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

By Sandeep R. Datta, A. Katsov, Linda S. Hu, A. Petros, Stephen W. Fesik, Michael B. Yaffe, Michael E. Greenberg. Molecules and Cells, 2000

653 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/811210e360d7f34ad9e4fe2c187a1c0340cd6d3b

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Cell Death Signaling. (2015, background): “…Yan et al. 2003 Phosphorylation PAK Cell survival Schürmann et al. 2000; Cotteret et al. 2003 Sequestration 14-3-3 Cell survival Zha et al. 1996; Datta et al. 2000 TNF Phosphorylation IKK Cell survival Yan et al. 2013 Neuronal activity deprivation Phosphorylation Cdc2 Apoptosis Konishi et al.…”
Mitochondrial membrane permeabilization in cell death. (2007, background): “Bad phosphorylated on serine112 or -136 by antiapoptotic kinases is sequestered by proteins of the 14–3-3 family and maintained in an inactive cytosolic localization (162).”
AKT/PKB signaling: navigating downstream. (2007, neutral): “Survival factors stimulate Akt-mediated phosphorylation of BAD on S136, and this creates a binding site for 14-3-3 proteins, which triggers release of BAD from its target proteins (Datta et al., 2000).”
Bcl-2 family members: intracellular targeting, membrane-insertion, and changes in subcellular localization (2004, background): “This phosphorylation event has been reported to decrease the affinity of Bad for Bcl-2 [83,86].”
Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model. (2004, neutral): “Activation of the antiapoptotic PI3-kinase cascade phosphorylates BAD at serine 136 (pBAD), through Akt or PAK, promoting its binding to 14-3-3 protein and preventing subsequent caspase activation (Datta et al., 2000; Schurmann et al., 2000; Yuan and Yankner, 2000).”
Anoikis molecular pathways and its role in cancer progression. (2013, background): “Bad on Ser136 [53,54,56], causing the release of Bcl-2 and directly inhibits the caspase cascade by phosphorylating the procaspase-9 [38].”
Protein Kinase SGK Mediates Survival Signals by Phosphorylating the Forkhead Transcription Factor FKHRL1 (FOXO3a) (2001, background): “A role for 14-3-3 proteins as cofactors that promote sequential protein phosphorylation was recently demonstrated for another Akt target, the Bcl-2 family member BAD (18).”
cGMP-Dependent Protein Kinases and cGMP Phosphodiesterases in Nitric Oxide and cGMP Action (2010, background): “Phosphorylation at Ser-155 blocks Bad binding to Bcl-xL, thereby fostering cytoprotection (Datta et al., 2000; Tan et al., 2000; Zhou et al., 2000).”
PI3K/Akt: getting it right matters (2008, background): “The importance of BAD as an integration point of survival signaling is underscored by the fact that it is a substrate for multiple independent kinase pathways in cells, not all of which phosphorylate BAD at the same site(s) as Akt (Datta et al., 2000).”
Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins (2002, background): “PKA has also been shown to phosphorylate serine 155 within the BH3 domain of Bad, thereby reducing its affinity for pro-survival Bcl-2 family members.(57) It therefore appears that reprieve from a Badimposed death sentence can occur at several locations within the cell.”
The expanding role of mitochondria in apoptosis. (2001, background): “Conversely, in the presence of trophic factors, Akt and mitochondria-anchored PKA phosphorylate Bad, allowing it to bind 14-3-3 protein and to remain in the cytosol (Datta et al. 1997; Harada et al. 1999).”