lethal caspase functions.

Main Methods:

  • Utilized Drosophila melanogaster salivary glands as a model system.
  • Investigated the function of the initiator caspase dronc and its adaptors.
  • Employed techniques to analyze F-actin dynamics and protein interactions at the cell cortex.

Main Results:

  • Identified a new role for caspases in dismantling cortical F-actin in living Drosophila salivary glands.
  • Demonstrated that tango7 regulates dronc activity at the cell cortex, distinct from dark's role in cytoplasmic cell death.
  • Showed that tango7-dependent caspase activity is triggered by a sublethal pulse of the IAP antagonist reaper.

Conclusions:

  • Tango7 and dark define distinct subcellular domains of caspase activity, regulating distinct cellular outcomes.
  • Biological outcomes of caspase activation are modulated by adaptor proteins and subcellular localization.
  • This study reveals a sophisticated mechanism for controlling caspase function in non-apoptotic cellular processes.

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