Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA (Q27675369)

1

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Frank Edlich

2

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Guillermo A Bermejo

3

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Kristi L Norris

4

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Nico Tjandra

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

18 December 2012

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published in

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volume

109

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issue

51

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page(s)

20901-6

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cites work

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Structure of Bax: coregulation of dimer formation and intracellular localization

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Bax dimerizes via a symmetric BH3:groove interface during apoptosis

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Cytomegalovirus proteins vMIA and m38.5 link mitochondrial morphogenesis to Bcl-2 family proteins

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Bax forms multispanning monomers that oligomerize to permeabilize membranes during apoptosis

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Cytomegalovirus cell death suppressor vMIA blocks Bax- but not Bak-mediated apoptosis by binding and sequestering Bax at mitochondria

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An anti-apoptotic viral protein that recruits Bax to mitochondria

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vMIA, a viral inhibitor of apoptosis targeting mitochondria

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

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An evolutionary perspective on apoptosis.

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Social controls on cell survival and cell death

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Differential function and expression of the viral inhibitor of caspase 8-induced apoptosis (vICA) and the viral mitochondria-localized inhibitor of apoptosis (vMIA) cell death suppressors conserved in primate and rodent cytomegaloviruses

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Crossref

https://api.crossref.org/works/10.1073%2FPNAS.1217094110

21 January 2018

Identifiers

DOI

10.1073/PNAS.1217094110

1 reference

3872930

ADS bibcode

2012PNAS..10920901M

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3872930

1 reference

1 reference

1 reference