PUBLICATION

Anks3 interacts with nephronophthisis proteins and is required for normal renal development

Authors
Yakulov, T.A., Yasunaga, T., Ramachandran, H., Engel, C., Müller, B., Hoff, S., Dengjel, J., Lienkamp, S.S., Walz, G.
ID
ZDB-PUB-150212-1
Date
2015
Source
Kidney International   87(6): 1191-200 (Journal)
Registered Authors
Ramachandran, Hari
Keywords
ankyrin-repeat proteins, ciliopathies, nephronophthisis, renal development
MeSH Terms
  • Adaptor Proteins, Signal Transducing/metabolism
  • Animals
  • Carrier Proteins/genetics*
  • Carrier Proteins/metabolism*
  • Cilia/metabolism
  • Gene Knockdown Techniques
  • HEK293 Cells
  • Humans
  • Kidney/abnormalities
  • Kidney/embryology*
  • Kidney Diseases, Cystic/metabolism
  • Membrane Proteins/metabolism
  • Mixed Function Oxygenases/metabolism
  • NIMA-Related Kinases
  • Nuclear Proteins/metabolism
  • Polymerization
  • Protein Kinases/metabolism
  • Proteins/metabolism
  • RNA-Binding Proteins/metabolism
  • Repressor Proteins/metabolism
  • Situs Inversus/genetics
  • Xenopus
  • Xenopus Proteins/genetics
  • Xenopus Proteins/metabolism*
  • Zebrafish
  • Zebrafish Proteins/genetics*
  • Zebrafish Proteins/metabolism
PubMed
25671767 Full text @ Kidney Int.
Abstract
Nephronophthisis (NPH) is a heterogenetic autosomal recessive disorder associated with kidney cysts and multiple extrarenal manifestations. The disease-associated gene products (NPHPs) typically contain domains involved in protein-protein interactions, and appear to exert their tissue-specific functions in large protein complexes. Most NPHPs localize to the cilium and/or basal body; however, their precise molecular functions remain largely unknown. We have recently identified the SAM-domain containing protein Anks3 as a potential ANKS6/NPHP16-interacting protein, and report now that Anks3 interacts with several NPHPs as well as with Bicc1 and the oxygen-sensitive asparaginyl hydroxylase HIF1AN. Knockdown of anks3 in zebrafish embryos was associated with NPH-typical manifestations, including ciliary abnormalities, cyst formation, and laterality defects. In multi-ciliated epidermal cells, GFP-tagged Anks3 localizes to the cilium, but forms large aggregates in the absence of NPHP1, indicating that the negatively charged NPHP1 curtails the polymerization of Anks3. Collectively, these findings suggest that Anks3 is a cilia-associated molecule that partners with the ANKS6- and via NPHP1 to the NPHP1-4-8 module. Thus, developmental defects associated with Anks3 depletion in zebrafish suggest that ANKS3 mutations may cause NPH or NPH-like disease in humans.Kidney International advance online publication, 11 February 2015; doi:10.1038/ki.2015.17.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping