IPS-1 is crucial for DAP3-mediated anoikis induction by caspase-8 activation

Li H., Fujikura D., Harada T., Uehara J., Ikeda H., Goto T., Nishida K., Iwai A., Chida K., Uede T. · Cell Death & Differentiation · DOI: 10.1038/cdd.2009.97

Research Archive

TL;DR — Key Findings

IPS-1 bound DAP3 during detachment-induced apoptosis.
Caspase-8 recruitment was central to the proposed mechanism.
This is indirect cell biology, not beta-glucan evidence.

Abstract

Researchers examined how DAP3 contributes to anoikis, the apoptosis triggered when adherent cells detach from the extracellular matrix. IPS-1 bound DAP3, its overexpression activated caspases-3, -8, and -9, and IPS-1-deficient mouse embryonic fibroblasts resisted anoikis. Cell detachment recruited caspase-8 to IPS-1, while IPS-1 knockdown weakened DAP3-mediated anoikis. This cell-signaling study did not test beta-glucan or Aureobasidium pullulans.

Summary

Study

The interaction of IPS-1 and DAP3 in detachment-induced apoptosis was tested.

Finding

IPS-1 recruited and activated caspase-8 and was required for full DAP3-mediated anoikis.

Limit

No beta-glucan or Aureobasidium intervention was studied.

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Citation

Li H., Fujikura D., Harada T., Uehara J., Ikeda H., Goto T., Nishida K., Iwai A., Chida K., Uede T.. IPS-1 is crucial for DAP3-mediated anoikis induction by caspase-8 activation. Cell Death & Differentiation. 2009. DOI: 10.1038/cdd.2009.97.

Study Details

Study Type

In Vitro

Published

2009

Journal

Cell Death & Differentiation

Authors

Li H., Fujikura D., Harada T., Uehara J., Ikeda H., Goto T., Nishida K., Iwai A., Chida K., Uede T.

DOI

10.1038/cdd.2009.97

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