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BCL-2 proteins and apoptosis: Recent insights and unknowns

Edlich, Frank

Biochemical and biophysical research communications, 2018-05, Vol.500 (1), p.26-34 [Periódico revisado por pares]

United States: Elsevier Inc

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  • Título:
    BCL-2 proteins and apoptosis: Recent insights and unknowns
  • Autor: Edlich, Frank
  • Assuntos: 60 APPLIED LIFE SCIENCES ; APOPTOSIS ; BCL-2 proteins ; BH3-only proteins ; LYMPHOMAS ; MITOCHONDRIA ; Mitochondrial apoptosis ; Retrotranslocation ; THERAPY
  • É parte de: Biochemical and biophysical research communications, 2018-05, Vol.500 (1), p.26-34
  • Notas: ObjectType-Article-2
    SourceType-Scholarly Journals-1
    ObjectType-Feature-3
    content type line 23
    ObjectType-Review-1
  • Descrição: Proteins of the B-cell lymphoma-2 (BCL-2) family control the intrinsic apoptosis pathway. The pro-apoptotic BCL-2 proteins BAX and BAK can commit a cell to its programmed death by permeabilizing the outer mitochondrial membrane (OMM) and subsequent initiation of the caspase cascade. Therefore, the activities of BAX and BAK are precisely controlled by a complex network of proteins inside and outside the BCL-2 family. Cells survive by constant control of dynamic translocation and retrotranslocation of BAX and BAK to the mitochondria and back into the cytosol. Recent insights into BAX/BAK shuttling, BCL-2 protein interactions, the role of BH3-only proteins in apoptosis signaling and the active BAX complex set the stage for the development of novel strategies in cancer therapy and the analysis of cellular predisposition to apoptosis. •The pro-apoptotic BCL-2 proteins can commit cells to apoptosis.•BAX and BAK are regulated by dynamic shuttling between mitochondria and cytosol of healthy cells.•BH3-only proteins, regulators of BAX and BAK, are not required for BAX activation.•Recent super-resolution microscopy studies provide novel insights into the active BAX complex.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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