Journal
JOURNAL OF CELL BIOLOGY
Volume 217, Issue 7, Pages 2583-2598Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201709026
Keywords
-
Categories
Funding
- Medical Research Council [MR/K018558/1, MC_UU_12018/26]
- Medical Research Council [MR/K018558/1, MC_UU_12018/26, MC_UU_00007/14] Funding Source: researchfish
- MRC [MC_UU_00007/14, MC_UU_12018/26, MR/K018558/1] Funding Source: UKRI
Ask authors/readers for more resources
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 DNA AFs 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available