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Related Experiment Video

Updated: May 28, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Active Bax and Bak are functional holins.

Xiaming Pang¹, Samir H Moussa, Natalie M Targy

¹Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, USA.

Genes & Development

|October 19, 2011

Summary

This summary is machine-generated.

Active Bax and Bak proteins mimic bacterial holins, forming membrane pores that cause cell lysis. This discovery links mitochondrial outer membrane permeabilization (MOMP) to bacterial lysis mechanisms.

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Area of Science:

Cell Biology
Molecular Biology
Biophysics

Background:

The mechanism of Bax/Bak-dependent mitochondrial outer membrane permeabilization (MOMP) is central to apoptosis but not fully understood.
Bcl-2 family proteins regulate MOMP, but their precise function in pore formation remains unclear.

Purpose of the Study:

To investigate the functional similarities between Bax/Bak and λ bacteriophage holins.
To elucidate the mechanism of Bax/Bak-mediated membrane permeabilization.

Main Methods:

Expression of active Bax/Bak in bacteria.
Assaying bacterial lysis and endolysin release.
Constructing bacteriophages with Bax/Bak alleles replacing the holin gene.
Analyzing membrane hole formation and regulation by Bcl-2 family proteins.

Main Results:

Active Bax/Bak, unlike other Bcl-2 proteins, induced bacterial lysis via oligomerization-dependent endolysin release, mimicking holin behavior.
Bacteriophages engineered with active Bax/Bak alleles formed plaques, demonstrating functional holin-like activity.
Active Bax formed large membrane holes, with size influenced by Bax structural elements.
Bcl-xL inhibited Bax-induced lysis, while BH3-only proteins stimulated wild-type Bax activity.

Conclusions:

Bax/Bak proteins exhibit holin-like pore-forming activity in bacterial membranes.
This study mechanistically links MOMP to holin-mediated membrane damage in bacteria.
The findings provide novel insights into the biophysical mechanisms of apoptosis regulation.