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Quantitative analysis of APP axonal transport in neurons: role of JIP1 in enhanced APP anterograde transport.

Chiba K, Araseki M, Nozawa K, Furukori K, Araki Y, Matsushima T, Nakaya T, Hata S, Saito Y, Uchida S, Okada Y, Nairn AC, Davis RJ, Yamamoto T, Kinjo M, Taru H, Suzuki T - Mol. Biol. Cell (2014)

Bottom Line: In JIP1-deficient neurons, we find that both the fast velocity (∼2.7 μm/s) and high frequency (66%) of anterograde transport of APP cargo are impaired to a reduced velocity (∼1.83 μm/s) and a lower frequency (45%).Furthermore, efficient APP axonal transport is not influenced by phosphorylation of APP at Thr-668, a site known to be phosphorylated by JNK.Our quantitative analysis indicates that enhanced fast-velocity and efficient high-frequency APP anterograde transport observed in neurons are mediated by novel roles of JIP1b.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

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JNK binding to JIP1b and APP phosphorylation do not participate in the regulation of efficient anterograde transport of APP cargo. APP-EGFP and the indicated JIP1b mutants were coexpressed in primary cultured neurons from JIP1-KO mice (A, B), and APP T668A-EGFP was expressed in primary cultured neurons from APP T668A-KI mice (C). Data are presented as in Figure 1. The transport of APP cargo is shown. Position of average velocity is indicated with arrows. See Supplemental Movie S2A for A, S2B for B, and S2C for C. Scale bar, 5 μm. The ratios of anterograde (A), retrograde (R), and stationary (S) vesicles are indicated in the insets at the right. Statistical analysis for direction of movement vesicles, except for C, is summarized in Table 1.
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Figure 2: JNK binding to JIP1b and APP phosphorylation do not participate in the regulation of efficient anterograde transport of APP cargo. APP-EGFP and the indicated JIP1b mutants were coexpressed in primary cultured neurons from JIP1-KO mice (A, B), and APP T668A-EGFP was expressed in primary cultured neurons from APP T668A-KI mice (C). Data are presented as in Figure 1. The transport of APP cargo is shown. Position of average velocity is indicated with arrows. See Supplemental Movie S2A for A, S2B for B, and S2C for C. Scale bar, 5 μm. The ratios of anterograde (A), retrograde (R), and stationary (S) vesicles are indicated in the insets at the right. Statistical analysis for direction of movement vesicles, except for C, is summarized in Table 1.

Mentions: Results of Figures 1, 2, A and B, and 5 are summarized, with statistical analysis for the ratio of movement directions. APP movement in JIP1−/− neurons is compared with that in JIP1+/+ neurons in the first row, and APP movement in JIP1−/− neurons expressing JIP1b proteins is compared with that in JIP1−/− neurons in subsequent rows.


Quantitative analysis of APP axonal transport in neurons: role of JIP1 in enhanced APP anterograde transport.

Chiba K, Araseki M, Nozawa K, Furukori K, Araki Y, Matsushima T, Nakaya T, Hata S, Saito Y, Uchida S, Okada Y, Nairn AC, Davis RJ, Yamamoto T, Kinjo M, Taru H, Suzuki T - Mol. Biol. Cell (2014)

JNK binding to JIP1b and APP phosphorylation do not participate in the regulation of efficient anterograde transport of APP cargo. APP-EGFP and the indicated JIP1b mutants were coexpressed in primary cultured neurons from JIP1-KO mice (A, B), and APP T668A-EGFP was expressed in primary cultured neurons from APP T668A-KI mice (C). Data are presented as in Figure 1. The transport of APP cargo is shown. Position of average velocity is indicated with arrows. See Supplemental Movie S2A for A, S2B for B, and S2C for C. Scale bar, 5 μm. The ratios of anterograde (A), retrograde (R), and stationary (S) vesicles are indicated in the insets at the right. Statistical analysis for direction of movement vesicles, except for C, is summarized in Table 1.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4230617&req=5

Figure 2: JNK binding to JIP1b and APP phosphorylation do not participate in the regulation of efficient anterograde transport of APP cargo. APP-EGFP and the indicated JIP1b mutants were coexpressed in primary cultured neurons from JIP1-KO mice (A, B), and APP T668A-EGFP was expressed in primary cultured neurons from APP T668A-KI mice (C). Data are presented as in Figure 1. The transport of APP cargo is shown. Position of average velocity is indicated with arrows. See Supplemental Movie S2A for A, S2B for B, and S2C for C. Scale bar, 5 μm. The ratios of anterograde (A), retrograde (R), and stationary (S) vesicles are indicated in the insets at the right. Statistical analysis for direction of movement vesicles, except for C, is summarized in Table 1.
Mentions: Results of Figures 1, 2, A and B, and 5 are summarized, with statistical analysis for the ratio of movement directions. APP movement in JIP1−/− neurons is compared with that in JIP1+/+ neurons in the first row, and APP movement in JIP1−/− neurons expressing JIP1b proteins is compared with that in JIP1−/− neurons in subsequent rows.

Bottom Line: In JIP1-deficient neurons, we find that both the fast velocity (∼2.7 μm/s) and high frequency (66%) of anterograde transport of APP cargo are impaired to a reduced velocity (∼1.83 μm/s) and a lower frequency (45%).Furthermore, efficient APP axonal transport is not influenced by phosphorylation of APP at Thr-668, a site known to be phosphorylated by JNK.Our quantitative analysis indicates that enhanced fast-velocity and efficient high-frequency APP anterograde transport observed in neurons are mediated by novel roles of JIP1b.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Neuroscience, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

Show MeSH
Related in: MedlinePlus