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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Cell Motility through Blebbing01:16

Cell Motility through Blebbing

Blebs are a type of membrane protrusion formed by the internal hydrostatic pressure of the cytoplasm. Blebs are observed in several cell types, including fibroblasts, immune cells, and single-celled organisms like the amoeba. The primary function of blebs is cell locomotion and apoptosis, but they are also found during necrosis and cell division. The life cycle of a bleb comprises an initiation phase followed by the expansion and retraction phases.
Blebbing Through the Matrix
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Mechanism of Filopodia Formation01:39

Mechanism of Filopodia Formation

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Protein Complex Assembly

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Related Experiment Video

Updated: Jun 14, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Bax forms an oligomer via separate, yet interdependent, surfaces.

Zhi Zhang1, Weijia Zhu, Suzanne M Lapolla

  • 1Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73126, USA.

The Journal of Biological Chemistry
|April 13, 2010
PubMed
Summary

Bax protein oligomerization, crucial for apoptosis, involves two distinct interaction surfaces. These surfaces, the BH1-3 groove and a rear pocket, allosterically couple to drive membrane permeabilization.

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Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

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Related Experiment Videos

Last Updated: Jun 14, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
08:35

Examining BCL-2 Family Function with Large Unilamellar Vesicles

Published on: October 5, 2012

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Biology

Background:

  • Bcl-2 family proteins regulate mitochondrial outer membrane permeability and apoptosis.
  • Bax protein oligomerization is a key event in initiating membrane permeabilization.

Purpose of the Study:

  • To map the interaction interfaces of the Bax oligomer.
  • To elucidate the mechanism of Bax oligomerization.

Main Methods:

  • Site-specific photocross-linking using photo-reactive probes.
  • Utilizing Triton X-100 as a membrane surrogate.
  • Cross-linking experiments with Bax BH3 peptides and mutants.

Main Results:

  • Two distinct interaction surfaces on the Bax oligomer were identified: the BH1-3 groove and a rear pocket.
  • These surfaces interact with counterparts on neighboring proteins, forming two separate interfaces.
  • Interaction at the BH1-3 groove primes the rear pocket for subsequent interactions.

Conclusions:

  • Bax oligomerization is a multi-step process driven by interactions at distinct, allosterically coupled interfaces.
  • This mechanism ensures controlled permeabilization of the mitochondrial outer membrane.
  • Understanding Bax oligomerization provides insights into apoptotic pathways.