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Reassembly of JIP1 scaffold complex in JNK MAP kinase pathway using heterologous protein interactions
- Source :
- PLoS ONE, Vol 9, Iss 5, p e96797 (2014), PLoS ONE
- Publication Year :
- 2014
- Publisher :
- Public Library of Science (PLoS), 2014.
-
Abstract
- Formation of signaling protein complexes is crucial for proper signal transduction. Scaffold proteins in MAP kinase pathways are thought to facilitate complex assembly, thereby promoting efficient and specific signaling. To elucidate the assembly mechanism of scaffold complexes in mammals, we attempted to rationally rewire JIP1-dependent JNK MAP kinase pathway via alternative assembly of JIP1 complex. When JIP1-JNK docking interaction in the complex was replaced with heterologous protein interaction domains, such as PDZ domains and JNK-binding domains, a functional scaffold complex was reconstituted, and JNK signaling was rescued. Reassembly of JIP1 complex using heterologous protein interactions was sufficient for restoring of JNK MAP kinase pathway to induce signaling responses, including JNK activation and cell death. These results suggest a simple yet modular mechanism for JIP1 scaffold assembly in mammals.
- Subjects :
- Scaffold protein
Cell biology
Cell signaling
MAPK signaling cascades
Stress signaling cascade
MAP Kinase Signaling System
PDZ domain
Intracellular Space
PDZ Domains
Heterologous
lcsh:Medicine
Signal transduction
Biochemistry
Cell Line
Protein–protein interaction
Mice
Signal Initiation
Molecular Cell Biology
Animals
Humans
Protein Interactions
lcsh:Science
Protein kinase signaling cascade
Adaptor Proteins, Signal Transducing
Multidisciplinary
Biology and life sciences
biology
Mechanisms of Signal Transduction
lcsh:R
JNK Mitogen-Activated Protein Kinases
Proteins
Signaling cascades
c-Jun N-terminal kinase signaling cascade
Transport protein
Protein Transport
Mitogen-activated protein kinase
Mutation
biology.protein
Phosphorylation
lcsh:Q
Protein Binding
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 9
- Issue :
- 5
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....e52756a33847414d387a151c75314577