Role of the RNA-binding protein Bicaudal-C1 and interacting factors in cystic kidney diseases.
Ciliopathies
Cystic kidney disease
P-bodies
PKD
SAM domain
mRNA translation
Journal
Cellular signalling
ISSN: 1873-3913
Titre abrégé: Cell Signal
Pays: England
ID NLM: 8904683
Informations de publication
Date de publication:
04 2020
04 2020
Historique:
received:
30
09
2019
revised:
09
12
2019
accepted:
10
12
2019
pubmed:
16
12
2019
medline:
10
6
2021
entrez:
16
12
2019
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 31838063
pii: S0898-6568(19)30295-5
doi: 10.1016/j.cellsig.2019.109499
pii:
doi:
Substances chimiques
RNA-Binding Proteins
0
RNA
63231-63-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
109499Informations de copyright
Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.