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Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

M Mancini1, C E Machamer, S Roy

  • 1Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

The Journal of Cell Biology
|May 3, 2000
PubMed

Insights

Caspase-2, a key apoptosis protein, is found in the Golgi complex. It uniquely cleaves golgin-160, delaying Golgi disintegration and influencing cell death pathways.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Caspases are crucial cysteine proteases regulating apoptosis.
  • Distinct caspases possess unique functions and regulation despite similar cleavage specificities.
  • Apoptotic stimuli activate specific proteolytic pathways at distinct subcellular locations.

Purpose of the Study:

  • To investigate the subcellular localization and function of caspase-2.
  • To identify unique substrates and cleavage sites for caspase-2.
  • To elucidate the role of caspase-2 in Golgi complex-mediated apoptosis.

Main Methods:

  • Immunofluorescence microscopy to determine caspase-2 localization.
  • In vitro assays to identify caspase-2 cleavage sites on golgin-160.
  • Cellular assays to assess the impact of caspase-2 activity on Golgi integrity during apoptosis.

Main Results:

  • Caspase-2 localizes to the Golgi complex in addition to the nucleus.
  • Caspase-2 cleaves golgin-160 at a unique site distinct from other caspases.
  • Inhibition of this specific cleavage delays Golgi disintegration following apoptotic signaling.

Conclusions:

  • The Golgi complex acts as a platform for localized apoptosis signaling by caspase-2.
  • Caspase-2's unique cleavage of golgin-160 is an early event in Golgi-mediated apoptosis.
  • This highlights the specialized roles of caspases in distinct cellular compartments during programmed cell death.

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