Shuttling and sorting lipid-modified cargo into the cilia

Biochem Soc Trans. 2016 Oct 15;44(5):1273-1280. doi: 10.1042/BST20160122.


Primary cilia are hair-like microtubule-based organelles that can be found on almost all human cell types. Although the cilium is not separated from the cell by membranes, their content is different from that of the cell body and their membrane composition is distinct from that of the plasma membrane. Here, we will introduce a molecular machinery that shuttles and sorts lipid-modified proteins to the cilium, thus contributing in maintaining its distinct composition. The mechanism involves the binding of the GDI-like solubilising factors, uncoordinated (UNC)119a, UNC119b and PDE6D, to the lipid-modified ciliary cargo and the specific release of the cargo in the cilia by the ciliary small G-protein Arl3 in a GTP-dependent manner.

Keywords: G-proteins; cilia; trafficking.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP-Ribosylation Factors / metabolism*
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Animals
  • Cilia / metabolism*
  • Cyclic Nucleotide Phosphodiesterases, Type 6 / metabolism*
  • Guanosine Triphosphate / metabolism
  • Humans
  • Membrane Lipids / metabolism*
  • Models, Biological
  • Protein Transport


  • Adaptor Proteins, Signal Transducing
  • Membrane Lipids
  • UNC119 protein, human
  • Guanosine Triphosphate
  • PDE6D protein, human
  • Cyclic Nucleotide Phosphodiesterases, Type 6
  • ADP-Ribosylation Factors
  • ARL3 protein, human