{"created":"2021-03-01T06:31:58.962586+00:00","id":24073,"links":{},"metadata":{"_buckets":{"deposit":"1f2a468f-3fd5-401c-aac4-a145c8f65e16"},"_deposit":{"id":"24073","owners":[],"pid":{"revision_id":0,"type":"depid","value":"24073"},"status":"published"},"_oai":{"id":"oai:nagoya.repo.nii.ac.jp:00024073","sets":["643:666:667"]},"author_link":["71456","71457","71458","71459","71460"],"item_10_biblio_info_6":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2017-01","bibliographicIssueDateType":"Issued"},"bibliographicIssueNumber":"1","bibliographicPageEnd":"76","bibliographicPageStart":"56","bibliographicVolumeNumber":"284","bibliographic_titles":[{"bibliographic_title":"FEBS Journal","bibliographic_titleLang":"en"}]}]},"item_10_description_4":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"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.","subitem_description_language":"en","subitem_description_type":"Abstract"}]},"item_10_identifier_60":{"attribute_name":"URI","attribute_value_mlt":[{"subitem_identifier_type":"DOI","subitem_identifier_uri":"http://doi.org/10.1111/febs.13949"},{"subitem_identifier_type":"HDL","subitem_identifier_uri":"http://hdl.handle.net/2237/26285"}]},"item_10_publisher_32":{"attribute_name":"出版者","attribute_value_mlt":[{"subitem_publisher":"Wiley","subitem_publisher_language":"en"}]},"item_10_relation_11":{"attribute_name":"DOI","attribute_value_mlt":[{"subitem_relation_type":"isVersionOf","subitem_relation_type_id":{"subitem_relation_type_id_text":"https://doi.org/10.1111/febs.13949","subitem_relation_type_select":"DOI"}}]},"item_10_rights_12":{"attribute_name":"権利","attribute_value_mlt":[{"subitem_rights":"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.","subitem_rights_language":"en"}]},"item_10_select_15":{"attribute_name":"著者版フラグ","attribute_value_mlt":[{"subitem_select_item":"author"}]},"item_10_source_id_7":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"1742-464X","subitem_source_identifier_type":"PISSN"}]},"item_1615787544753":{"attribute_name":"出版タイプ","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_ab4af688f83e57aa","subitem_version_type":"AM"}]},"item_access_right":{"attribute_name":"アクセス権","attribute_value_mlt":[{"subitem_access_right":"open access","subitem_access_right_uri":"http://purl.org/coar/access_right/c_abf2"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Kanadome, Takashi","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"71456","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Shibata, Hideki","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"71457","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Kuwata, Keiko","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"71458","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Takahara, Terunao","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"71459","nameIdentifierScheme":"WEKO"}]},{"creatorNames":[{"creatorName":"Maki, Masatoshi","creatorNameLang":"en"}],"nameIdentifiers":[{"nameIdentifier":"71460","nameIdentifierScheme":"WEKO"}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2018-01-01"}],"displaytype":"detail","filename":"FJ_KanadomeT_ShibataH_170510.pdf","filesize":[{"value":"7.5 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"FJ_KanadomeT_ShibataH_170510.pdf ファイル公開：2018/01/01","objectType":"fulltext","url":"https://nagoya.repo.nii.ac.jp/record/24073/files/FJ_KanadomeT_ShibataH_170510.pdf"},"version_id":"c9e86cc8-c81f-46d2-9152-96e7fbb6ed9f"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"journal article","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein","subitem_title_language":"en"}]},"item_type_id":"10","owner":"1","path":["667"],"pubdate":{"attribute_name":"PubDate","attribute_value":"2017-05-11"},"publish_date":"2017-05-11","publish_status":"0","recid":"24073","relation_version_is_last":true,"title":["The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein"],"weko_creator_id":"1","weko_shared_id":-1},"updated":"2023-01-16T04:54:37.997010+00:00"}