RT Journal Article SR Electronic T1 Protein turnover dynamics suggest a diffusion to capture mechanism for peri-basal body recruitment and retention of intraflagellar transport proteins JF bioRxiv FD Cold Spring Harbor Laboratory SP 2020.11.16.385518 DO 10.1101/2020.11.16.385518 A1 Hibbard, Jaime V.K. A1 Vazquez, Neftali A1 Satija, Rohit A1 Wallingford, John B. YR 2020 UL http://biorxiv.org/content/early/2020/11/17/2020.11.16.385518.abstract AB Intraflagellar transport (IFT) is essential for construction and maintenance of cilia. IFT proteins concentrate at the basal body, where they are thought to assemble into trains and bind cargoes for transport. To study the mechanisms of IFT recruitment to this peri-basal body pool, we quantified protein dynamics of eight IFT proteins, as well as five other basal body localizing proteins, using fluorescence recovery after photobleaching in vertebrate multiciliated cells. We found that members of the IFT-A and IFT-B protein complexes show distinct turnover kinetics from other basal body components. Additionally, known IFT sub-complexes displayed shared dynamics, and these dynamics were not altered during cilia regeneration as compared to homeostasis. Finally, we evaluated the mechanisms of basal body recruitment by depolymerizing cytosolic MTs, which suggested that IFT proteins are recruited to basal bodies through a diffusion-to-capture mechanism. Our survey of IFT protein dynamics provides new insights into IFT recruitment to basal bodies, a crucial step in ciliogenesis.Competing Interest StatementThe authors have declared no competing interest.