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Stoichiometry and regulation network of Bcl-2 family complexes quantified by live-cell FRET assay.
Yang, Fangfang; Qu, Wenfeng; Du, Mengyan; Mai, Zihao; Wang, Bin; Ma, Yunyun; Wang, Xiaoping; Chen, Tongsheng.
Afiliação
  • Yang F; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Qu W; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Du M; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Mai Z; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Wang B; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Ma Y; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China.
  • Wang X; Department of Pain Management, The First Affiliated Hospital of Jinan University, Guangzhou, China. txp2938@jnu.edu.cn.
  • Chen T; MOE Key Laboratory of Laser Life Science and College of Biophotonics, South China Normal University, Guangzhou, China. chentsh@scnu.edu.cn.
Cell Mol Life Sci ; 77(12): 2387-2406, 2020 Jun.
Article em En | MEDLINE | ID: mdl-31492967
The stoichiometry and affinity of Bcl-2 family complexes are essential information for understanding how their interactome network is orchestrated to regulate mitochondrial permeabilization and apoptosis. Based on over-expression model system, FRET analysis was used to quantify the protein-protein interactions among Bax, Bcl-xL, Bad and tBid in healthy and apoptotic cells. Our data indicate that the stoichiometry and affinity of Bcl-2 complexes are dependent on their membrane environment. Bcl-xL, Bad and tBid can form hetero-trimers in mitochondria. Bcl-xL binds preferentially to Bad, then to tBid and Bax in mitochondria, whilst Bcl-xL displays higher affinity to Bad or tBid than to itself. Strikingly, Bax can bind to Bcl-xL in cytosol. In cytosol of apoptotic cells, Bcl-xL associates with Bax to form hetero-trimer with 1:2 stoichiometry, while Bcl-xL associates with Bad to form hetero-trimer with 2:1 stoichiometry and Bcl-xL associates with tBid to form hetero-dimer. In mitochondria, Bcl-xL associates with Bax/Bad to form hetero-dimer in healthy cells, while Bcl-xL associates with Bad to form hetero-tetramer with 3:1 stoichiometry in apoptotic cells.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Proto-Oncogênicas c-bcl-2 Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas Proto-Oncogênicas c-bcl-2 Tipo de estudo: Prognostic_studies Limite: Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article