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Zur Lage, P., Stefanopoulou, P., Styczynska-Soczka, K., Quinn, N., Mali, G., von Kriegsheim, A., Mill, P., Jarman, A.P. (2018). Ciliary dynein motor preassembly is regulated by Wdr92 in association with HSP90 co-chaperone, R2TP.  J. Cell Biol. 217(7): 2583--2598.
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Research paper

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 unclear. Here we show that in Drosophila melanogaster, the R2TP-associated factor, Wdr92, is required exclusively for axonemal dynein assembly, likely in association with canonical R2TP. Proteomic analyses suggest that in addition to being a regulator of R2TP chaperoning activity, Wdr92 works with the DNAAF Spag1 at a distinct stage in dynein preassembly. Wdr92/R2TP function is likely distinct from that of the DNAAFs proposed to form dynein-specific R2TP-like complexes. Our findings thus establish a connection between dynein assembly and a core multifunctional cochaperone.

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PMC6028525 (PMC) (EuropePMC)
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    J. Cell Biol.
    Journal of Cell Biology
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