14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation

Molecular Cell

Volumn 6, Issue 1, 2000, Pages 41-51

  Datta, Sandeep Robert ^a   Katsov, Alex ^a   Hu, Linda ^a   Petros, Andrew ^b   Fesik, Stephen W ^b   Yaffe, Michael B ^c   Greenberg, Michael E ^a  

^a BOSTON CHILDREN S HOSPITAL   (United States)

^b ABBOTT LABORATORIES   (United States)

^c BETH ISRAEL DEACONESS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOTRANSFERASE; PROTEIN BCL 2; PROTEIN KINASE;

ANIMAL CELL; ANIMAL EXPERIMENT; APOPTOSIS; ARTICLE; CELL SURVIVAL; GENE INACTIVATION; METABOLIC REGULATION; NONHUMAN; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; RABBIT; SEQUENCE HOMOLOGY;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0033635235     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(05)00012-2     Document Type: Article

References (31)

1. Akt promotes cell survival by phosphorylating and inhibiting a forkhead transcription factor
2. Equilibrium and kinetic inhibition assays based upon fluorescence polarization
3. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
4. Cellular survival: A play in three Akts
5. Regulated targeting of BAX to mitochondria
6. SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative protein modeling
7. Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A
8. Interference of BAD (BCL-X(L)/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11
9. Bad is a BH3 domain-containing molecule that forms an inactivating dimer with BCL-X(L)
10. Akt/protein kinase B inhibits cell death by preventing the release of cytochrome c from mitochondria
11. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
12. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
13. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
14. Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine
15. Differential regulation of gene expression by insulin and IGF-1 receptors correlates with phosphorylation of a single amino acid residue in the forkhead transcription factor FKHR
16. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
17. Checkpoints of dueling dimers foil death wishes
18. Dimerization properties of human Bad: Identification of a BH-3 domain and analysis of its binding to mutant Bcl-2 and BCL-X(L) proteins
19. ProMod and Swiss-Model: Internet based tools for automated comparative protein modeling
20. The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex
21. Bcl-2 family proteins
22. Structure of BCL-X(L)-Bak peptide complex: Recognition between regulators of apoptosis
23. Use of an oriented peptide library to determine the optimal subtrates of protein kinases
24. 14-3-3 isotypes facilitate coupling of protein kinase C-zeta to Raf-1: Negative regulation by 14-3-3 phosphorylation
25. Cell death in development
26. 2+-induced apoptosis through calcineurin dephosphorylation of Bad
27. 14-3-3 proteins block apoptosis and differentially regulate MAPK cascades
28. The structural basis for 14-3-3: Phosphopeptide binding specificity
29. Bad, a heterodimeric partner for BCL-X(L) and Bcl-2, displaces BAX and promotes cell death
30. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
31. BH3 domain of Bad is required for heterodimerization with BCL-X(L) and proapoptotic activity