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Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >
Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1.
| Title: | Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1. |
| Authors: | Chiba, Kyoko Browse this author | | Chien, Ko-Yi Browse this author | | Sobu, Yuriko Browse this author | | Hata, Saori Browse this author →KAKEN DB | | Kato, Shun Browse this author | | Nakaya, Tadashi Browse this author →KAKEN DB | | Okada, Yasushi Browse this author | | Nairn, Angus C Browse this author | | Kinjo, Masataka Browse this author | | Taru, Hidenori Browse this author →KAKEN DB | | Wang, Rong Browse this author | | Suzuki, Toshiharu Browse this author →KAKEN DB |
| Issue Date: | 15-Dec-2017 |
| Journal Title: | Molecular biology of the cell |
| Volume: | 28 |
| Issue: | 26 |
| Start Page: | 3857 |
| End Page: | 3869 |
| Publisher DOI: | 10.1091/mbc.E17-05-0303 |
| PMID: | 29093025 |
| Abstract: | In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously, we showed that EFV requires conventional interaction between the JIP1b C-terminal region and the kinesin light chain 1 (KLC1) tetratricopeptide repeat, whereas EHF requires a novel interaction between the central region of JIP1b and the coiled-coil domain of KLC1. We found that phosphorylatable Thr466 of KLC1 regulates the conventional interaction with JIP1b. Substitution of Glu for Thr466 abolished this interaction and EFV, but did not impair the novel interaction responsible for EHF. Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 binding to kinesin-1 decreased, suggesting that APP transport is impaired by aging. We conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP by kinesin-1 by modulating its interaction with JIP1b. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/68319 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 鈴木 利治
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