Rothe, BenjaminGagnieux, CelineLeal-Esteban, Lucia CarolinaConstam, Daniel B.2020-03-112020-03-112020-03-112020-04-0110.1016/j.cellsig.2019.109499https://infoscience.epfl.ch/handle/20.500.14299/167175WOS:000515207300016Polycystic 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 a 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.Cell Biologyciliopathiescystic kidney diseasepkdmrna translationp-bodiessam domainsterile alpha-motifmessenger-rnastranslational repressionmouse modelnek8mutationslocalizationbicc1nephronophthisiskinasetext::journal::journal article::research article