ArticleNucleic acids research2003
Adaptation of the Ras-recruitment system to the analysis of interactions between membrane-associated proteins.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 21 citations in OpenAlex.
- Gγ recruitment systems specifically select PPI and affinity-enhanced candidate proteins that interact with membrane protein targets.Scientific reports · 2015Article
- Gap junction channel protein innexin 2 is essential for epithelial morphogenesis in the Drosophila embryo.Molecular biology of the cell · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Interactions of membrane-associated proteins play important roles in many cellular processes. The yeast two-hybrid assay is of limited utility for the analysis of such interactions, due to the need for soluble protein partners, whose interaction is assessed in the nucleus. The advent of the Ras-recruitment system (RRS) has enabled the study of membrane-associated proteins interacting with cytoplasmic proteins fused to Ras. Constitutive membrane association of the Ras fusion protein is expected to complement the growth defect of the yeast strain CDC25-2, assayed in the RRS, independent from the interaction with a membrane-bound partner. We describe the adaptation of the RRS to the analysis of interactions between two membrane-associated proteins using a model system. These results may facilitate the study of protein-protein interactions between membrane-bound proteins and further increase the utility of the RRS.
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