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Accession number;05A0630943
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| Title;Critical role of posttranslational modification of Ras proteins in effector activation |
| Author;
SHIMA FUMI
(Kobedai Daigakuin'igakukeikenkyuka Bunshisaibouseibutsugaku Bunshiseibutsugakubun'ya)
KATAOKA TOORU
(Kobedai Daigakuin'igakukeikenkyuka Bunshisaibouseibutsugaku Bunshiseibutsugakubun'ya)
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Journal Title;Seikagaku
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Journal Code:G0184A
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ISSN:0037-1017
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VOL.77;NO.6;PAGE.519-526(2005)
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| Figure&Table&Reference; |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;Ras protein, the product of ras oncogene, is a low-molecular-weight G protein and functions as a molecular switch in intracellular signal transmission. Ras undergoes a series of post-translational lipid modifications including farnesyl group addition at the C-terminal. These lipid modifications play an important role not only in Ras localization in membrane but also in its interaction with the effector protein. The mechanism of the lipid modifications is mediated by Ras binding at the second binding site present on the effector protein. Recent analyses of high-level structure are clarifying that Ras lipid modifications cause a structural alteration in a specific cellular domain, particularly in the activator domain, and the alteration causes changes in the manner of Ras interaction with the effector protein. This article summarizes recent findings on the analyses of high-level structure of the Ras-effector interaction and discusses the significance of post-translational modifications. (Author's abstract). |
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