期刊
MOLECULAR BIOLOGY OF THE CELL
卷 28, 期 5, 页码 624-633出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E16-09-0648
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资金
- Ministry of Education, Culture, Sports, Science and Technology, Japan [25113514, 15H01211]
- Japan Society for the Promotion of Science [22390013, 15H04370, 15K14456, 25860044, 15K07929]
- Uehara Memorial Foundation
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [15K14456, 25860044, 15H04370, 25113514, 22390013, 15K07929, 15H01211] Funding Source: KAKEN
Cilia function as cellular antennae to sense and transduce extracellular signals. A number of proteins are specifically localized in cilia. Anterograde and retrograde ciliary protein trafficking are mediated by the IFT-B and IFT-A complexes in concert with kinesin-2 and dynein-2 motors, respectively. However, the role of KIF17, a homodimeric kinesin-2 protein, in protein trafficking has not been fully understood in vertebrate cilia. In this study, we demonstrated, by using the visible immunoprecipitation assay, that KIF17 interacts with the IFT46-IFT56 dimer in the IFT-B complex through its C-terminal sequence located immediately upstream of the nuclear localization signal ( NLS). We then showed that KIF17 reaches the ciliary tip independently of its motor domain and requires IFT-B binding for its entry into cilia rather than for its intraciliary trafficking. We further showed that KIF17 ciliary entry depends not only on its binding to IFT-B but also on its NLS, to which importin a proteins bind. Taking the results together, we conclude that in mammalian cells, KIF17 is dispensable for ciliogenesis and IFT-B trafficking but requires IFT-B, as well as its NLS, for its ciliary entry across the permeability barrier located at the ciliary base.
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