Journal
JOURNAL OF CELL BIOLOGY
Volume 212, Issue 4, Pages 409-423Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.201507046
Keywords
-
Categories
Funding
- Japan Society for the Promotion of Science
- Ministry of Education, Culture, Sports, Science, and Technology of Japan
- Takeda Science Foundation
- Astellas Foundation for Research on Metabolic Disorders
- Princess Takamatsu Cancer Research Fund
- Uehara Memorial Foundation
- Grants-in-Aid for Scientific Research [15K08324, 24113007, 24113001, 25460089, 15H02398] Funding Source: KAKEN
Ask authors/readers for more resources
Primary cilia protrude from the surface of quiescent cells and disassemble at cell cycle reentry. We previously showed that ciliary reassembly is suppressed by trichoplein-mediated Aurora A activation pathway in growing cells. Here, we report that Ndel1, a well-known modulator of dynein activity, localizes at the subdistal appendage of the mother centriole, which nucleates a primary cilium. In the presence of serum, Ndel1 depletion reduces trichoplein at the mother centriole and induces unscheduled primary cilia formation, which is reverted by forced trichoplein expression or coknockdown of KCTD17 (an E3 ligase component protein for trichoplein). Serum starvation induced transient Ndel1 degradation, subsequent to the disappearance of trichoplein at the mother centriole. Forced expression of Ndel1 suppressed trichoplein degradation and axonemal microtubule extension during ciliogenesis, similar to trichoplein induction or KCTD17 knockdown. Most importantly, the proportion of ciliated and quiescent cells was increased in the kidney tubular epithelia of newborn Ndel1-hypomorphic mice. Thus, Ndel1 acts as a novel upstream regulator of the trichopleinAurora A pathway to inhibit primary cilia assembly.
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