PUBLICATION

The Retinitis Pigmentosa Protein RP2 Interacts With Polycystin 2 and Regulates Cilia-Mediated Vertebrate Development

Authors
Hurd, T., Zhou, W., Jenkins, P., Liu, C.J., Swaroop, A., Khanna, H., Martens, J., Hildebrandt, F., and Margolis, B.
ID
ZDB-PUB-100826-13
Date
2010
Source
Human molecular genetics   19(22): 4330-4344 (Journal)
Registered Authors
Khanna, Hemant, Zhou, Weibin
Keywords
none
MeSH Terms
  • Acylation
  • Animals
  • Cilia/genetics
  • Cilia/metabolism
  • Cilia/physiology*
  • Eye Proteins/metabolism*
  • Gene Knockdown Techniques
  • Humans
  • Intracellular Signaling Peptides and Proteins/metabolism*
  • Kidney/metabolism
  • Kidney/physiopathology
  • Kidney Diseases, Cystic/genetics
  • Kidney Diseases, Cystic/metabolism
  • Membrane Proteins/metabolism*
  • Mutation
  • TRPP Cation Channels/metabolism*
  • Vertebrates/genetics
  • Vertebrates/metabolism
  • Zebrafish/genetics
  • Zebrafish/metabolism
PubMed
20729296 Full text @ Hum. Mol. Genet.
Abstract
Ciliopathies represent a growing group of human genetic diseases whose etiology lies in defects in ciliogenesis or ciliary function. Given the established entity of renal-retinal ciliopathies, we have been examining the role of cilia-localized proteins mutated in Retinitis Pigmentosa (RP) in regulating renal ciliogenesis or cilia-dependent signaling cascades. Specifically, this study examines the role of the RP2 gene product with an emphasis on renal and vertebrate development. We demonstrate that in renal epithelia RP2 localizes to the primary cilium through dual acylation of the amino-terminus. We also show that RP2 forms a calcium-sensitive complex with the autosomal dominant polycystic kidney disease protein Polycystin 2. Ablation of RP2 by shRNA promotes swelling of the cilia tip that may be a result of aberrant trafficking of Polycystin 2 and other ciliary proteins. Morpholino-mediated repression of RP2 expression in zebrafish results in multiple developmental defects that have been previously associated with ciliary dysfunction such as hydrocephalus, kidney cysts and situs inversus. Finally we demonstrate that in addition to our observed physical interaction between RP2 and Polycystin 2, dual morpholino-mediated knockdown of Polycystin 2 and RP2 results in enhanced situs inversus, indicating that these two genes also regulate a common developmental process. This work suggests that RP2 may be an important regulator of ciliary function through its association with Polycystin 2 and provides evidence of a further link between retinal and renal cilia function.
Genes / Markers
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Mutations / Transgenics
Human Disease / Model
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Mapping