Receptor for RACK1 Mediates Activation of JNK by Protein Kinase C

López-Bergami, Pablo; Habelhah, Hasem; Bhoumik, Anindita; Zhang, Weizhou; Wang, Lu‐Hai; Ronai, Ze’ev

doi:10.1016/j.molcel.2005.08.005

Cited by 66 publications

(121 citation statements)

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“…After treatment of cells with ultraviolet B or anisomysin, we also observed that the low c-Jun level in siRack1 cells is a general phenomenon (Supplementary Figure S2C). Others have reported that JNKs activity is decreased after Rack1 knockdown (Lopez-Bergami et al, 2005). However, our results indicated that Rack1 knockdown in JB6 cells had no effect on JNKs phosphorylation or JNKs activity toward its substrate ATF2 (Supplementary Figure S2C), which suggested that the low c-Jun protein level is not related to JNKs activity in JB6 cells.…”

Section: Rack1 Promotes Cell Transformation By Maintaining C-jun Protcontrasting

confidence: 65%

“…Through its WD40 domains, Rack1 can bind one or two other molecules to form a complex that has an important role in various cellular functions (Schechtman and Mochly-Rosen, 2001). For example, Rack1 functions as an adaptor protein between activated protein kinase C and JNKs to enhance JNKs phosphorylation (Lopez-Bergami et al, 2005) and regulates translation as a component of the 80S ribosome (Sengupta et al, 2004). Rack1 also promotes degradation of HIF1a (Liu et al, 2007) and BimEL (Zhang et al, 2008) by mediating the interaction between each of these proteins and the ubiquitin complex.…”

Section: Introductionmentioning

confidence: 99%

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Rack1 protects N-terminal phosphorylated c-Jun from Fbw7-mediated degradation

Zhang

Zhu

et al. 2011

Oncogene

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Section: Rack1 Promotes Cell Transformation By Maintaining C-jun Protcontrasting

confidence: 65%

Section: Introductionmentioning

confidence: 99%

Rack1 protects N-terminal phosphorylated c-Jun from Fbw7-mediated degradation

Zhang

Zhu

et al. 2011

Oncogene

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“…As PKC is known to both scaffold with and phosphorylate JNK (Lopez-Bergami et al, 2005;Ping, 2003;Pontrelli et al, 2004), we propose that in wild-type mice, morphine recruitment of PKC activates JNK but that barrestin 2 recruitment limits further JNK activation. However, if b-arrestin 2 is absent and is coupled with the inability of morphine to recruit b-arrestin 1 (Groer et al, 2011), sufficient PKC recruitment results in sustained activation of the JNK cascade in b-arr2À/À neurons to affect analgesia.…”

Section: Discussionmentioning

confidence: 94%

Evidence that Behavioral Phenotypes of Morphine in β-arr2−/− Mice Are Due to the Unmasking of JNK Signaling

Mittal

Tan

Egbuta

et al. 2012

Neuropsychopharmacol

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The altered behavioral effects of morphine, but not most other mu agonists, in mice lacking b-arrestin 2, suggest that this scaffolding protein regulates the signaling cascade of this commonly used analgesic. One of the cascades that could be regulated by b-arrestin 2 is cJun-N-terminal kinase (JNK), which binds with b-arrestin 2 and modulates the analgesic effects of morphine. Using neurons lacking b-arrestin 2 (b-arr2À/À) to examine this interaction, we found that b-arr2À/À neurons show altered intracellular distribution of JNK and cJun, and that morphine, but not fentanyl, increased the nuclear localization of the phosphorylated, therefore activated, form of cJun, a JNK target in dorsal root ganglia neurons. This suggests that deleting b-arrestin 2 affects the JNK cascade. We therefore examined whether some of the behavioral phenotypes of mice lacking b-arrestin 2 could be a result of altered JNK signaling. Indeed, two different JNK inhibitors reversed the enhanced analgesic effect of morphine, a known phenotype of b-arr2À/À mice, to + / + levels. Both the reduced locomotor effect of morphine and the psychomotor sensitization to repeated morphine administration in b-arr2À/À mice were also returned to + / + levels by inhibiting JNK. In contrast, the behavioral effects of fentanyl were neither genotype-dependent nor affected by JNK inhibition. Furthermore, a PKC inhibitor had a similar effect as inhibiting JNK in reducing the enhanced analgesic effect of morphine in b-arr2À/À mice to + / + levels. In summary, removing b-arrestin 2 reveals mu receptor activation of the JNK cascade in a ligand-specific manner explaining several behavioral phenotypes of b-arr2À/À mice.

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“…Bax and JNK are binding partners of RACK1 (28,60). Currently it is still not clear how these proteins interact and act during IBDV infection.…”

Section: Discussionmentioning

confidence: 99%

The Association of Receptor of Activated Protein Kinase C 1(RACK1) with Infectious Bursal Disease Virus Viral Protein VP5 and Voltage-dependent Anion Channel 2 (VDAC2) Inhibits Apoptosis and Enhances Viral Replication

Lin

Zhang

et al. 2015

Journal of Biological Chemistry

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Background: IBDV VP5 protein induces apoptosis in DF-1 cells via interaction with VDAC2. Results: RACK1 inhibits IBDV-induced apoptosis, enhances viral replication, and interacts with both VDAC2 and VP5. Conclusion: RACK1 forms a complex with VDAC2 and VP5, affecting IBDV-induced apoptosis and viral replication. Significance: RACK1 inhibits apoptosis via interaction with VDAC2, indicating sequestration of RACK1 and VDAC2 by VP5 during IBDV infection.

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Receptor for RACK1 Mediates Activation of JNK by Protein Kinase C

Abstract: There was an error in the Experimental Procedures section under the subheading "Crystallization." The complex cocrystals were obtained with a final DNA concentration of 0.85 mM (not nM).

Cited by 66 publications

References 0 publications

Rack1 protects N-terminal phosphorylated c-Jun from Fbw7-mediated degradation

Rack1 protects N-terminal phosphorylated c-Jun from Fbw7-mediated degradation

Evidence that Behavioral Phenotypes of Morphine in β-arr2−/− Mice Are Due to the Unmasking of JNK Signaling

The Association of Receptor of Activated Protein Kinase C 1(RACK1) with Infectious Bursal Disease Virus Viral Protein VP5 and Voltage-dependent Anion Channel 2 (VDAC2) Inhibits Apoptosis and Enhances Viral Replication

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