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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

Overview of attention for article published in Journal of Biological Chemistry, November 2016
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Title
The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes
Published in
Journal of Biological Chemistry, November 2016
DOI 10.1074/jbc.m116.733634
Pubmed ID
Authors

Vicente Andreu-Fernández, María J. García-Murria, Manuel Bañó-Polo, Juliette Martin, Luca Monticelli, Mar Orzáez, Ismael Mingarro

Abstract

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the insertion capacity of hydrophobic C-terminal regions of the BH3-only proteins Bik, Bim, Noxa, Bmf, and Puma into microsomal membranes. An Escherichia coli complementation assay was used to validate the results in a cellular context, and peptide insertions were modeled using molecular dynamics simulations. We also found that some of the C-terminal domains were sufficient to direct green fluorescent protein-fusion proteins to specific membranes in human cells, but the domains did not activate apoptosis. Thus, the hydrophobic regions in the C-termini of BH3-only members associated in distinct ways with various biological membranes, suggesting that a detailed investigation of the entire process of apoptosis should include studying the membranes as a setting for protein-protein and protein-membrane interactions.

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Mendeley readers

The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Spain 1 4%
United States 1 4%
Unknown 24 92%

Demographic breakdown

Readers by professional status Count As %
Researcher 6 23%
Student > Ph. D. Student 6 23%
Student > Master 3 12%
Professor 2 8%
Student > Bachelor 1 4%
Other 3 12%
Unknown 5 19%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 8 31%
Agricultural and Biological Sciences 7 27%
Chemistry 2 8%
Immunology and Microbiology 1 4%
Business, Management and Accounting 1 4%
Other 1 4%
Unknown 6 23%