Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1.

By U. Maurer, C. Charvet, A. Wagman, E. Dejardin, Douglas R. Green. Molecules and Cells, 2006

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Cell Death Signaling. (2015, background): “GSK3 then phosphorylates Mcl1, allowing its ubiquitylation by the E3 ligaseb-transductin-repeat-containing protein (b-TrCP) and its subsequent degradation (Maurer et al. 2006; Ding et al. 2007).”
Synthetic Lethality of Combined Bcl-2 Inhibition and p53 Activation in AML: Mechanisms and Superior Antileukemic Efficacy (2017, background): “p53 Activation Downregulates the Ras/Raf/MEK/ERK Signaling Cascade To determine the mechanism by which p53 activation regulates GSK3 activity, we first measured the effects of p53 expression on AKT, which is widely known to phosphorylate and inactivate GSK3 (Cohen and Frame, 2001; Maurer et al., 200”
Cracking the BAFF code (2009, background): “Finally, and in agreement with the negative regulation that BAFF and AKT1 impose on glycogen synthase kinase 3β (GSK3β) and PKCδ, these two kinases destabilize MCL1 (Ref”
ABT-263: a potent and orally bioavailable Bcl-2 family inhibitor. (2008, background): “has previously been shown to dramatically increase Bim and reduce Mcl-1 levels, resulting in the induction of apoptosis (24, 32).”
FKBP51 Affects Cancer Cell Response to Chemotherapy by Negatively Regulating Akt (2009, positive): “, 1995) that play a proapoptotic role by inhibiting antiapoptotic protein MCL-1 (Maurer et al., 2006).”