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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Cell Line
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Cytoskeletal Proteins / genetics
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Cytoskeletal Proteins / metabolism
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Ecdysterone / analogs & derivatives
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Ecdysterone / metabolism
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Endoplasmic Reticulum / metabolism*
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Humans
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Membrane Proteins / genetics
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Membrane Proteins / metabolism
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Mice
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Microtubules / metabolism*
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Molecular Sequence Data
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Polycystic Kidney, Autosomal Dominant / genetics
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Polycystic Kidney, Autosomal Dominant / metabolism
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Protein Structure, Tertiary
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Sequence Alignment
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TRPP Cation Channels / genetics
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TRPP Cation Channels / metabolism*
Substances
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CKAP4 protein, human
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Cytoskeletal Proteins
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Membrane Proteins
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TRPP Cation Channels
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polycystic kidney disease 1 protein
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muristerone A
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Ecdysterone