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Published online
doi:10.1083/jcb.200903066
The Journal of Cell Biology, Vol. 186, No. 4, 601-613
The Rockefeller University Press, 0021-9525 $30.00
© Huang et al.
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Article

The ubiquitin conjugation system is involved in the disassembly of cilia and flagella



Kaiyao Huang, Dennis R. Diener, and Joel L. Rosenbaum

Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520

Correspondence to Joel L. Rosenbaum: joel.rosenbaum{at}yale.edu

The disassembly of cilia and flagella is linked to the cell cycle and environmental cues. We have found that ubiquitination of flagellar proteins is an integral part of flagellar disassembly. Free ubiquitin and the ubiquitin-conjugating enzyme CrUbc13 are detected in flagella, and several proteins are ubiquitinated in isolated flagella when exogenous ubiquitin and adenosine triphosphatase are added, suggesting that the ubiquitin conjugation system operates in flagella. Levels of ubiquitinated flagellar proteins increase during flagellar resorption, especially in intraflagellar transport (IFT) mutants, suggesting that disassembly products are labeled with ubiquitin and transported to the cell body by IFT. Substrates of the ubiquitin conjugation system include {alpha}-tubulin (but not β-tubulin), a dynein subunit (IC2), two signaling proteins involved in the mating process, cyclic guanosine monophosphate–dependent kinase, and the cation channel polycystic kidney disease 2. Ubiquitination of flagellar proteins is enhanced early in mating, suggesting that ubiquitination also plays an active role in regulating signaling pathways in flagella.

Abbreviations used in this paper: IBMX, isobutylmethylxanthine; IFT, intraflagellar transport; NaPPi, sodium pyrophosphate.

© 2009 Huang et al.
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