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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Maeda, Yusuke Yamaguchi, Yoshiki Kinoshita, Taroh Theiler, Romina Nagae, Masamichi Fujita, Morihisa |
| Description | Author Affiliation: Theiler R ( From the World Premier International (WPI) Immunology Frontier Research Center and Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan and.); Fujita M ( From the World Premier International (WPI) Immunology Frontier Research Center and Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan and.); Nagae M ( the Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.); Yamaguchi Y ( the Structural Glycobiology Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center, RIKEN Global Research Cluster, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.); Maeda Y ( From the World Premier International (WPI) Immunology Frontier Research Center and Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan and.); Kinoshita T ( From the World Premier International (WPI) Immunology Frontier Research Center and Research Institute for Microbial Diseases, Osaka University, Suita, Osaka 565-0871, Japan and tkinoshi@biken.osaka-u.ac.jp.) |
| Abstract | Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are group of proteins that depend on p24 cargo receptors for their transport from the endoplasmic reticulum to the Golgi apparatus. The GPI anchor is expected to act as a sorting and transport signal, but so far little is known about the recognition mechanism. In the present study we investigate the GPI-AP transport in cell knockdown of p24γ, the most diverse p24 subfamily. Knockdown of p24γ2 but not of other p24γ family members impaired the transport of a reporter GPI-AP. Restoration of the knockdown-induced phenotype using chimeric constructs between p24γ2 and the related p24γ1 further implied a role of the -helical region of p24γ2 but not its GOLD domain in the specific binding of GPI-APs. We conclude that motifs in the membrane-adjacent -helical region of p24γ2 are involved in recognition of GPI-APs and are consequently responsible for the incorporation of these proteins into coat protein complex II-coated transport vesicles. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 24 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-06-13 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | GPI-Linked Proteins Metabolism Vesicular Transport Proteins Amino Acid Motifs Amino Acid Sequence Animals Binding Sites CHO Cells Calcium Channels Cricetinae Cricetulus Mice Molecular Sequence Data Protein Binding Protein Subunits Chemistry Genetics Protein Transport TRPV Cation Channels Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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