RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly
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- Yuya Nishijima
- Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
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- Yohei Hagiya
- Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
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- Tomohiro Kubo
- University of Yamanashi Graduate School of Medical Science, Chuo 409-3898, Japan
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- Ryota Takei
- Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
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- Yohei Katoh
- Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
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- Kazuhisa Nakayama
- Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
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- Yixian Zheng
- editor
書誌事項
- 公開日
- 2017-06-15
- 資源種別
- journal article
- DOI
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- 10.1091/mbc.e17-01-0017
- 公開者
- American Society for Cell Biology (ASCB)
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説明
<jats:p> Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and that CEP19 is recruited to the centriole probably via its binding to the centrosomal protein FGFR1OP. Disruption of the RABL2 gene in Chlamydomonas reinhardtii results in the nonflagellated phenotype, suggesting a crucial role of RABL2 in ciliary/flagellar assembly. We also show that RABL2 interacts, in its GTP-bound state, with the intraflagellar transport (IFT)-B complex via the IFT74–IFT81 heterodimer and that the interaction is disrupted by a mutation found in male infertile mice (Mot mice) with a sperm flagella motility defect. Intriguingly, RABL2 binds to CEP19 and the IFT74–IFT81 heterodimer in a mutually exclusive manner. Furthermore, exogenous expression of the GDP-locked or Mot-type RABL2 mutant in human cells results in mild defects in ciliary assembly. These results indicate that RABL2 localized to the basal body plays crucial roles in ciliary/flagellar assembly via its interaction with the IFT-B complex. </jats:p>
収録刊行物
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- Molecular Biology of the Cell
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Molecular Biology of the Cell 28 (12), 1652-1666, 2017-06-15
American Society for Cell Biology (ASCB)
