Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies

During apoptosis, Bak and Bax are activated by BH3-only proteins binding to a specific hydrophobic groove. Here, the authors show that antibodies can also activate Bak and mitochondrial Bax by binding to the α1-α2 loop, thus identifying a potential clinical target.

Bibliographic Details
Main Authors: Sweta Iyer, Khatira Anwari, Amber E. Alsop, Wai Shan Yuen, David C. S. Huang, John Carroll, Nicholas A. Smith, Brian J. Smith, Grant Dewson, Ruth M. Kluck
Format: Article
Language:English
Published: Nature Publishing Group 2016-05-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms11734
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spelling doaj-7e08a7aefe7a40b3835bb796864f5aae2021-05-11T10:47:19ZengNature Publishing GroupNature Communications2041-17232016-05-017111010.1038/ncomms11734Identification of an activation site in Bak and mitochondrial Bax triggered by antibodiesSweta Iyer0Khatira Anwari1Amber E. Alsop2Wai Shan Yuen3David C. S. Huang4John Carroll5Nicholas A. Smith6Brian J. Smith7Grant Dewson8Ruth M. Kluck9Molecular Genetics of Cancer Division, The Walter and Eliza Hall Institute of Medical ResearchMolecular Genetics of Cancer Division, The Walter and Eliza Hall Institute of Medical ResearchMolecular Genetics of Cancer Division, The Walter and Eliza Hall Institute of Medical ResearchMonash Biomedicine Discovery Institute and Department of Anatomy and Developmental Biology, Development and Stem Cells Program, Monash University, MelbourneCancer and Haematology Division, The Walter and Eliza Hall Institute of Medical ResearchMonash Biomedicine Discovery Institute and Department of Anatomy and Developmental Biology, Development and Stem Cells Program, Monash University, MelbourneDepartment of Chemistry and Physics, La Trobe Institute for Molecular Sciences, La Trobe UniversityDepartment of Chemistry and Physics, La Trobe Institute for Molecular Sciences, La Trobe UniversityCell Signalling and Cell Death Division, The Walter and Eliza Hall Institute of Medical ResearchMolecular Genetics of Cancer Division, The Walter and Eliza Hall Institute of Medical ResearchDuring apoptosis, Bak and Bax are activated by BH3-only proteins binding to a specific hydrophobic groove. Here, the authors show that antibodies can also activate Bak and mitochondrial Bax by binding to the α1-α2 loop, thus identifying a potential clinical target.https://doi.org/10.1038/ncomms11734
collection DOAJ
language English
format Article
sources DOAJ
author Sweta Iyer
Khatira Anwari
Amber E. Alsop
Wai Shan Yuen
David C. S. Huang
John Carroll
Nicholas A. Smith
Brian J. Smith
Grant Dewson
Ruth M. Kluck
spellingShingle Sweta Iyer
Khatira Anwari
Amber E. Alsop
Wai Shan Yuen
David C. S. Huang
John Carroll
Nicholas A. Smith
Brian J. Smith
Grant Dewson
Ruth M. Kluck
Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
Nature Communications
author_facet Sweta Iyer
Khatira Anwari
Amber E. Alsop
Wai Shan Yuen
David C. S. Huang
John Carroll
Nicholas A. Smith
Brian J. Smith
Grant Dewson
Ruth M. Kluck
author_sort Sweta Iyer
title Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
title_short Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
title_full Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
title_fullStr Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
title_full_unstemmed Identification of an activation site in Bak and mitochondrial Bax triggered by antibodies
title_sort identification of an activation site in bak and mitochondrial bax triggered by antibodies
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2016-05-01
description During apoptosis, Bak and Bax are activated by BH3-only proteins binding to a specific hydrophobic groove. Here, the authors show that antibodies can also activate Bak and mitochondrial Bax by binding to the α1-α2 loop, thus identifying a potential clinical target.
url https://doi.org/10.1038/ncomms11734
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