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Loop 5 region is important for the activity of the long-chain base transporter Rsb1
| Title: | Loop 5 region is important for the activity of the long-chain base transporter Rsb1 |
| Authors: | Makuta, Hiroshi Browse this author | | Obara, Keisuke Browse this author →KAKEN DB | | Kihara, Akio Browse this author →KAKEN DB |
| Keywords: | lipid | | long-chain base | | plasma membrane | | sphingolipid | | transporter |
| Issue Date: | Feb-2017 |
| Publisher: | Oxford University Press |
| Journal Title: | Journal of biochemistry |
| Volume: | 161 |
| Issue: | 2 |
| Start Page: | 207 |
| End Page: | 213 |
| Publisher DOI: | 10.1093/jb/mvw059 |
| PMID: | 28175317 |
| Abstract: | Intracellular lipid amounts are regulated not only by metabolism but also by efflux. Yeast Rsb1 is the only known transporter/floppase of the sphingolipid components long-chain bases (LCBs). However, even fundamental knowledge about Rsb1, such as important amino acid residues for activity and substrate recognition, still remains unclear. Rsb1 belongs to the Rtal-like family. To date, it has not been determined whether all family members share a common ability to export LCBs. Here, we revealed that within the Rtal-like family, only Rsb1 suppressed the hypersensitivity of the mutant cells lacking LCB 1-phoshate-degrading enzymes, suggesting that LCB-exporting activity is specific to Rsb1. Rsb1 contains a characteristic region (loop 5), which does not exist in other proteins of the Rtal-like family. We found that deletion of this region caused loss of Rsb1 function. Further mutational analysis of loop 5 revealed that the charged amino acid residues E223, D225 and R236 were important for Rsb1 activity. In addition to LCBs, Rsb1 facilitated the export of 1-hexadecanol, but not pahnitic acid, which suggests that Rsb1 recognizes the C1 hydroxyl group. Thus, our findings provide an important clue for understanding the molecular mechanism of LCB export. |
| Rights: | This is a pre-copyedited, author-produced version of an article accepted for publication in Journal of Biochemistry following peer review. The version of record 161(2), 207-213, 2017 is available online at: DOI:10.1093/jb/mvw059. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/68388 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 木原 章雄
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