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. 2018 Jul 1;29(13):1611–1627. doi: 10.1091/mbc.E18-02-0088

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© 2018 Copeland et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 9: — Cep170 is an FHDC1-interacting protein. BirA*-tagged FHDC1 was expressed in NIH 3T3 cells by transient transfection. Ciliogenesis was induced as before in low-serum media. BirA*-FHDC1 (red) was detected by virtue of the encoded myc-tag. (A) BirA*-FHDC1 is recruited to the elongated cilia and, following exogenous biotin treatment, induces biotinylation of cytoplasmic microtubules (green) and the cilia (acetylated tubulin, white). Specific punctate structures within the cytoplasmic microtubule network were also labeled (arrows). Biotinylated proteins were detected with Alexa488-streptavidin. (B) BirA*-FHDC1 (red) induces biotinylation of puncta (green) that colocalize with γ-tubulin puncta detected with anti–γ-tubulin (white). (C) BirA*-FHDC1 induces biotinylation of endogenous Cep170. As in B, BirA*-FHDC1 was expressed by transient transfection and its ability to induce biotinylation of the endogenous Cep170 was assessed by IB. myc-FHDC1 and FMNL2-BirA* were included as negative controls. Total biotinylated proteins were isolated from each sample using streptavidin–agarose beads. The eluted proteins were immunoblotted using the indicated antibodies. Endogenous Cep170 is only present in the pool of biotinylated proteins induced by BirA*-FHDC1 (arrow).