The primary cilium is a microtubule-based organelle that performs sensory functions and is often referred to as the antenna of the cell. Cilium assembly and disassembly, in most cells, is tightly regulated in concert with the cell cycle. Although we understand a great deal about how cells build up the cilium, the molecular mechanisms responsible for cilium disassembly as cells re-enter the cell cycle after quiescence are less clear. Now, Matsumoto and colleagues (Hanafusa et al., 2022) study this question in RPE cells in which they trigger cilium formation and resorption by serum starvation and serum addition, respectively. They first identify the kinase LRRK1 as a key factor required for serum-induced ciliary resorption. The authors then investigate its upstream and downstream targets and reveal that LRRK1 is phosphorylated by the kinase PLK1 at the ciliary base, and in turn LRRK1 phosphorylates the protein NDEL1, a known positive regulator of cilium disassembly. Finally, by monitoring the localisation of IFT88, a subunit of the intraflagellar transport (IFT)-B complex, the authors find that the loss of LRRK1 or NDEL1 impairs dynein-2-driven retrograde IFT. Together, these results identify a PLK1-LRRK1-NDEL1 axis that regulates cilium disassembly by affecting IFT.
L(IFT)ing the lid on cilium disassembly
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L(IFT)ing the lid on cilium disassembly. J Cell Sci 1 November 2022; 135 (21): e135_e2102. doi:
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