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Sunday Driver links axonal transport to damage signaling.

Cavalli V, Kujala P, Klumperman J, Goldstein LS - J. Cell Biol. (2005)

Bottom Line: We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex.Finally, we found that injury induces an enhanced interaction between syd and dynactin.Thus, a mobile axonal JNK-syd complex may generate a transport-dependent axonal damage surveillance system.

View Article: PubMed Central - PubMed

Affiliation: Department of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093, USA.

ABSTRACT
Neurons transmit long-range biochemical signals between cell bodies and distant axonal sites or termini. To test the hypothesis that signaling molecules are hitchhikers on axonal vesicles, we focused on the c-Jun NH2-terminal kinase (JNK) scaffolding protein Sunday Driver (syd), which has been proposed to link the molecular motor protein kinesin-1 to axonal vesicles. We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex. Nerve injury induces local activation of JNK, primarily within axons, and activated JNK and syd are then transported primarily retrogradely. In axons, syd and activated JNK colocalize with p150Glued, a subunit of the dynactin complex, and with dynein. Finally, we found that injury induces an enhanced interaction between syd and dynactin. Thus, a mobile axonal JNK-syd complex may generate a transport-dependent axonal damage surveillance system.

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P-JNK colocalizes with dynactin, dynein, and syd in axons distal to a ligation. (A–C) Deconvoluted images of single axons, stained with SMI31 and the indicated antibodies, distal to the ligation site. Arrowheads show colocalized puncta. Bars, 2 μm.
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fig7: P-JNK colocalizes with dynactin, dynein, and syd in axons distal to a ligation. (A–C) Deconvoluted images of single axons, stained with SMI31 and the indicated antibodies, distal to the ligation site. Arrowheads show colocalized puncta. Bars, 2 μm.

Mentions: Because syd interacts with the dynactin complex and colocalizes in axons with p150Glued and DHC (Fig. 4), this interaction could mediate axonal retrograde transport. To further support the suggestion that P-JNK retrograde transport after injury depends on syd and the dynactin–dynein motor complex, we examined the localization of P-JNK in axons distal to a ligation site. We observed that P-JNK colocalized with both p150Glued and DHC (Fig. 7, A and B). Consistent with what we observed for syd, the extent of colocalization is higher with p150Glued than with DHC. P-JNK and syd were also found to colocalize on the same puncta (Fig. 7 C). Similar results were found when the portion proximal to the ligation site was analyzed (unpublished data).


Sunday Driver links axonal transport to damage signaling.

Cavalli V, Kujala P, Klumperman J, Goldstein LS - J. Cell Biol. (2005)

P-JNK colocalizes with dynactin, dynein, and syd in axons distal to a ligation. (A–C) Deconvoluted images of single axons, stained with SMI31 and the indicated antibodies, distal to the ligation site. Arrowheads show colocalized puncta. Bars, 2 μm.
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Related In: Results  -  Collection

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getmorefigures.php?uid=PMC2171809&req=5

fig7: P-JNK colocalizes with dynactin, dynein, and syd in axons distal to a ligation. (A–C) Deconvoluted images of single axons, stained with SMI31 and the indicated antibodies, distal to the ligation site. Arrowheads show colocalized puncta. Bars, 2 μm.
Mentions: Because syd interacts with the dynactin complex and colocalizes in axons with p150Glued and DHC (Fig. 4), this interaction could mediate axonal retrograde transport. To further support the suggestion that P-JNK retrograde transport after injury depends on syd and the dynactin–dynein motor complex, we examined the localization of P-JNK in axons distal to a ligation site. We observed that P-JNK colocalized with both p150Glued and DHC (Fig. 7, A and B). Consistent with what we observed for syd, the extent of colocalization is higher with p150Glued than with DHC. P-JNK and syd were also found to colocalize on the same puncta (Fig. 7 C). Similar results were found when the portion proximal to the ligation site was analyzed (unpublished data).

Bottom Line: We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex.Finally, we found that injury induces an enhanced interaction between syd and dynactin.Thus, a mobile axonal JNK-syd complex may generate a transport-dependent axonal damage surveillance system.

View Article: PubMed Central - PubMed

Affiliation: Department of Cellular and Molecular Medicine, Howard Hughes Medical Institute, University of California, San Diego, La Jolla, CA 92093, USA.

ABSTRACT
Neurons transmit long-range biochemical signals between cell bodies and distant axonal sites or termini. To test the hypothesis that signaling molecules are hitchhikers on axonal vesicles, we focused on the c-Jun NH2-terminal kinase (JNK) scaffolding protein Sunday Driver (syd), which has been proposed to link the molecular motor protein kinesin-1 to axonal vesicles. We found that syd and JNK3 are present on vesicular structures in axons, are transported in both the anterograde and retrograde axonal transport pathways, and interact with kinesin-I and the dynactin complex. Nerve injury induces local activation of JNK, primarily within axons, and activated JNK and syd are then transported primarily retrogradely. In axons, syd and activated JNK colocalize with p150Glued, a subunit of the dynactin complex, and with dynein. Finally, we found that injury induces an enhanced interaction between syd and dynactin. Thus, a mobile axonal JNK-syd complex may generate a transport-dependent axonal damage surveillance system.

Show MeSH
Related in: MedlinePlus