The polycystic kidney disease-related proteins Bicc1 and SamCystin interact |
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Authors: | Emily E Stagner Jianlin Cheng |
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Institution: | a Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Missouri, Columbia, MO 65211, USA b Genetics Area Program, University of Missouri, Columbia, MO 65211, USA c Department of Computer Science, Informatics Institute, University of Missouri, Columbia, MO 65211, USA |
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Abstract: | Mutations in either the Bicaudal-C or the Anks6 gene which encode the Bicc1 and SamCystin proteins respectively cause formation of renal cysts in rodent models of polycystic kidney disease, however their role in the mammalian kidney is unknown. Immunolocalization studies demonstrated that, unlike many other PKD-related proteins, SamCystin and Bicc1 do not localize to the primary cilia of cultured kidney cells. Epitope-tagged recombinant SamCystin and Bicc1 proteins were transiently transfected into inner medullary collecting duct (IMCD) cells and co-immunoprecipitated. The results showed that SamCystin self-associates, Bicc1 and SamCystin interact, the mutation responsible for PKD in the Han:SPRD-Cy rat disrupts the self-association of SamCystin but not the Bicc1-SamCystin interaction, and RNA may be an important component of the Bicc1-SamCystin complex. These studies provide the first evidence that Bicc1 and SamCystin interact at the protein level suggesting that they function in a common molecular pathway that when perturbed, is involved in cystogenesis. |
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Keywords: | Polycystic kidney disease Bicc1 Cy SamCystin Anks6 Cysts Protein-protein interaction SAM domain KH domain Ankyrin repeats |
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