2013 Fiscal Year Final Research Report
Regulation of peroxisomal protein import by modification of cysteine residue
| Project/Area Number |
24770130
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Functional biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
OKUMOTO Kanji 九州大学, 理学(系)研究科(研究院), 助教 (20363319)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Keywords | 細胞内小器官 / ユビキチン化 / タンパク質輸送 / RINGフィンガー |
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| Research Abstract |
Peroxisome is an essential organelle containing various metabolic pathways and the physiological functions are assured by selective protein import into peroxisomes. Pex5p, a cytosolic receptor of peroxisome targeting signal type-1, plays a pivotal role in peroxisome matrix protein import.
This study clarified that Pex5p is modified by three distinct modes of ubiquitination, a cysteine-linked monoubiquitination and two types of lysine-linked monoubiquitination. Cys-linked ubiquitination of Pex5p is prerequisite for export of Pex5p from peroxisomal membrane to the cytosol and its complementing activity. On the other hand, monoubiquitination of Pex5p at multiple lysine residues ensures the efficient export of Pex5p from peroxisomes. Monoubiquitination of Pex5p at Lys520 in vivo might play a role in self-inhibition of Pex5p in the cargo recognition in the cytosol. Therefore, import of peroxisome matrix proteins is elaborately regulated by unique ubiquitin modifications of Pex5p.
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Research Products
(10 results)
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[Book] Molecular basis for peroxisome biogenesis disorders. In : Brocard, C. and Hartig, A. (eds) Molecular machines involved in peroxisomes maintenance2014
Author(s)
Fujiki, Y., Okumoto, K., Mukai, S., and Tamura, S.
Publisher
Berlin, Springer-Verlag (in press)
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