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c-Jun N-terminal kinase (JNK) Inhibitor: SU 3327
No.178(July 2018)
SU 3327 (1) is a JNK (c-Jun N-terminal kinase) inhibitor developed based on structure-activity relationship studies.1) 1 inhibits activating transcription factor-2 (AFT-2) phosphorylation by JNK1 with IC50 = 0.7 μM in a substrate competitive manner. 1 also inhibits protein-protein interaction between JNK and JIP-1* with IC50 = 239 nM.
As one of the important roles JNK plays in the induction of autophagy via stimulations as shown in Table 1. It has been demonstrated that acute ethanol treatment decreased autophagy in mouse models and the decrease in autophagy was prevented by 1.2)
* JIP-1: JNK-interacting proteins (JIP) were identified as JNK scaffold proteins.3,4) JIP1 is a member of the JIP family and contains a JNK binding domain (JBD), a SRC homology (SH3) domain, and phosphotyrosine-binding (PTB) domain. JBD possesses the consensus sequence, R/KXXXXLXL.5) The probe, pep-JIP1, used in the reference (1), contains the sequence.
Table 1. Autophagy by various stimuli implicating JNK
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References
- 1)Design, synthesis, and structure-activity relationship of substrate competitive, selective, and in vivo active triazole and thiadiazole inhibitors of the c-Jun N-terminal kinase
- 2)Cytochrome P4502E1, oxidative stress, JNK and autophagy in acute alcohol-induced fatty liver
- 3)Scaffold proteins of MAP-kinase modules
- 4)A mammalian Scaffold complex that selectively mediated MAP kinase activation
- 5)Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1
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