RGS5 is a R4 type RGS that regulates GPCR signalling. Using western blot, we detected RGS5 as a specific 23 kDa protein in cells overexpressing RGS5. A 42 kDa band representing a possible RGS5 dimer was also detected. Given that GPCRs and their associated proteins form complexes involving multiple protein-protein interactions, we investigated the possibility that the 42 kDa band represents an RGS5-RGS5 dimer. RGS5 dimerization was confirmed by the analysis of a GFP tagged RGS5 fusion in yeast and with two-hybrid assays. Analysis of RGS5 in HEK293A cells suggests that the dimer may serve a regulatory function since it is longer lived than the monomer. Copyright © 2007 S. Karger AG.
CITATION STYLE
Yang, Z., Gaudio, S., Song, W., Greenwood, M., Jean-Baptiste, G., & Greenwood, M. T. (2007). Evidence for the dimerization of human regulator of G-protein signalling 5 (RGS5). Cellular Physiology and Biochemistry, 20(5), 303–310. https://doi.org/10.1159/000107516
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