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- W4386328180 endingPage "13527" @default.
- W4386328180 startingPage "13527" @default.
- W4386328180 abstract "The response of cells to extracellular signals is mediated by a variety of intracellular signaling pathways that determine stimulus-dependent cell fates. One such pathway is the cJun-N-terminal Kinase (JNK) cascade, which is mainly involved in stress-related processes. The cascade transmits its signals via a sequential activation of protein kinases, organized into three to five tiers. Proper regulation is essential for securing a proper cell fate after stimulation, and the mechanisms that regulate this cascade may involve the following: (1) Activatory or inhibitory phosphorylations, which induce or abolish signal transmission. (2) Regulatory dephosphorylation by various phosphatases. (3) Scaffold proteins that bring distinct components of the cascade in close proximity to each other. (4) Dynamic change of subcellular localization of the cascade's components. (5) Degradation of some of the components. In this review, we cover these regulatory mechanisms and emphasize the mechanism by which the JNK cascade transmits apoptotic signals. We also describe the newly discovered PP2A switch, which is an important mechanism for JNK activation that induces apoptosis downstream of the Gq protein coupled receptors. Since the JNK cascade is involved in many cellular processes that determine cell fate, addressing its regulatory mechanisms might reveal new ways to treat JNK-dependent pathologies." @default.
- W4386328180 created "2023-09-01" @default.
- W4386328180 creator A5060540188 @default.
- W4386328180 creator A5060633986 @default.
- W4386328180 creator A5079331236 @default.
- W4386328180 date "2023-08-31" @default.
- W4386328180 modified "2023-10-05" @default.
- W4386328180 title "JNK Cascade-Induced Apoptosis—A Unique Role in GqPCR Signaling" @default.
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