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| pubmed-article:11073942 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:11073942 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11073942 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11073942 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:11073942 | pubmed:dateCreated | 2001-5-25 | lld:pubmed |
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| pubmed-article:11073942 | pubmed:abstractText | Rag A/Gtr1p are G proteins and are known to be involved in the RCC1-Ran pathway. We employed the two-hybrid method using Rag A as the bait to identify proteins binding to Rag A, and we isolated two novel human G proteins, Rag C and Rag D. Rag C demonstrates homology with Rag D (81.1% identity) and with Gtr2p of Saccharomyces cerevisiae (46.1% identity), and it belongs to the Rag A subfamily of the Ras family. Rag C and Rag D contain conserved GTP-binding motifs (PM-1, -2, and -3) in their N-terminal regions. Recombinant glutathione S-transferase fusion protein of Rag C efficiently bound to both [(3)H]GTP and [(3)H]GDP. Rag A was associated with both Rag C and Rag D in their C-terminal regions where a potential leucine zipper motif and a coiled-coil structure were found. Rag C and D were associated with both the GDP and GTP forms of Rag A. Both Rag C and Rag D changed their subcellular localization, depending on the nucleotide-bound state of Rag A. In a similar way, the disruption of S. cerevisiae GTR1 resulted in a change in the localization of Gtr2p. | lld:pubmed |
| pubmed-article:11073942 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11073942 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11073942 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11073942 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11073942 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11073942 | pubmed:author | pubmed-author:SekiguchiTT | lld:pubmed |
| pubmed-article:11073942 | pubmed:author | pubmed-author:NishimotoTT | lld:pubmed |
| pubmed-article:11073942 | pubmed:author | pubmed-author:NakashimaNN | lld:pubmed |
| pubmed-article:11073942 | pubmed:author | pubmed-author:IiMM | lld:pubmed |
| pubmed-article:11073942 | pubmed:author | pubmed-author:HiroseEE | lld:pubmed |
| pubmed-article:11073942 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11073942 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:11073942 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11073942 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11073942 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11073942 | pubmed:pagination | 7246-57 | lld:pubmed |
| pubmed-article:11073942 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11073942 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11073942 | pubmed:articleTitle | Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B. | lld:pubmed |
| pubmed-article:11073942 | pubmed:affiliation | Department of Molecular Biology, Graduate School of Medical Science, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan. sekigu@molbiol.med.kyushu-u.ac.jp | lld:pubmed |
| pubmed-article:11073942 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11073942 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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