English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Bardet-Biedl syndrome (BBS) is a rare human ciliopathy associated with blindness, obesity, and kidney anomalies. It is caused by defects in the assembly or transport of the BBSome, a conserved octamer of BBS proteins, which assists intraflagellar transport (IFT) with the removal of signaling proteins from cilia. Here, we show that the GTPase component of IFT-B1, IFT22, autonomous of IFT-B1 association, binds and stabilizes BBS3 in the cell body. When both are in their GTP-bound state, IFT22 and BBS3 recruit the BBSome to the basal body for loading onto the IFT machinery for ciliary entry. IFT22 recruits the BBSome to the basal body through BBS3 in a nucleotide-dependent manner providing a regulatory mechanism for BBSome entry into the cilium.

Intraflagellar transport protein RABL5/IFT22 recruits the BBSome to the basal body through the GTPase ARL6/BBS3