2013 Fiscal Year Final Research Report
A novel role of CLPTM1 in the ER-associated degradation of membrane proteins
| Project/Area Number |
24658262
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Clinical veterinary science
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| Research Institution | Hokkaido University |
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Principal Investigator |
INABA MUTSUMI 北海道大学, (連合)獣医学研究科, 教授 (00183179)
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| Co-Investigator(Kenkyū-buntansha) |
SATO Kota 北海道大学, 大学院獣医学研究科, 准教授 (50283974)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 小胞体関連分解 / プロテアソーム系 / 膜蛋白質 / 小胞体品質管理 / シャペロン |
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| Research Abstract |
The ER-associated degradation (ERAD) of various polytopic membrane proteins involves recognition of the polypeptide in the ER and its retrotranslocation into the cytosol, leading to its degradation by the proteasome system. The purpose of the present study was to unravel the role of CLPTM1 in the ERAD of an AE1 anion exchanger mutant, R664X AE1, with characteristic features of ubiquitin- and glycosylation-independence. In HEK293 cells expressing the AE1 mutant, CLPTM1 was localized in the ER and associated with several ER chaperone proteins including KIAA0090, p97/VCP, Derlins, and calnexin. However, overexpression or suppression of CLPTM1 had no apparent effect on proteasomal degradation of R664X AE1. In contrast, overexpression of KIAA0090 and/or p97/VCP accelerated the proteasomal degradation of the mutant.
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Research Products
(7 results)
