After Embedding in membranes antiapoptotic bcl-xl protein binds both bcl-2 homology region 3 and helix 1 of proapoptotic bax protein to inhibit apoptotic mitochondrial permeabilization

Jingzhen Ding, Blaine H.M. Mooers, Zhi Zhang, Justin Kale, Domina Falcone, Jamie McNichol, Bo Huang, Xuejun C. Zhang, Chengguo Xing, David W. Andrews, Jialing Lin

Research output: Contribution to journalArticlepeer-review

47 Scopus citations

Abstract

Background: Bcl-XL binds Bax at mitochondria, inhibiting Bax oligomerization and apoptosis. Results: Anchored in membranes, Bcl-XL•Bax heterodimer is formed from a rigid helix-in-groove interface plus a flexible helical dimer interface. Conclusion: Two interfaces contribute equally to the heterodimer stability required to inhibit Bax. Significance: This novel kind of protein-protein interaction stabilizes the membrane-bound heterodimer that is pivotal to apoptosis regulation.

Original languageEnglish (US)
Pages (from-to)11873-11896
Number of pages24
JournalJournal of Biological Chemistry
Volume289
Issue number17
DOIs
StatePublished - Apr 25 2014

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