Challenge to reveal the ER targeting suppressor
| Project/Area Number |
26650063
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Cell biology
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| Research Institution | University of Hyogo |
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Principal Investigator |
Sakaguchi Masao 兵庫県立大学, 生命理学研究科, 教授 (30205736)
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 小胞体 / 膜タンパク質 / ペルオキシソーム / シグナル配列 / 細胞オルガネラ / トランスロコン |
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| Outline of Final Research Achievements |
Many membrane proteins possessing hydrophobic transmembrane segments are cotranslationally integrated into the ER membrane. Various peroxisomal and mitochondrial membrane proteins escape the ER-targeting mechanism and are targeted to their destinations. Here we discovered a short segment in the 70-kDa peroxisomal membrane protein (PMP70) that suppresses ER targeting. The first transmembrane segment has an intrinsic signal function. The ER-targeting was suppressed by a short N-terminal sequence of 9 residues that is 80 residues upstream of the transmembrane segment. Among the 9 residues, Ser5 is indispensable. The short segment also suppressed the signal peptide function of an authentic secretory protein. The 50-kDa and 20-kDa proteins were crosslinked with the motif. We propose the concept of an ER-targeting suppressor that suppresses the ER-targeting mechanism via a binding factor.
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Report
(3 results)
Research Products
(23 results)
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[Journal Article] A few positively charged residues slow movement of a polypeptide chainacross the endoplasmic reticulum membrane2014
Author(s)
Yamagishi, M., Onishi, Y., Yoshimura, S., Fujita, H., Imai, K., Kida, Y.,and Sakaguchi, M.
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Journal Title
Biochemistry
Volume: 53
Pages: 5375-5383
Related Report
Peer Reviewed / Acknowledgement Compliant
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