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Hokkaido University Collection of Scholarly and Academic Papers >
Faculty of Pharmaceutical Sciences >
Peer-reviewed Journal Articles, etc >
Phosphorylation of multiple sites within an acidic region of Alcadein α is required for kinesin-1 association and Golgi exit of Alcadein α cargo.
| Title: | Phosphorylation of multiple sites within an acidic region of Alcadein α is required for kinesin-1 association and Golgi exit of Alcadein α cargo. |
| Authors: | Sobu, Yuriko Browse this author | | Furukori, Keiko Browse this author | | Chiba, Kyoko Browse this author | | Nairn, Angus C Browse this author | | Kinjo, Masataka Browse this author | | Hata, Saori Browse this author →KAKEN DB | | Suzuki, Toshiharu Browse this author →KAKEN DB |
| Keywords: | Alcadein | | Golgi | | Kinesin | | Protein phosphorylation | | Axonal transport |
| Issue Date: | 15-Dec-2017 |
| Journal Title: | Molecular biology of the cell |
| Volume: | 28 |
| Issue: | 26 |
| Start Page: | 3844 |
| End Page: | 3856 |
| Publisher DOI: | 10.1091/mbc.E17-05-0301 |
| PMID: | 29093024 |
| Abstract: | Alcadein α (Alcα) is a major cargo of kinesin-1 that is subjected to anterograde transport in neuronal axons. Two tryptophan- and aspartic acid-containing (WD) motifs located in its cytoplasmic domain directly bind the tetratricopeptide repeat (TPR) motifs of the kinesin light chain (KLC), which activate kinesin-1 and recruit kinesin-1 to Alcα cargo. We found that phosphorylation of three serine residues in the acidic region located between the two WD motifs is required for interaction with KLC. Phosphorylation of these serine residues may alter the disordered structure of the acidic region to induce direct association with KLC. Replacement of these serines with Ala results in a mutant that is unable to bind kinesin-1, which impairs exit of Alcα cargo from the Golgi. Despite this deficiency, the compromised Alcα mutant was still transported, albeit improperly by vesicles following missorting of the Alcα mutant with amyloid β-protein precursor (APP) cargo. This suggests that APP partially compensates for defective Alcα in anterograde transport by providing an alternative cargo receptor for kinesin-1. |
| Type: | article |
| URI: | http://hdl.handle.net/2115/68318 |
| 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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