JIP3 Mediates TrkB Axonal Anterograde Transport and Enhances BDNF Signaling by Directly Bridging TrkB with Kinesin-1

Huang, Shuhong; Duan, Shan; Sun, Tao; Wang, Jue; Zhao, Ling; Zhao, Guanghui; Yan, Junkai; Sun, Hongchen; Chen, Zhe-Yu

doi:10.1523/jneurosci.0436-11.2011

Cited by 80 publications

(96 citation statements)

References 61 publications

(70 reference statements)

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“…4, A-C) (14). The JIP3(1-625) mutant had a similar capacity to enhance axon elongation compared with wild type JIP3 (Fig.…”

Section: Jip3 Enhances Cortical Neuronal Axon Elongation In Vivo-mentioning

confidence: 83%

“…Four constructs were used in our studies as follows: scrambled siRNA sequence together with EGFP (scramble); fusion protein of JIP3 and EGFP (JIP3-EGFP); JIP3 siRNA sequence (14) together with EGFP (siJIP3), and JIP3 siRNA sequence together with RNAi-resistant JIP3 fused with EGFP (siJIP3 ϩ rJIP3-EGFP). The expression levels of JIP3-EGFP fusion protein were approximately twice the amount of endogenous JIP3 (Fig.…”

Section: Jip3 Enhances Axon Elongation In Hippocampal Neurons In Vitro-mentioning

confidence: 99%

“…4D), suggesting that amino acids 1-625 were sufficient for JIP3 to promote axon elongation. It has been reported that several functional domains exist in the 1-625-amino acid region of JIP3, namely the kinesin binding domain (KBD) (6), JNK binding domain (JBD) (4, 6), leucine zipper-like domain (LZ) (4), coiledcoil 1 (CC1) (14), and coiled-coil 2 (CC2) (4). To more precisely define the regions required for its effect on axon elongation, four JIP3 mutants with KBD and LZ (JIP3⌬⌬), JBD (JIP3⌬JBD), and CC1 (JIP3⌬CC1) or CC2 (JIP3⌬CC2) domain deletions were constructed (Fig.…”

Section: Jip3 Enhances Cortical Neuronal Axon Elongation In Vivo-mentioning

confidence: 99%

“…The JNK pathway is involved in axon formation/polarization, extension, synaptic plasticity, and dendrite development (7)(8)(9)(10)(11). Moreover, as a homology of UNC-16 in Caenorhabditis elegans and Sunday Driver in Drosophila, JIP3 is implicated as an adaptor protein in kinesin-dependent vesicular transport to axons (12,13) and has recently been reported to be a mediator in TrkB anterograde axonal transport in hippocampal neurons (14). Interestingly, JIP3 is selectively expressed in the embryonic and adult mouse brains (3,4).…”

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confidence: 99%

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c-Jun NH2-terminal Kinase (JNK)-interacting Protein-3 (JIP3) Regulates Neuronal Axon Elongation in a Kinesin- and JNK-dependent Manner

Sun

Zhai

et al. 2013

Journal of Biological Chemistry

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“…4, A-C) (14). The JIP3(1-625) mutant had a similar capacity to enhance axon elongation compared with wild type JIP3 (Fig.…”

Section: Jip3 Enhances Cortical Neuronal Axon Elongation In Vivo-mentioning

confidence: 83%

Section: Jip3 Enhances Axon Elongation In Hippocampal Neurons In Vitro-mentioning

confidence: 99%

Section: Jip3 Enhances Cortical Neuronal Axon Elongation In Vivo-mentioning

confidence: 99%

mentioning

confidence: 99%

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c-Jun NH2-terminal Kinase (JNK)-interacting Protein-3 (JIP3) Regulates Neuronal Axon Elongation in a Kinesin- and JNK-dependent Manner

Sun

Zhai

et al. 2013

Journal of Biological Chemistry

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“…21 On the other hand, JIP1 and JSAP1 were recently shown to be important for the anterograde axonal transport of plasmalemmal precursor vesicles and TrkB, respectively, in rat neurons. 22,23 Collectively, these data indicate that the regulation of axonal transport in mammals is complex, with JIPs mediating the transport of selective cargo. It is also possible that mammalian JIPs function redundantly, at least in part, in regulating axonal transport.…”

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confidence: 92%

JSAP1/JIP3 and JLP regulate kinesin-1-dependent axonal transport to prevent neuronal degeneration

et al. 2015

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Axonal transport is critical for neuronal development and function, and defective axonal transport has been implicated in neurodegenerative diseases. However, how axonal transport is regulated, or how defective transport leads to neuronal degeneration, remains unclear. Here, we report that c-Jun NH 2 -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. Mice with a double-knockout (dKO) in Jsap1 and Jlp in the dorsal telencephalon developed progressive neuron loss. Using a primary neuron culture system with induced disruption of targeted genes, combined with gene rescue experiments, we show that JSAP1 and JLP regulate kinesin-1-dependent axonal transport with functional redundancy. We also show that the binding of JSAP1 and JLP to kinesin-1 heavy chain is crucial for interactions between kinesin-1 and microtubules. Furthermore, we describe a molecular mechanism by which defective kinesin-1-dependent axonal transport in Jsap1:Jlp dKO neurons causes axonal degeneration and subsequent neuronal death. JNK hyperactivation because of increased intra-axonal Ca 2+ in the Jsap1:Jlp dKO neurons was found to mediate both the axonal degeneration and neuronal death, in cooperation with the Ca 2+ -dependent protease calpain. Our results indicate that axonal JNK may relocate to the nucleus in a dynein-dependent manner, where it activates the transcription factor c-Jun, resulting in neuronal death. Taken together, our data establish JSAP1 and JLP as positive regulators of kinesin-1-dependent axonal transport, which prevents neuronal degeneration.

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The many disguises of the signalling endosome

2018

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Neurons are highly complex and polarised cells that must overcome a series of logistic challenges to maintain homeostasis across their morphological domains. A very clear example is the propagation of neurotrophic signalling from distal axons, where target‐released neurotrophins bind to their receptors and initiate signalling, towards the cell body, where nuclear and cytosolic responses are integrated. The mechanisms of propagation of neurotrophic signalling have been extensively studied and, eventually, the model of a ‘signalling endosome’, transporting activated receptors and associated complexes, has emerged. Nevertheless, the exact nature of this organelle remains elusive. In this Review, we examine the evidence for the retrograde transport of neurotrophins and their receptors in endosomes, outline some of their diverse physiological and pathological roles, and discuss the main interactors, morphological features and trafficking destinations of a highly flexible endosomal signalling organelle with multiple molecular signatures.

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JIP3 Mediates TrkB Axonal Anterograde Transport and Enhances BDNF Signaling by Directly Bridging TrkB with Kinesin-1

Abstract: Brain-derived neurotrophic factor (BDNF),

Cited by 80 publications

References 61 publications

c-Jun NH2-terminal Kinase (JNK)-interacting Protein-3 (JIP3) Regulates Neuronal Axon Elongation in a Kinesin- and JNK-dependent Manner

c-Jun NH2-terminal Kinase (JNK)-interacting Protein-3 (JIP3) Regulates Neuronal Axon Elongation in a Kinesin- and JNK-dependent Manner

JSAP1/JIP3 and JLP regulate kinesin-1-dependent axonal transport to prevent neuronal degeneration

The many disguises of the signalling endosome

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