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Physicochemical Properties of α-Taxilin as a Putative Tethering Factor
https://dmu.repo.nii.ac.jp/records/5256
https://dmu.repo.nii.ac.jp/records/5256d8ee8a96-d01e-453e-8ce0-56cc90d21760
| 名前 / ファイル | ライセンス | アクション |
|---|---|---|
DKMJ-1-3-Higashi-Fulltext (546.1 kB)
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| Item type | 学術雑誌論文 / Journal Article(1) | |||||||||
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| タイトル | ||||||||||
| タイトル | Physicochemical Properties of α-Taxilin as a Putative Tethering Factor | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| キーワード | ||||||||||
| 主題Scheme | Other | |||||||||
| 主題 | α-taxilin | |||||||||
| キーワード | ||||||||||
| 主題Scheme | Other | |||||||||
| 主題 | intracellular vesicle traffic | |||||||||
| キーワード | ||||||||||
| 主題Scheme | Other | |||||||||
| 主題 | SNARE | |||||||||
| キーワード | ||||||||||
| 主題Scheme | Other | |||||||||
| 主題 | syntaxin | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||||||
| 資源タイプ | journal article | |||||||||
| 著者 |
Higashi, Satoru
× Higashi, Satoru
× Shirataki, Hiromichi
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| 著者所属 | ||||||||||
| Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University, Tochigi, Japan | ||||||||||
| 著者所属 | ||||||||||
| Department of Molecular and Cell Biology, Graduate School of Medicine, Dokkyo Medical University, Tochigi, Japan | ||||||||||
| 書誌情報 |
Dokkyo Medical Journal 巻 1, 号 3, p. 167-175, 発行日 2022-09 |
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| 抄録 | ||||||||||
| 内容記述タイプ | Abstract | |||||||||
| 内容記述 | α-Taxilin is a member of the taxilin family, a binding partner of the syntaxin family involved in intracellular vesicle traffic. The taxilin family members share a long coiled-coil structure, which is homologous to that of Uso1, a yeast homologue of p115. It has been revealed that a parallel homodimerization of p115, an elongated polypeptide, is required for tethering of the transport vesicles to the acceptor membrane. In this study we examined whether α-taxilin has similar biochemical properties to p115. Gel filtration and sedimentation analyses suggest that α-taxilin is an elongated polypeptide containing a long coiled-coil structure. A pull-down assay revealed that His6-α-taxilin binds to GST-α-taxilin, and not to GST in dose-dependent and saturable manners. α-Taxilin formed a parallel homodimer through at least two independent regions. Together, α-taxilin may be involved in tethering of the transport vesicles to the acceptor membranes in a similar way to p115. | |||||||||
| 記事種別 | ||||||||||
| Original | ||||||||||
| 出版者 | ||||||||||
| 出版者 | Dokkyo Medical Society | |||||||||
| ISSN | ||||||||||
| 収録物識別子タイプ | ISSN | |||||||||
| 収録物識別子 | 2436-522X | |||||||||
| DOI | ||||||||||
| 識別子タイプ | DOI | |||||||||
| 関連識別子 | 10.51040/dkmj.2022-002 | |||||||||
