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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)
Papers on JSAP1
JNK-Interacting Protein 3 Mediates the Retrograde Transport of Activated c-Jun N-Terminal Kinase and Lysosomes.
New
Nechiporuk et al., Portland, United States. In Plos Genet, 28 Feb 2013
Using forward genetics and a novel 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.
Differential regulation of M3/6 (DUSP8) signaling complexes in response to arsenite-induced oxidative stress.
New
Panayotou et al., Greece. In Cell Signal, 28 Feb 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 Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes.
New
Fukuda et al., Sendai, Japan. In J Biol Chem, Sep 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.
GeneRIF
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
DLK induces developmental neuronal degeneration via selective regulation of proapoptotic JNK activity.
Lewcock et al., San Francisco, United States. In J Cell Biol, 2011
This specificity is dependent on interaction of DLK with the scaffolding protein JIP3 to form a specialized JNK signaling complex.
JNK/stress-activated protein kinase associated protein 1 is required for early development of telencephalic commissures in embryonic brains.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Decoupling of activation and effector binding underlies ARF6 priming of fast endocytic recycling.
Chavrier et al., Paris, France. In Curr Biol, 2011
In CCP, GTP-ARF6 mediates the recruitment of the ARF-binding domain of downstream effectors including JNK-interacting proteins 3 and 4 (JIP3 and JIP4) after the burst recruitment of the clathrin uncoating component auxilin.
Sub-cellular distribution of UNC-104(KIF1A) upon binding to adaptors as UNC-16(JIP3), DNC-1(DCTN1/Glued) and SYD-2(Liprin-α) in C. elegans neurons.
Wagner et al., Huazhou, China. In Neuroscience, 2011
Inspecting an interactome map, we identify three putative UNC-104 interactors, namely UNC-16(JIP3), DNC-1(DCTN1/Glued) and SYD-2(Liprin-α), known to be adaptors in essential neuronal protein complexes.
The Caenorhabditis elegans JIP3 protein UNC-16 functions as an adaptor to link kinesin-1 with cytoplasmic dynein.
Hisamoto et al., Nagoya, Japan. In J Neurosci, 2011
Kinesin-1 is a microtubule plus-end-directed motor that transports various cargos along the axon.
Role of plasma membrane localization of the scaffold protein JSAP1 during differentiation of cerebellar granule cell precursors.
Yoshioka et al., Kanazawa, Japan. In Genes Cells, 2011
We previously reported that the scaffold protein c-Jun NH₂-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) functions in cerebellar granule cell precursors (GCPs) to promote their cell-cycle exit and differentiation.
A JIP3-regulated GSK3β/DCX signaling pathway restricts axon branching.
Bonni et al., Boston, United States. In J Neurosci, 2011
Here we report that knockdown of the brain-enriched signaling protein JNK-interacting protein 3 (JIP3) triggers exuberant axon branching and self-contact in primary granule neurons of the rat cerebellar cortex.
Regulation of stress-associated scaffold proteins JIP1 and JIP3 on the c-Jun NH2-terminal kinase in ischemia-reperfusion.
GeneRIF
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.
Review
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.
Impact
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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