Title |
Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3
|
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Published in |
BMC Molecular and Cell Biology, July 2014
|
DOI | 10.1186/1472-6807-14-17 |
Pubmed ID | |
Authors |
Catherine N Leettola, Mary Jane Knight, Duilio Cascio, Sigrid Hoffman, James U Bowie |
Abstract |
Autosomal dominant polycystic kidney disease (ADPKD) is the most common genetic disorder leading to end-stage renal failure in humans. In the PKD/Mhm(cy/+) rat model of ADPKD, the point mutation R823W in the sterile alpha motif (SAM) domain of the protein ANKS6 is responsible for disease. SAM domains are known protein-protein interaction domains, capable of binding each other to form polymers and heterodimers. Despite its physiological importance, little is known about the function of ANKS6 and how the R823W point mutation leads to PKD. Recent work has revealed that ANKS6 interacts with a related protein called ANKS3. Both ANKS6 and ANKS3 have a similar domain structure, with ankyrin repeats at the N-terminus and a SAM domain at the C-terminus. |
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