Proteomics

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Ciliary motility and axonemal dynein pre-assembly in Drosophila require Wdr92 in association with the HSP90 co-chaperone, R2TP

ABSTRACT: To clarify the role of Wdr92, and R2TP, in motile cilium formation, we explored its function in Drosophila. We show that Drosophila Wdr92 is a cytoplasmic protein exclusively expressed in motile ciliated cells and is required exclusively for ciliary/flagellar motility. The major effect of its mutation is loss of dynein arms from the axonemes of sensory neuron cilia and sperm flagella. We confirm that Drosophila Wdr92 interacts with R2TP and that R2TP depletion also impairs dynein arm formation. We provide proteomic evidence that Wdr92 is associated especially with heavy chain assembly and propose that it acts as a specificity factor to bring axonemal dynein clients to the R2TP/HSP90 complex. Thus, Wdr92 is a new dynein assembly factor and it strongly reinforces the critical role of HSP90 and co-chaperones in dynein assembly.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Drosophila Melanogaster (fruit Fly) Mus Musculus (mouse)

TISSUE(S): Testis

SUBMITTER: Alex von kriegsheim  

LAB HEAD: Alex von Kriegsheim

PROVIDER: PXD006935 | Pride | 2018-04-25

REPOSITORIES: Pride

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02_CG14353-control-1.raw Raw
03_CG14353-CRISPR-1.raw Raw
04_CG14353-control-2.raw Raw
05_CG14353-CRISPR-2.raw Raw
06_CG14353-control-3.raw Raw
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Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP.

Zur Lage Petra P   Stefanopoulou Panagiota P   Styczynska-Soczka Katarzyna K   Quinn Niall N   Mali Girish G   von Kriegsheim Alex A   Mill Pleasantine P   Jarman Andrew P AP  

The Journal of cell biology 20180509 7

The massive dynein motor complexes that drive ciliary and flagellar motility require cytoplasmic preassembly, a process requiring dedicated dynein assembly factors (DNAAFs). How DNAAFs interact with molecular chaperones to control dynein assembly is not clear. By analogy with the well-known multifunctional HSP90-associated cochaperone, R2TP, several DNAAFs have been suggested to perform novel R2TP-like functions. However, the involvement of R2TP itself (canonical R2TP) in dynein assembly remains  ...[more]

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