Reactome | Sequestration of BAD protein by 14-3-3

Sequestration of BAD protein by 14-3-3

Stable Identifier

R-HSA-139899

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

14-3-3 proteins bind BAD phosphorylated by activated AKT on serine residue S99 (corresponds to mouse Bad serine residue S136). Binding of 14-3-3 proteins to p-S99-BAD facilitates subsequent phosphorylation of BAD on serine residue S118 (corresponds to mouse serine S155), which disrupts binding of BAD to BCL2 proteins and promotes cell survival (Datta et al. 2000). Caspase-3 mediated cleavage of 14-3-3 proteins releases BAD and promotes apoptosis (Won et al. 2003). All known 14-3-3 protein isoforms (beta/alpha i.e. YWHAB, gamma i.e. YWHAG, zeta/delta i.e. YWHAZ, epsilon i.e. YWHAE, eta i.e. YWHAH, sigma i.e. SFN and theta i.e. YWHAQ) can interact with BAD and inhibit it (Subramanian et al. 2001, Chen et al. 2005).

Literature References

PubMed ID	Title	Journal	Year
11697890	Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis Subramanian, RR, Masters, SC, Zhang, H, Fu, H	Exp. Cell Res.	2001
15660102	Association of 14-3-3gamma and phosphorylated bad attenuates injury in ischemic astrocytes Chen, XQ, Fung, YW, Yu, AC	J. Cereb. Blood Flow Metab.	2005
12657644	Cleavage of 14-3-3 protein by caspase-3 facilitates bad interaction with Bcl-x(L) during apoptosis Won, J, Kim, DY, La, M, Kim, D, Meadows, GG, Joe, CO	J Biol Chem	2003
10949026	14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation Datta, SR, Katsov, A, Hu, L, Petros, A, Fesik, SW, Yaffe, MB, Greenberg, ME	Mol. Cell	2000