Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-60505
Mol Biol Cell 2024 Mar 01;353:ar39. doi: 10.1091/mbc.E23-03-0084.
Show Gene links Show Anatomy links

Label-free proteomic comparison reveals ciliary and nonciliary phenotypes of IFT-A mutants.

Leggere JC , Hibbard JVK , Papoulas O , Lee C , Pearson CG , Marcotte EM , Wallingford JB .


Abstract
DIFFRAC is a powerful method for systematically comparing proteome content and organization between samples in a high-throughput manner. By subjecting control and experimental protein extracts to native chromatography and quantifying the contents of each fraction using mass spectrometry, it enables the quantitative detection of alterations to protein complexes and abundances. Here, we applied DIFFRAC to investigate the consequences of genetic loss of Ift122, a subunit of the intraflagellar transport-A (IFT-A) protein complex that plays a vital role in the formation and function of cilia and flagella, on the proteome of Tetrahymena thermophila. A single DIFFRAC experiment was sufficient to detect changes in protein behavior that mirrored known effects of IFT-A loss and revealed new biology. We uncovered several novel IFT-A-regulated proteins, which we validated through live imaging in Xenopus multiciliated cells, shedding new light on both the ciliary and non-ciliary functions of IFT-A. Our findings underscore the robustness of DIFFRAC for revealing proteomic changes in response to genetic or biochemical perturbation.

PubMed ID: 38170584
PMC ID: PMC10916875
Article link: Mol Biol Cell
Grant support: [+]

Genes referenced: ak8 ccdc157 cfap45 ift122 pccb pip5kl1 pkm rfx2 sort1
Morpholinos: Ift122 MO1

References [+] :
Ahmed, ODA16 aids axonemal outer row dynein assembly through an interaction with the intraflagellar transport machinery. 2008, Pubmed