2012 Fiscal Year Final Research Report
Functional analysis of budding yeast Cullin based E3
Project/Area Number |
22370051
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Functional biochemistry
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Research Institution | Nagoya University |
Principal Investigator |
KAMURA Takumi 名古屋大学, 理学研究科, 教授 (40333455)
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Project Period (FY) |
2010 – 2012
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Keywords | タンパク質分解 |
Research Abstract |
Protein degradation via ubiquitin-proteasome system regulates a variety of cellular processes. In budding yeast, the cullin protein family includes three members: Cdc53, Cul3, and Cul8. Recently we have reported Lag2 as a novel regulator of SCF complex. In this study, we performed the functional analysis of Lag2, Cul3 and Cul8. We identify that a single lysine, K16, on Lag2 is a target of Rub1 conjugation and Dcn1 is required for this reaction. Like wild-type Lag2, Lag2 K16R mutant also negatively modulates the SCF function, indicating that Rub1 conjugation to Lag2 is not required for the function of Lag2. In budding yeast, the BTB protein family includes four members. We identify a BTB protein, Yil001w as a Cul3 binding protein and Okp1 as a candidate of Cul3-type E3. Furthermore, we identify several proteins as Cul8 binding proteins. These observations indicate that Cul3 and Cul8 form complexes and function as E3 ubiquitin ligases.
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[Journal Article] Activation of double-stranded RNA-activated protein kinase (PKR) by interferon-stimulated gene 15 (ISG15) modification down-regulates protein translation2013
Author(s)
Okumura, F., Okumura, AJ., Uematsu, K., Hatakeyama, S., Zhang, DE., Kamura, T
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Journal Title
J Biol Chem
Volume: 288(4)
Pages: 2839-47
DOI
Peer Reviewed
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[Journal Article] Non-SCF type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase Ypt52 and inhibits Ypt52 function2011
Author(s)
Liu, Y., Nakatsukasa, K., Kotera, M., Kanada, A., Nishimura, T., Kishi, T., Mimura, S., Kamura, T
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Journal Title
Mol. Biol. Cell
Volume: 22
Pages: 1575-1584
DOI
Peer Reviewed
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