Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1.

Chiba, Kyoko; Chien, Ko-Yi; Sobu, Yuriko; Hata, Saori; Kato, Shun; Nakaya, Tadashi; Okada, Yasushi; Nairn, Angus C; Kinjo, Masataka; Taru, Hidenori; Wang, Rong; Suzuki, Toshiharu

Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1.

Chiba, Kyoko; Chien, Ko-Yi; Sobu, Yuriko et al.

Molecular biology of the cell, 2017, 28(26), 3857-3869

Permalink : https://hdl.handle.net/2115/68319

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アクセス権	open access
URI	https://hdl.handle.net/2115/68319
タイトル	Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1.
著者	Chiba, Kyoko ; Chien, Ko-Yi ; Sobu, Yuriko ; Hata, Saori ; Kato, Shun ; Nakaya, Tadashi ; Okada, Yasushi ; Nairn, Angus C ; Kinjo, Masataka ; Taru, Hidenori ; Wang, Rong ; Suzuki, Toshiharu
著者名 Chiba, Kyoko
著者名 Chien, Ko-Yi
著者名 Sobu, Yuriko
e-Rad_Researcher 40581012 著者名 Hata, Saori
著者名 Kato, Shun
e-Rad_Researcher 50374559 著者名 Nakaya, Tadashi
著者名 Okada, Yasushi
著者名 Nairn, Angus C
著者名 Kinjo, Masataka
e-Rad_Researcher 30533731 著者名 Taru, Hidenori
著者名 Wang, Rong
e-Rad_Researcher 80179233 著者名 Suzuki, Toshiharu
言語	英語
発行日	2017-12-15
収録物名	Molecular biology of the cell
巻(号)	28(26)
ページ	3857-3869
抄録	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.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
PISSN	1939-4586
関連情報	PMID 29093025
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1091/mbc.E17-05-0303