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Isoform-specific palmitoylation of JNK regulates axonal development
1College of Interdisciplinary Studies, University of British Columbia, Brain Research Centre, 2211 Wesbrook Mall, Vancouver, BC V6T2B5, Canada. photonyg@interchange.ubc.ca
Cell Death and Differentiation
|September 24, 2011
Summary
Post-translational modification by palmitoylation specifically regulates JNK3, impacting axonal development. This finding reveals a novel mechanism controlling JNK3
Area of Science:
- Neuroscience
- Molecular Biology
- Cell Biology
Background:
- The c-jun N-terminal kinase (JNK) family, with 10 isoforms in the mammalian brain, plays critical roles in neuronal cell death and development.
- Mechanisms regulating specific JNK isoforms for distinct functions remain largely unknown.
Purpose of the Study:
- To investigate the isoform-specific regulation of JNK3.
- To explore the role of JNK3 palmitoylation in axonal development and morphogenesis.
Main Methods:
- Investigated JNK3 regulation via palmitoylation, a post-translational modification.
- Utilized cultured hippocampal neurons to study JNK3's effect on axonal branching and filopodia motility.
- Examined the interaction between JNK3 palmitoylation and Wnt7a signaling.
Main Results:
- Identified two COOH-terminal cysteine residues essential for dynamic JNK3 palmitoylation, regulating its actin cytoskeleton distribution.
- Palmitoylation-deficient JNK3 enhanced axonal branching and filopodia motility in neurons.
- Wnt7a regulates JNK3 palmitoylation and distribution; palmitoylation-deficient JNK3 mimicked Wnt7a's effects on axonal branching.
Conclusions:
- Protein palmitoylation is a novel mechanism for isoform-specific regulation of JNK3.
- JNK3 palmitoylation plays a significant role in modulating axonal branching and neuronal development.
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