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- W2994830025 endingPage "109499" @default.
- W2994830025 startingPage "109499" @default.
- W2994830025 abstract "Polycystic kidneys frequently associate with mutations in individual components of cilia, basal bodies or centriolar satellites that perturb complex protein networks. In this review, we focus on the RNA-binding protein Bicaudal-C1 (BICC1) which was found mutated in renal cystic dysplasia, and on its interactions with the ankyrin repeat and sterile α motif (SAM)-containing proteins ANKS3 and ANKS6 and associated kinases and their partially overlapping ciliopathy phenotypes. After reviewing BICC1 homologs in model organisms and their functions in mRNA and cell metabolism during development and in renal tubules, we discuss recent insights from cell-based assays and from structure analysis of the SAM domains, and how SAM domain oligomerization might influence multivalent higher order complexes that are implicated in ciliary signal transduction." @default.
- W2994830025 created "2019-12-26" @default.
- W2994830025 creator A5010009278 @default.
- W2994830025 creator A5039697019 @default.
- W2994830025 creator A5054495304 @default.
- W2994830025 date "2020-04-01" @default.
- W2994830025 modified "2023-10-17" @default.
- W2994830025 title "Role of the RNA-binding protein Bicaudal-C1 and interacting factors in cystic kidney diseases" @default.
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