JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis

By Kui Lei, R. Davis. Proceedings of the National Academy of Sciences of the United States of America, 2003

1,157 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/4d9e0db237c3ff0b53cbfc7811324dc6a700c088

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Citations in the corpus

Endoplasmic Reticulum Stress in Liver Disease (2010, background): “JNK has several proapoptotic effects, including phosphorylationinduced activation of the proapoptotic Bim, and inactivation of the antiapoptotic Bcl2 proteins [75,149].”
Role of Bcl-2 family proteins and caspases in the regulation of apoptosis (2011, background): “However, c-Jun N-terminal protein kinase (JNK) that causes phosphorylation of Bim is involved in ischemiainduced neuronal apoptosis through activation and translocation of Bax [82, 83].”
Cell Biology of Ischemia/Reperfusion Injury (2012, background): “, 2000), both MAPKs have also been shown to phosphorylate and activate several pro-death Bcl2 proteins (Bright et al., 2004; Donovan et al., 2002; Lei and Davis, 2003; Metukuri et al., 2009; Murriel et al., 2004; Sitailo et al., 2004; Zhuang et al., 2000).”
JNK Signaling in Apoptosis (2008, background): “JNK has also been observed to modulate the activities of other pro-apoptotic BH3-only subgroup of Bcl2 family of proteins such as Bim and Bmf (Lei and Davis, 2003).”
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “The IRE1α–ASK1–JNK signalling pathway is also connected to a cell death mechanism, whereby JNK-mediated phosphorylation has been reported to activate the pro-apoptotic BCL-2 family member BIM (also known as BCL2L11”
The Bcl-2 family: roles in cell survival and oncogenesis (2003, background): “In contrast, UV irradiation of cells releases both Bim and Bmf, and their release is mediated via phosphorylation of the conserved DLC binding motif by JNK (Lei and Davis, 2003).”
Oxygen Toxicity and Reactive Oxygen Species: The Devil Is in the Details (2009, background): “ROS can activate c-Jun N-terminal kinase (possibly through production of lipid peroxide intermediates), a crucial mitogen-activated protein kinase, which then phosphorylates and releases two Bcl-2–related proteins that are normally sequestered within the cell (15,16).”
Endoplasmic Reticulum Stress and Associated ROS (2016, background): “IRE1α also activates apoptotic signaling kinase-1 (ASK-1), activating downstream factors such as Jun-N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (p38 MAPK), which enhance apoptosis [15–17].”
ER stress-induced cell death mechanisms. (2013, background): “Among the apoptosis-inducing substrates of JNK are Bcl-2 and Bim, which are inhibited and activated, respectively, by JNK phosphorylation [6,7].”
Understanding MAPK Signaling Pathways in Apoptosis (2020, background): “During UV-induced apoptosis, Bim and Bmf (Bcl-2-modifying factor), normally sequestered by dynein and myosin V motor complexes, are released by JNK-dependent phosphorylation [46].”
The role of BH3-only proteins in the immune system (2005, background): “Finally, it has also been reported that, in growth-factor-deprived neurons or ultraviolet-light-irradiated fibroblasts, BIM can be activated by the kinase JNK (JUN amino-terminal kinase), either through direct phosphorylation (presumably on sites distinct from those phosphorylated by ERK”