|
Hokkaido University Collection of Scholarly and Academic Papers >
Institute for Genetic Medicine >
Peer-reviewed Journal Articles, etc >
Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase
| Title: | Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase |
| Authors: | Takahashi, Yasuhiro Browse this author | | Fujimura-Kamada, Konomi Browse this author →KAKEN DB | | Kondo, Satoshi Browse this author | | Tanaka, Kazuma Browse this author |
| Keywords: | flippase | | phospholipid asymmetry | | type 4 P-type ATPase | | yeast |
| Issue Date: | Apr-2011 |
| Publisher: | Oxford University Press |
| Journal Title: | The Journal of Biochemistry |
| Volume: | 149 |
| Issue: | 4 |
| Start Page: | 423 |
| End Page: | 432 |
| Publisher DOI: | 10.1093/jb/mvq155 |
| PMID: | 21212072 |
| Abstract: | Flippases (type 4 P-type ATPases) are believed to translocate phospholipids from the exoplasmic to the cytoplasmic leaflet in bilayer membranes. Since flippases are structurally similar to ion-transporting P-type ATPases such as the Ca2+ ATPase, one important question is how flippases have evolved to transport phospholipids instead of ions. We previously showed that a conserved membrane protein, Cdc50p, is required for the ER exit of the Drs2p flippase in yeast. However, Cdc50p is still associated with Drs2p after its transport to the endosomal/TGN membranes, and its function in the complex with Drs2p is unknown. In this study, we isolated novel temperature-sensitive (ts) cdc50 mutants whose products were still localized to endosomal/TGN compartments at the non-permissive temperature. Mutant Cdc50 proteins colocalized with Drs2p in endosomal/TGN compartments, and they co-immunoprecipitated with Drs2p. These cdc50-ts mutants exhibited defects in vesicle transport from early endosomes to the TGN as the cdc50 deletion mutant did. These results suggest that mutant Cdc50 proteins could be complexed with Drs2p, but the resulting Cdc50p-Drs2p complex is functionally defective at the non-permissive temperature. Cdc50p may play an important role for phospholipid translocation by Drs2p. |
| Rights: | This is a pre-copy-editing, author-produced PDF of an article accepted for publication in The Journal of Biochemistry following peer review. The definitive publisher-authenticated version J Biochem (2011) 149 (4): 423-432 is available online at: http://jb.oxfordjournals.org/content/149/4/423 |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/47953 |
| Appears in Collections: | 遺伝子病制御研究所 (Institute for Genetic Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 鎌田 このみ
|
