Why doregulators of apoptosis look like bacterial toxins?

Current Biology

Volumn 11, Issue 19, 2001, Pages

  Lazebnik, Yuri ^a  

^a Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COLICIN; DIPHTHERIA TOXIN; PROTEIN BCL 2;

APOPTOSIS; CHEMISTRY; HUMAN; METABOLISM; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; REVIEW; TRANSPORT AT THE CELLULAR LEVEL;

APOPTOSIS; BIOLOGICAL TRANSPORT; COLICINS; DIPHTHERIA TOXIN; HUMANS; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-BCL-2;

EID: 0035797909     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(01)00465-1     Document Type: Note

References (14)

1. BCL-2 family members and the mitochondria in apoptosis
2. Life-or-death decisions by the Bcl-2 protein family
3. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
4. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
5. The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
6. X-ray and NMR structure of human Bcl-xL, an inhibitor of programmed cell death
7. Pore-forming colicins and their relatives
8. Bcl-2 family proteins as ion-channels
9. Structure of bax. Coregulation of dimer formation and intracellular localization
10. Penetration of protein toxins into cells
11. GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity
12. Receptor-mediated uptake of an extracellular Bcl-x(L) fusion protein inhibits apoptosis
13. Membrane translocation of diphtheria toxin carrying passenger protein domains
14. The substitution of the C-terminus of bax by that of bcl-xL does not affect its subcellular localization but abrogates its pro-apoptotic properties