Dishevelled stabilization by the ciliopathy protein Rpgrip1l is essential for planar cell polarity
- Authors
- Mahuzier, A., Gaudé, H.M., Grampa, V., Anselme, I., Silbermann, F., Leroux-Berger, M., Delacour, D., Ezan, J., Montcouquiol, M., Saunier, S., Schneider-Maunoury, S., and Vesque, C.
- ID
- ZDB-PUB-120830-40
- Date
- 2012
- Source
- The Journal of cell biology 198(5): 927-940 (Journal)
- Registered Authors
- Anselme, Isabelle, Schneider-Maunoury, Sylvie
- Keywords
- none
- MeSH Terms
-
- Animals
- Cell Line
- Cell Polarity/physiology*
- Cilia/metabolism
- Cilia/physiology*
- Cochlea/metabolism
- Cochlea/physiology
- Mice
- Mice, Inbred C57BL
- Proteins/metabolism*
- Transcription Factors/metabolism
- Zebrafish
- Zebrafish Proteins/metabolism*
- PubMed
- 22927466 Full text @ J. Cell Biol.
Cilia are at the core of planar polarity cellular events in many systems. However, the molecular mechanisms by which they influence the polarization process are unclear. Here, we identify the function of the ciliopathy protein Rpgrip1l in planar polarity. In the mouse cochlea and in the zebrafish floor plate, Rpgrip1l was required for positioning the basal body along the planar polarity axis. Rpgrip1l was also essential for stabilizing dishevelled at the cilium base in the zebrafish floor plate and in mammalian renal cells. In rescue experiments, we showed that in the zebrafish floor plate the function of Rpgrip1l in planar polarity was mediated by dishevelled stabilization. In cultured cells, Rpgrip1l participated in a complex with inversin and nephrocystin-4, two ciliopathy proteins known to target dishevelled to the proteasome, and, in this complex, Rpgrip1l prevented dishevelled degradation. We thus uncover a ciliopathy protein complex that finely tunes dishevelled levels, thereby modulating planar cell polarity processes.