Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Distinct domains control the addressing and the insertion of Bax into mitochondria.

The Journal of biological chemistry - 18 Mar 2005

Cartron Pierre-François, Arokium Hubert, Oliver Lisa, Meflah Khaled, Manon Stephen, Vallette François M

Abstract excerpt

The translocation of Bax from the cytosol into the mitochondrial outer membrane is a central event during apoptosis. We report that beyond the addressing step, which involves its first alpha-helix (halpha1), the helices alpha5 and alpha6 (halpha5alpha6) are responsible for the insertion of Bax into mitochondrial outer membrane bilayer. The translocation of Bax to mitochondria is associated with specific changes...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid
Share to bcl-2-Associated X Protein

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell-Free System

Share to Cytosol

Share to Lipid Bilayers

Share to Proto-Oncogene Proteins c-bcl-2

Share to Static Electricity

Share to Subcellular Fractions

Source

Identifiers

PMID: 15590655
DOI: 10.1074/jbc.M409714200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Distinct domains control the addressing and the insertion of Bax into mitochondria.PMID 15590655Read ↗

The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core.Semantic proximity Read ↗

Bax-induced cytochrome c release from mitochondria depends on alpha-helices-5 and -6.Semantic proximity Read ↗

The substitution of Proline 168 favors Bax oligomerization and stimulates its interaction with LUVs and mitochondria.Semantic proximity Read ↗

Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.Semantic proximity Read ↗

Involvement of the N-terminus of Bax in its intracellular localization and function.Semantic proximity Read ↗

The first alpha helix of Bax plays a necessary role in its ligand-induced activation by the BH3-only proteins Bid and PUMA.Semantic proximity Read ↗

Conformation of the Bax C-terminus regulates subcellular location and cell death.Semantic proximity Read ↗

The Bax carboxy-terminal hydrophobic helix does not determine organelle-specific targeting but is essential for maintaining Bax in an inactive state and for stable mitochondrial membrane insertion.Semantic proximity Read ↗

The N-terminal conformation of Bax regulates cell commitment to apoptosis.Semantic proximity Read ↗

Conformation of the C-terminal domain of the pro-apoptotic protein Bax and mutants and its interaction with membranes.Semantic proximity Read ↗

Bax Forms a Membrane Surface Protein-Lipid Complex as it Initiates ApoptosisSemantic proximity Read ↗

Substitutions of potentially phosphorylatable serine residues of Bax reveal how they may regulate its interaction with mitochondria.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.