A short carboxy-terminal domain of polycystin-1 reorganizes the microtubular network and the endoplasmic reticulum |
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Authors: | Hongyu Gao,Lorenz K. Sellin,Michael Pü tz,Michael Imgrund,Roland Nitschke,Albrecht G. Kramer-Zucker |
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Affiliation: | a Renal Division, University Hospital Freiburg, Hugstetter Strasse 55, 79106 Freiburg, Germany b Renal Division, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, China c Renal Division, Department of Medicine, University Hospital Düsseldorf, Düsseldorf, Germany d Institute of Biology I, Life Imaging Center, University of Freiburg, Freiburg, Germany |
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Abstract: | Mutations of PKD1 cause autosomal dominant polycystic kidney disease (ADPKD), a syndrome characterized by kidney cysts and progressive renal failure. Polycystin-1, the protein encoded by PKD1, is a large integral membrane protein with a short carboxy-terminal cytoplasmic domain that appears to initiate multiple cellular programs. We report now that this polycystin-1 domain contains a novel motif responsible for rearrangements of intermediate filaments, microtubules and the endoplasmic reticulum (ER). This motif reveals homology to CLIMP-63, a microtubule-binding protein that rearranges the ER. Our findings suggest that polycystin-1 influences the shape and localization of both the microtubular network and the ER. |
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Keywords: | Polycystic kidney disease PKD Polycystin-1 TRPP2 Endoplasmic reticulum Microtubule Cytoskeleton |
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