Topology of active, membrane-embedded Bax in the context of a toroidal pore (Q91304407)

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21 April 2020

title

Topology of active, membrane-embedded Bax in the context of a toroidal pore (English)

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21 April 2020

1

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21 April 2020

author name string

Tufa E Assafa

2

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21 April 2020

Carolin Stegmueller

3

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21 April 2020

Alice Wittig

4

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21 April 2020

Ana J Garcia-Saez

5

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21 April 2020

Enrica Bordignon

6

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21 April 2020

publication date

5 September 2018

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Cell Death & Differentiation

21 April 2020

published in

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21 April 2020

volume

25

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21 April 2020

issue

10

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21 April 2020

page(s)

1717-1731

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Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy.

21 April 2020

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Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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Stepwise activation of BAX and BAK by tBID, BIM, and PUMA initiates mitochondrial apoptosis.

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Bax monomers form dimer units in the membrane that further self-assemble into multiple oligomeric species

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Membrane binding by tBid initiates an ordered series of events culminating in membrane permeabilization by Bax

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Structure of Bax: coregulation of dimer formation and intracellular localization

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The X-ray structure of a BAK homodimer reveals an inhibitory zinc binding site

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Differential retrotranslocation of mitochondrial Bax and Bak.

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VDAC2 inhibits BAK activation and mitochondrial apoptosis

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Bax targets mitochondria by distinct mechanisms before or during apoptotic cell death: a requirement for VDAC2 or Bak for efficient Bax apoptotic function

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7 January 2021

Inhibition of Bak activation by VDAC2 is dependent on the Bak transmembrane anchor

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7 January 2021

Bax exists in a dynamic equilibrium between the cytosol and mitochondria to control apoptotic priming

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Multimodal interaction with BCL-2 family proteins underlies the proapoptotic activity of PUMA BH3

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BAX activation is initiated at a novel interaction site

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Multiple partners can kiss-and-run: Bax transfers between multiple membranes and permeabilizes those primed by tBid

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Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis

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7 January 2021

BID-induced structural changes in BAK promote apoptosis

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

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7 January 2021

Conformational changes and protein stability of the pro-apoptotic protein Bax.

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7 January 2021

BH3-triggered structural reorganization drives the activation of proapoptotic BAX.

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7 January 2021

Structural model of active Bax at the membrane.

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7 January 2021

A Small-Molecule Inhibitor of Bax and Bak Oligomerization Prevents Genotoxic Cell Death and Promotes Neuroprotection.

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7 January 2021

Molecular details of Bax activation, oligomerization, and membrane insertion.

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7 January 2021

Bak core and latch domains separate during activation, and freed core domains form symmetric homodimers

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7 January 2021

BH3-in-groove dimerization initiates and helix 9 dimerization expands Bax pore assembly in membranes

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7 January 2021

Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices

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7 January 2021

Bax dimerizes via a symmetric BH3:groove interface during apoptosis

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7 January 2021

Bak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains

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7 January 2021

Bax forms an oligomer via separate, yet interdependent, surfaces

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7 January 2021

Disordered clusters of Bak dimers rupture mitochondria during apoptosis.

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7 January 2021

Proapoptotic Bax and Bak proteins form stable protein-permeable pores of tunable size

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7 January 2021

Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores.

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7 January 2021

Visual and functional demonstration of growing Bax-induced pores in mitochondrial outer membranes

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7 January 2021

Mitochondrial outer membrane proteins assist Bid in Bax-mediated lipidic pore formation

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7 January 2021

cBid, Bax and Bcl-xL exhibit opposite membrane remodeling activities.

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7 January 2021

Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores

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7 January 2021

Association of Bax and Bak homo-oligomers in mitochondria. Bax requirement for Bak reorganization and cytochrome c release

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7 January 2021

Apoptotic pore formation is associated with in-plane insertion of Bak or Bax central helices into the mitochondrial outer membrane

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7 January 2021

Bak Conformational Changes Induced by Ligand Binding: Insight into BH3 Domain Binding and Bak Homo-Oligomerization

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7 January 2021

Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis

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7 January 2021

Dissociation of Bak α1 helix from the core and latch domains is required for apoptosis

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7 January 2021

BAK α6 permits activation by BH3-only proteins and homooligomerization via the canonical hydrophobic groove

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Cystic fibrosis transmembrane conductance regulator mutations that disrupt nucleotide binding

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7 January 2021

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7 January 2021

Bax-independent inhibition of apoptosis by Bcl-XL.

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7 January 2021

Quantitative interactome of a membrane Bcl-2 network identifies a hierarchy of complexes for apoptosis regulation.

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7 January 2021

Inactivation of prosurvival Bcl-2 proteins activates Bax/Bak through the outer mitochondrial membrane

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7 January 2021

Multiple Bcl-2 family members demonstrate selective dimerizations with Bax

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7 January 2021

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

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7 January 2021

Complete activation of Bax by a single site mutation

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7 January 2021

Bax targeting to mitochondria occurs via both tail anchor-dependent and -independent mechanisms

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7 January 2021

Conformational control of Bax localization and apoptotic activity by Pro168.

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7 January 2021

To trigger apoptosis, Bak exposes its BH3 domain and homodimerizes via BH3:groove interactions.

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7 January 2021

Translocation of a Bak C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax apoptotic function

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7 January 2021

Conformational changes in BAK, a pore-forming proapoptotic Bcl-2 family member, upon membrane insertion and direct evidence for the existence of BH3-BH3 contact interface in BAK homo-oligomers

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7 January 2021

Organization of the mitochondrial apoptotic BAK pore: oligomerization of the BAK homodimers

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7 January 2021

BIM-mediated membrane insertion of the BAK pore domain is an essential requirement for apoptosis

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7 January 2021

Conformation of the Bax C-terminus regulates subcellular location and cell death

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7 January 2021

Single color FRET based measurements of conformational changes of proteins resulting from translocation inside cells

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7 January 2021

Conformational rearrangements in the pro-apoptotic protein, Bax, as it inserts into mitochondria: a cellular death switch

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7 January 2021

Mechanistic differences in the membrane activity of Bax and Bcl-xL correlate with their opposing roles in apoptosis.

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7 January 2021

Pushing the size limit of de novo structure ensemble prediction guided by sparse SDSL-EPR restraints to 200 residues: The monomeric and homodimeric forms of BAX

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7 January 2021

Measuring membrane penetration with depth-dependent fluorescence quenching: distribution analysis is coming of age.

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7 January 2021

Membrane insertion of the BAX core, but not latch domain, drives apoptotic pore formation

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7 January 2021

Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb

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7 January 2021

Water accessibility in a membrane-inserting peptide comparing Overhauser DNP and pulse EPR methods.

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7 January 2021

Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy

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7 January 2021

Utilizing ESEEM spectroscopy to locate the position of specific regions of membrane-active peptides within model membranes

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7 January 2021

The expression of a new variant of the pro-apoptotic molecule Bax, Baxpsi, is correlated with an increased survival of glioblastoma multiforme patients

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7 January 2021

The N-terminal end of Bax contains a mitochondrial-targeting signal.

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7 January 2021

The N-terminal conformation of Bax regulates cell commitment to apoptosis

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7 January 2021

Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins

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7 January 2021

BAK/BAX macropores facilitate mitochondrial herniation and mtDNA efflux during apoptosis.

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7 January 2021

The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis

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7 January 2021

The membrane activity of BOK involves formation of large, stable toroidal pores and is promoted by cBID.

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7 January 2021

Membrane curvature at a glance

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7 January 2021

How proteins produce cellular membrane curvature

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7 January 2021

A cost-benefit analysis of the physical mechanisms of membrane curvature

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7 January 2021

Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells

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7 January 2021

Bax transmembrane domain interacts with prosurvival Bcl-2 proteins in biological membranes

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7 January 2021

The EMBL-EBI bioinformatics web and programmatic tools framework.

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7 January 2021

10.1038/S41418-018-0184-6

Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30185826 AND SRC:MED&resulttype=core&format=json

21 April 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30185826 AND SRC:MED&resulttype=core&format=json

21 April 2020

PubMed publication ID

30185826

1 reference