A WDR35-dependent coat protein complex transports ciliary membrane cargo vesicles to cilia.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 34734804.
- Also identified by DOI 10.7554/eLife.69786 and PMC identifier 8754431.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Intraflagellar transport (IFT) is a highly conserved mechanism for motor-driven transport of cargo within cilia, but how this cargo is selectively transported to cilia is unclear. WDR35/IFT121 is a component of the IFT-A complex best known for its role in ciliary retrograde transport. In the absence of WDR35, small mutant cilia form but fail to enrich in diverse classes of ciliary membrane proteins. In <i>Wdr35</i> mouse mutants, the non-core IFT-A components are degraded and core components accumulate at the ciliary base. We reveal deep sequence homology of WDR35 and other IFT-A subunits to α and ß' COPI coatomer subunits and demonstrate an accumulation of 'coat-less' vesicles that fail to fuse with <i>Wdr35</i> mutant cilia. We determine that recombinant non-core IFT-As can bind directly to lipids and provide the first in situ evidence of a novel coat function for WDR35, likely with other IFT-A proteins, in delivering ciliary membrane cargo necessary for cilia elongation.
Medical subject headings
- Chlamydomonas reinhardtii
- Cilia
- Cytoskeletal Proteins
- Intracellular Signaling Peptides and Proteins