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JIP3 Activates Kinesin-1 Motility to Promote Axon Elongation
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Alternative adaptor mechanisms on lysosomes for kinesins include the scaffolds JIP3 and JIP4.
“Alternative adaptor mechanisms on lysosomes for kinesins have been described, among the scaffolds c-Jun NH2-terminal kinase (JNK)-interacting protein 3 (JIP3) and JIP4 (Vilela et al., 2026;Watt et al., 2015).”
From TMEM55B promotes anterograde transport and distal axonal distribution of LAMP1-positive organelles (2026) · cites this paper as Watt et al., 2015
The Discussion (page not available) shows that the scaffold JIP3 activates kinesin-1 motility through interactions with its light and heavy chains. Our copy does not establish this mechanism on lysosomes or describe JIP4 as a kinesin adaptor; lysosomes appear in the title of a cited work in the References, not in this paper’s reported findings. (LLM, conf=0.87)
Experimental — accuracy not yet measuredJIP3 can induce kinesin activity in vitro.
“Accordingly, JIP3 (a paralog of JIP4) can induce kinesin activity in vitro (Vilela et al., 2026;Watt et al., 2015), and JIP3/4 can also activate dynein (Cason and Holzbaur, 2023).”
From TMEM55B promotes anterograde transport and distal axonal distribution of LAMP1-positive organelles (2026) · cites this paper as Watt et al., 2015
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Citations
Cites
Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012
Self-citationInteraction of a mitogen-activated protein kinase signaling module with the neuronal protein JIP3
Kelkar, N., Gupta, S., Dickens, M., & Davis, R. J. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.3.1030-1043.2000 · Cited by 281 · cited 1×
“Deletion of the KHC Binding Domain in JIP3 Has a Dominant Negative Effect—Because JIP3 can homo-oligomerize (5, 60) we next determined whether JIP3 lacking the KHC binding domain had dominant negative effects on axon morphology in a WT background.”
BackgroundKinesin Light Chains Are Essential for Axonal Transport in Drosophila
Gindhart, J. G., Desai, C. J., Beushausen, S., Zinn, K., & Goldstein, L. S. B. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.2.443 · Cited by 179
Presenilin controls kinesin-1 and dynein function during APP-vesicle transport in vivo
Gunawardena, S., Yang, G., & Goldstein, L. S. B. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt237 · Cited by 66
Light chains of sea urchin kinesin identified by immunoadsorption
Johnson, C. S., Buster, D., & Scholey, J. M. (1990) · Cell Motility · doi:10.1002/cm.970160307 · Cited by 37
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Cited by
Sorted by citations
TMEM55B promotes anterograde transport and distal axonal distribution of LAMP1-positive organelles
Rudnik, S., Li, C. H., Gottschling, D.-C., Veh, A., Barbosa, D. J., Richter, J., Stroobants, S., Schuster, B., Beck, I. M., Sedlack, R., et al. (2026) · doi:10.64898/2026.10.27.762112
Metadata
- Authors
- Watt, D., Dixit, R., & Cavalli, V.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2015-06
- Volume
- 290
- Issue
- 25
- Pages
- 15512-15525
- ISSN
- 0021-9258
- Cited by
- 46
- References
- 5
- Language
- en
- Licence
- Funders
- National Institutes of Health (R01 NS082446)
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