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The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein
http://hdl.handle.net/2237/26285
http://hdl.handle.net/2237/26285779003a4-cf5e-46cd-acb9-5e9b6c36a61a
| 名前 / ファイル | ライセンス | アクション |
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FJ_KanadomeT_ShibataH_170510.pdf ファイル公開：2018/01/01 (7.5 MB)
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| アイテムタイプ | 学術雑誌論文 / Journal Article(1) | |||||
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| 公開日 | 2017-05-11 | |||||
| タイトル | ||||||
| タイトル | The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein | |||||
| 言語 | en | |||||
| 著者 |
Kanadome, Takashi
× Kanadome, Takashi× Shibata, Hideki× Kuwata, Keiko× Takahara, Terunao× Maki, Masatoshi |
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| アクセス権 | ||||||
| アクセス権 | open access | |||||
| アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
| 権利 | ||||||
| 権利情報 | This is the peer reviewed version of the following article: [Kanadome, T., Shibata, H., Kuwata, K., Takahara, T. and Maki, M. (2017), The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein. FEBS J, 284: 56–76. doi:10.1111/febs.13949], which has been published in final form at [http://doi.org/10.1111/febs.13949]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving. | |||||
| 言語 | en | |||||
| 抄録 | ||||||
| 内容記述タイプ | Abstract | |||||
| 内容記述 | Apoptosis-linked gene 2 (ALG-2), which is a gene product of PDCD6, is a 22-kDa Ca2+-binding protein. Accumulating evidence points to a role for ALG-2 as a Ca2+-responsive adaptor protein. On binding to Ca2+, ALG-2 undergoes a conformational change that facilitates its interaction with various proteins. It also forms a homodimer and heterodimer with peflin, a paralog of ALG-2. However, the differences in cellular roles for the ALG-2 homodimer and ALG-2/peflin heterodimer are unclear. In the present study, we found that Trk-fused gene (TFG) protein interacted with the ALG-2 homodimer. Immunostaining analysis revealed that TFG and ALG-2 partially overlapped at endoplasmic reticulum exit sites (ERES), a platform for COPII-mediated protein transport from the endoplasmic reticulum. Time-lapse live-cell imaging demonstrated that both green fluorescent protein-fused TFG and mCherry-fused ALG-2 are recruited to ERES after thapsigargin treatment, which raises intracellular Ca2+ levels. Furthermore, overexpression of ALG-2 induced the accumulation of TFG at ERES. TFG has an ALG-2-binding motif and deletion of the motif decreased TFG binding to ALG-2 and shortened its half-life at ERES, suggesting a critical role for ALG-2 in retaining TFG at ERES. We also demonstrated, by in vitro cross-linking assays, that ALG-2 promoted the polymerization of TFG in a Ca2+-dependent manner. Collectively, the results suggest that ALG-2 acts as a Ca2+-sensitive adaptor to concentrate and polymerize TFG at ERES, supporting a potential role for ALG-2 in COPII-dependent trafficking from the endoplasmic reticulum. | |||||
| 言語 | en | |||||
| 出版者 | ||||||
| 出版者 | Wiley | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプresource | http://purl.org/coar/resource_type/c_6501 | |||||
| タイプ | journal article | |||||
| 出版タイプ | ||||||
| 出版タイプ | AM | |||||
| 出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
| DOI | ||||||
| 関連タイプ | isVersionOf | |||||
| 識別子タイプ | DOI | |||||
| 関連識別子 | https://doi.org/10.1111/febs.13949 | |||||
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| 収録物識別子タイプ | PISSN | |||||
| 収録物識別子 | 1742-464X | |||||
| 書誌情報 |
en : FEBS Journal 巻 284, 号 1, p. 56-76, 発行日 2017-01 |
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| 著者版フラグ | ||||||
| 値 | author | |||||
| URI | ||||||
| 識別子 | http://doi.org/10.1111/febs.13949 | |||||
| 識別子タイプ | DOI | |||||
| URI | ||||||
| 識別子 | http://hdl.handle.net/2237/26285 | |||||
| 識別子タイプ | HDL | |||||
