| http://purl.uniprot.org/citations/27813252 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27813252 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27813252 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.13949"xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.org/dc/terms/identifier | "doi:10.1111/febs.13949"xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Maki M."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Maki M."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Shibata H."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Shibata H."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Takahara T."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Takahara T."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Kuwata K."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Kuwata K."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Kanadome T."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/author | "Kanadome T."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/date | "2017"xsd:gYear |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/name | "FEBS J."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/pages | "56-76"xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/pages | "56-76"xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/title | "The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/title | "The calcium-binding protein ALG-2 promotes endoplasmic reticulum exit site localization and polymerization of Trk-fused gene (TFG) protein."xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/volume | "284"xsd:string |
| http://purl.uniprot.org/citations/27813252 | http://purl.uniprot.org/core/volume | "284"xsd:string |