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

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Title: Quantitative analysis of APP axonal transport in neurons: role of JIP1 in enhanced APP anterograde transport
Authors: Chiba, Kyoko Browse this author
Araseki, Masahiko Browse this author
Nozawa, Keisuke Browse this author
Furukori, Keiko Browse this author
Araki, Yoichi Browse this author
Matsushima, Takahide Browse this author
Nakaya, Tadashi Browse this author →KAKEN DB
Hata, Saori Browse this author →KAKEN DB
Saito, Yuhki Browse this author →KAKEN DB
Uchida, Seiichi Browse this author →KAKEN DB
Okada, Yasushi Browse this author →KAKEN DB
Nairn, Angus C. Browse this author
Davis, Roger J. Browse this author
Yamamoto, Tohru Browse this author →KAKEN DB
Kinjo, Masataka Browse this author →KAKEN DB
Taru, Hidenori Browse this author →KAKEN DB
Suzuki, Toshiharu Browse this author →KAKEN DB
Issue Date: 5-Nov-2014
Publisher: American Society for Cell Biology
Journal Title: Molecular biology of the cell
Volume: 25
Issue: 22
Start Page: 3569
End Page: 3580
Publisher DOI: 10.1091/mbc.E14-06-1111
PMID: 25165140
Abstract: Alzheimer's beta-amyloid precursor protein (APP) associates with kinesin-1 via JNK-interacting protein 1 (JIP1); however, the role of JIP1 in APP transport by kinesin-1 in neurons remains unclear. We performed a quantitative analysis to understand the role of JIP1 in APP axonal transport. In JIP1-deficient neurons, we find that both the fast velocity (similar to 2.7 mu m/s) and high frequency (66%) of anterograde transport of APP cargo are impaired to a reduced velocity (similar to 1.83 mu m/s) and a lower frequency (45%). We identified two novel elements linked to JIP1 function, located in the central region of JIP1b, that interact with the coiled-coil domain of kinesin light chain 1 (KLC1), in addition to the conventional interaction of the JIP1b 11-amino acid C-terminal (C11) region with the tetratricopeptide repeat of KLC1. High frequency of APP anterograde transport is dependent on one of the novel elements in JIP1b. Fast velocity of APP cargo transport requires the C11 domain, which is regulated by the second novel region of JIP1b. 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.
Type: article
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 鈴木 利治

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