A novel in vivo assay for the analysis of protein-protein interaction | Zendy

Mouna Maroun | Zendy; Ami Aronheim | Zendy

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A novel in vivo assay for the analysis of protein-protein interaction

Author(s) -

Mouna Maroun,

Ami Aronheim

Publication year - 1999

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/27.13.e4-i

Subject(s) - biology , vesicle associated membrane protein 8 , protein kinase a , retinoblastoma like protein 1 , protein–protein interaction , reporter gene , microbiology and biotechnology , autophagy related protein 13 , ddb1 , two hybrid screening , cytoplasm , gene , membrane protein , biochemistry , kinase , dna binding protein , mitogen activated protein kinase kinase , gene expression , transcription factor , membrane

The Ras Recruitment System (RRS) is a method for identification and isolation of protein-protein interaction. The method is based on translocation of cytoplasmic mammalian Ras protein to the inner leaflet of the plasma membrane through protein-protein interaction. The system is studied in a temperature-sensitive yeast strain where the yeast Ras guanyl nucleotide exchange factor is inactive at 36 degrees C. Protein-protein interaction results in cell growth at the restrictive temperature. We developed a gene reporter assay for the analysis of protein-protein interaction in mammalian cells. Ras activation in mammalian cells induces the mitogen-activated kinase cascade (MAPK), which can be monitored using Ras-dependent reporter genes. This greatly extends the usefulness of the system and provides a novel assay for protein-protein interaction in mammalian cells.

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