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Mitogen-activated protein kinase 8 interacting protein 3

JSAP1, JIP3, JNK-interacting protein 3
The protein encoded by this gene shares similarity with the product of Drosophila syd gene, required for the functional interaction of kinesin I with axonal cargo. Studies of the similar gene in mouse suggested that this protein may interact with, and regulate the activity of numerous protein kinases of the JNK signaling pathway, and thus function as a scaffold protein in neuronal cells. The C. elegans counterpart of this gene is found to regulate synaptic vesicle transport possibly by integrating JNK signaling and kinesin-1 transport. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: JNK, AP-1, IB1, MAPK, V1a
Papers on JSAP1
Effects of JIP3 on epileptic seizures: evidence from temporal lobe epilepsy patients, kainic-induced acute seizures and pentylenetetrazole-induced kindled seizures.
Wang et al., Chongqing, China. In Neuroscience, 19 Jun 2015
UNASSIGNED: JNK-interacting protein3 (JIP3), also known as JNK stress-activated protein kinase-associated protein 1 (JSAP1), is a scaffold protein mainly involved in the regulation of the pro-apoptotic signaling cascade mediated by c-Jun N-terminal kinase (JNK).
JIP3 activates kinesin-1 motility to promote axon elongation.
Cavalli et al., Saint Louis, United States. In J Biol Chem, 05 Jun 2015
We previously showed that the scaffolding protein JIP3 interacts directly with KHC in addition to its interaction with KLC and positively regulates dimeric KHC motility.
JSAP1/JIP3 and JLP regulate kinesin-1-dependent axonal transport to prevent neuronal degeneration.
Yoshioka et al., Kanazawa, Japan. In Cell Death Differ, Feb 2015
Here, we report that c-Jun NH2-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1, also known as JNK-interacting protein 3 (JIP3)) and JNK-associated leucine zipper protein (JLP) are essential for postnatal brain development.
Syd/JIP3 and JNK signaling are required for myonuclear positioning and muscle function.
Baylies et al., New York City, United States. In Plos Genet, Dec 2014
Using Drosophila melanogaster, we identified that Sunday Driver (Syd), a homolog of mammalian JNK-interacting protein 3 (JIP3), specifically regulates Kinesin- and Dynein-dependent cortical pulling of myonuclei without affecting motor activity near the nucleus.
Integrated regulation of motor-driven organelle transport by scaffolding proteins.
Holzbaur et al., Philadelphia, United States. In Trends Cell Biol, Oct 2014
Recent progress demonstrates that organelle-associated scaffolding proteins, including Milton/TRAKs (trafficking kinesin-binding protein), JIP1, JIP3 (JNK-interacting proteins), huntingtin, and Hook1, interact with molecular motors to coordinate activity and sustain unidirectional transport.
JSAP1 and JLP are required for ARF6 localization to the midbody in cytokinesis.
Yoshioka et al., Kanazawa, Japan. In Genes Cells, Sep 2014
Here, we investigated the functions of two binding partners of active ARF6, c-Jun NH2 -terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) and JNK-associated leucine zipper protein (JLP), by gene knockout and rescue experiments in mouse embryonic fibroblasts.
c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) regulates neuronal axon elongation in a kinesin- and JNK-dependent manner.
Chen et al., Key West, United States. In J Biol Chem, 2013
Here, we report that c-Jun NH2-terminal kinase (JNK)-interacting protein-3 (JIP3) is highly expressed at axon tips during the critical period for axon development.
An organelle gatekeeper function for Caenorhabditis elegans UNC-16 (JIP3) at the axon initial segment.
Miller et al., Oklahoma City, United States. In Genetics, 2013
Here we use electron microscopy and quantitative imaging of tagged organelles to show that Caenorhabditis elegans axons lacking UNC-16 (JIP3/Sunday Driver) accumulate Golgi, endosomes, and lysosomes at levels up to 10-fold higher than wild type, while ER membranes are largely unaffected.
Differential regulation of M3/6 (DUSP8) signaling complexes in response to arsenite-induced oxidative stress.
Panayotou et al., Greece. In Cell Signal, 2013
Furthermore, arsenite treatment resulted in an inducible recruitment of M3/6 to JNK-interacting protein 3 (JIP3) scaffold complexes, while its interaction with JIP1 or JIP2 was constitutive.
The interaction of Kinesin-1 with its adaptor protein JIP1 can be regulated via proteins binding to the JIP1-PTB domain.
Hirai et al., Yokohama, Japan. In Bmc Cell Biol, 2012
Proteomic analysis revealed another kinesin-1 binding protein, JIP3, as a major JIP1 binding protein.
JNK-interacting protein 3 mediates the retrograde transport of activated c-Jun N-terminal kinase and lysosomes.
Nechiporuk et al., Portland, United States. In Plos Genet, 2012
Using forward genetics and a novel in vivo imaging approach, we identified JNK-interacting protein 3 (Jip3) as a direct mediator of dynein-based retrograde transport of activated (phosphorylated) c-Jun N-terminal Kinase (JNK) and lysosomes.
The Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes.
Fukuda et al., Sendai, Japan. In J Biol Chem, 2012
RILP, RILP-L1, RILP-L2, and JIP3/4, contain a conserved coiled-coil domain.
Crystal structures of the tetratricopeptide repeat domains of kinesin light chains: insight into cargo recognition mechanisms.
Park et al., Toronto, Canada. In Plos One, 2011
We further propose a third binding site on KLC1 which involves a stretch of polar residues along the inter-TPR loops that may form a network of hydrogen bonds to JIP3 and JIP4.
The Liprin homology domain is essential for the homomeric interaction of SYD-2/Liprin-α protein in presynaptic assembly.
Jin et al., Sapporo, Japan. In J Neurosci, 2011
The results of this study finding suggested that a model by which the self-assembly of SYD-2/Liprin-alpha proteins mediated by the coiled-coil LH1 domain is one of the key steps to the accumulation of presynaptic components at nascent synaptic junctions
JNK/stress-activated protein kinase associated protein 1 is required for early development of telencephalic commissures in embryonic brains.
Han et al., Seoul, South Korea. In Exp Mol Med, 2011
Results suggest that JSAP1 is required for the pathfinding of the developing telencephalic commissures in the early brains.
Sunday Driver/JIP3 binds kinesin heavy chain directly and enhances its motility.
Cavalli et al., Saint Louis, United States. In Embo J, 2011
syd activates kinesin heavy chain for transport & enhances its motility, increasing its velocity & run length. syd mutants binding KHC but not kinesin light chain are transported to axons & dendrites normally.
JIP3 mediates TrkB axonal anterograde transport and enhances BDNF signaling by directly bridging TrkB with kinesin-1.
Chen et al., Jinan, China. In J Neurosci, 2011
This study demonistrated that JIP3 mediates TrkB axonal anterograde transport and enhances BDNF signaling by directly bridging TrkB with kinesin-1.
Regulation of stress-associated scaffold proteins JIP1 and JIP3 on the c-Jun NH2-terminal kinase in ischemia-reperfusion.
Siow et al., Winnipeg, Canada. In Can J Physiol Pharmacol, 2010
JIP1 and JIP3 play important roles in the activation of JNK during simulated ischemia-reperfusion challenge in H9c2 cells.
"JIP"ing along the axon: the complex roles of JIPs in axonal transport.
Koushika, Bengaluru, India. In Bioessays, 2008
JIP1 and JIP3 were known to be adaptors linking cargo to Kinesin-I, a major molecular motor for axonal transport.
Glutamate-receptor-interacting protein GRIP1 directly steers kinesin to dendrites.
Hirokawa et al., Tokyo, Japan. In Nature, 2002
This pattern was different from that generated by the overexpression of the kinesin-binding scaffold protein JSAP1 (JNK/SAPK-associated protein-1, also known as Mapk8ip3), which occurred predominantly in the somatoaxon area.
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