Degrading proteins at the primary cilium

Wrighton, Katharine H.

doi:10.1038/nrm4035

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Published: 23 July 2015

Cytoskeleton

Degrading proteins at the primary cilium

Katharine H. Wrighton

Nature Reviews Molecular Cell Biology volume 16, page 453 (2015)Cite this article

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As mutations in the gene encoding the ciliary protein RPGRIP1L cause ciliopathies, Gerhardt et al. characterized this protein further. They confirmed its presence at the ciliary transition zone of cilia in mouse embryonic fibroblasts (MEFs) and in the limbs of mouse embryos; cilia were longer in the absence of RPGRIP1L in both systems. The authors asked whether RPGRIP1L influenced ciliary signalling to control cilia length and found that a component of the sonic hedgehog pathway was inefficiently processed in Rpgrip1l-null MEFs and that a phosphorylated form of β-catenin (a mediator of WNT signalling) accumulated at the ciliary base in these cells. These data suggest that RPGRIP1L promotes proteasomal activity at the ciliary base. Indeed, RPGRIP1L promoted protein degradation specifically in primary cilia by interacting with PSMD2, a component of the 19S proteasomal subunit, at the transition zone.

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References

Gerhardt, C. et al. The transition zone protein Rpgrip1l regulates proteasomal activity at the primary cilium. J. Cell Biol. 210, 115–133 (2015)
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