The mitochondrial TOM complex is required for tBid/Bax-induced cytochrome c release (Q24319971)

GOA release 2020-03-11

Tom22p YNL131W

1 reference

GOA release 2020-03-11

1 reference

6

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Sten Orrenius

8

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Boris Zhivotovsky

7

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Martin Ott

1

object named as

Martin Ott

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author name string

Erik Norberg

2

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Katharina M Walter

3

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Patrick Schreiner

4

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Christian Kemper

Journal of Biological Chemistry

5

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language of work or name

English

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publication date

21 September 2007

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published in

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volume

282

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issue

38

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page(s)

27633-9

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cites work

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Cell death: critical control points

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Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

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Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis

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Inhibition of Bax channel-forming activity by Bcl-2

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Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis

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Interaction with a membrane surface triggers a reversible conformational change in Bax normally associated with induction of apoptosis

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

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Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

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Cardiolipin Is Not Required for Bax-mediated Cytochrome c Release from Yeast Mitochondria

21 January 2018

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Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein

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Cytochrome c release from mitochondria proceeds by a two-step process

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Signal-anchored proteins follow a unique insertion pathway into the outer membrane of mitochondria

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The TOM core complex: the general protein import pore of the outer membrane of mitochondria.

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VDAC2 inhibits BAK activation and mitochondrial apoptosis

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Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex

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How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?

21 January 2018

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

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Targeting and assembly of rat mitochondrial translocase of outer membrane 22 (TOM22) into the TOM complex.

21 January 2018

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

21 January 2018

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Preprotein Transport Machineries of Yeast Mitochondrial Outer Membrane Are not Required for Bax-induced Release of Intermembrane Space Proteins

21 January 2018

1 reference

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Cardiolipin provides specificity for targeting of tBid to mitochondria

21 January 2018

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

BID-dependent and BID-independent pathways for BAX insertion into mitochondria

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M703155200