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OCTN2VT, a splice variant of OCTN2, does not transport carnitine because of the retention in the endoplasmic reticulum caused by insertion of 24 amino acids in the first extracellular loop of OCTN2
Title: | OCTN2VT, a splice variant of OCTN2, does not transport carnitine because of the retention in the endoplasmic reticulum caused by insertion of 24 amino acids in the first extracellular loop of OCTN2 |
Authors: | Maekawa, Satoshi Browse this author | Mori, Daisuke Browse this author | Nishiya, Tadashi Browse this author | Takikawa, Osamu Browse this author | Horinouchi, Takahiro Browse this author | Nishimoto, Arata Browse this author →KAKEN DB | Kajita, Emi Browse this author | Miwa, Soichi Browse this author →KAKEN DB |
Keywords: | OCTN2 | OCTN2VT | Splicing | Carnitine | N-glycosylation | Endoplasmic reticulum |
Issue Date: | Jun-2007 |
Publisher: | Elsevier B.V. |
Journal Title: | Biochimica et Biophysica Acta (BBA) : Molecular Cell Research |
Volume: | 1773 |
Issue: | 6 |
Start Page: | 1000 |
End Page: | 1006 |
Publisher DOI: | 10.1016/j.bbamcr.2007.04.005 |
PMID: | 17509700 |
Abstract: | A novel organic cation transporter OCTN2 is indispensable for carnitine transport across plasma membrane and subsequent fatty acid metabolism in the mitochondria. Here, we report a novel splice variant of OCTN2 (OCTN2VT), in which a 72-base-pair sequence located in the first intron of OCTN2 gene was spliced between exons 1 and 2 of OCTN2, causing the insertion of 24 amino acids in the first extracellular loop of OCTN2. Despite the similarity between OCTN2 and OCTN2VT regarding primary structure and tissue distribution, their biochemical characteristics were significantly different. OCTN2 was expressed on the plasma membrane with robust N-glycosylation, whereas OCTN2VT was retained in the endoplasmic reticulum (ER) with poor N-glycosylation. In addition, the retention in the ER caused no carnitine uptake into the cells. These results demonstrate that the biochemical and functional characteristics of OCTN2VT are distinct from OCTN2 due to the insertion of 24 amino acids in the first extracellular loop. |
Relation: | http://www.sciencedirect.com/science/journal/01674889 |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/28237 |
Appears in Collections: | 医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 三輪 聡一
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