Analysis of soluble protein entry into primary cilia using semipermeabilized cells

Methods in Cell Biology

Volumn 127, Issue , 2015, Pages 203-221

  Breslow, David K ^a   Nachury, Maxence V ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Cilium; Diffusion barrier; Digitonin; Primary cilia; Semipermeabilization

Indexed keywords

GREEN FLUORESCENT PROTEIN; PROTEIN BINDING; SOMATOSTATIN RECEPTOR; SOMATOSTATIN RECEPTOR 3;

AMINO ACID SEQUENCE; ANIMAL; CELL LINE; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CYTOLOGY; CYTOSOL; EPITHELIUM CELL; EUKARYOTIC FLAGELLUM; GENETICS; KIDNEY; METABOLISM; MOLECULAR GENETICS; MOUSE; PHYSIOLOGY; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; CILIA; CYTOSOL; EPITHELIAL CELLS; GREEN FLUORESCENT PROTEINS; KIDNEY; MICE; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN TRANSPORT; RECEPTORS, SOMATOSTATIN; SIGNAL TRANSDUCTION;

EID: 84955410314     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.mcb.2014.12.006     Document Type: Article

References (20)

1. Bielas, S. L., Silhavy, J. L., Brancati, F., Kisseleva, M. V., Al-Gazali, L., Sztriha, L., & Gleeson, J. G. (2009). Mutations in INPP5E, encoding inositol polyphosphate-5-phosphatase E, link phosphatidyl inositol signaling to the ciliopathies. Nature Genetics, 41(9), 1032-1036. http://dx.doi.org/10.1038/ng.423.
2. Breslow, D. K., Koslover, E. F., Seydel, F., Spakowitz, A. J., & Nachury, M. V. (2013). An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier. The Journal of Cell Biology, 203(1), 129-147. http://dx.doi.org/10.1083/jcb.201212024.
3. Calvert, P. D., Schiesser, W. E., & Pugh, E. N. (2010). Diffusion of a soluble protein, photoactivatable GFP, through a sensory cilium. The Journal of General Physiology, 135(3), 173-196. http://dx.doi.org/10.1085/jgp.200910322.
4. Chih, B., Liu, P., Chinn, Y., Chalouni, C., Komuves, L. G., Hass, P. E., & Peterson, A. S. (2012). A ciliopathy complex at the transition zone protects the cilia as a privileged membrane domain. Nature Cell Biology, 14(1), 61-72. http://dx.doi.org/10.1038/ncb2410.
5. Decaen, P. G., Delling, M., Vien, T. N., & Clapham, D. E. (2013). Direct recording and molecular identification of the calcium channel of primary cilia. Nature, 504(7479), 315-318. http://dx.doi.org/10.1038/nature12832.
6. Delling, M., Decaen, P. G., Doerner, J. F., Febvay, S., & Clapham, D. E. (2013). Primary cilia are specialized calcium signalling organelles. Nature, 504(7479), 311-314. http://dx.doi.org/10.1038/nature12833.
7. Francis, S. S., Sfakianos, J., Lo, B., & Mellman, I. (2011). A hierarchy of signals regulates entry of membrane proteins into the ciliary membrane domain in epithelial cells. The Journal of Cell Biology, 193(1), 219-233. http://dx.doi.org/10.1083/jcb.201009001.
8. Garcia-Gonzalo, F. R., & Reiter, J. F. (2012). Scoring a backstage pass: mechanisms of ciliogenesis and ciliary access. The Journal of Cell Biology, 197(6), 697-709. http://dx.doi.org/10.1083/jcb.201111146.
9. Heuck, A. P., Moe, P. C., & Johnson, B. B. (2010). The cholesterol-dependent cytolysin family of gram-positive bacterial toxins. Sub-Cellular Biochemistry, 51, 551-577. http://dx.doi.org/10.1007/978-90-481-8622-8_20.
10. Hoover, D. M., & Lubkowski, J. (2002). DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Research, 30(10), e43.
11. Hu, Q., Milenkovic, L., Jin, H., Scott, M. P., Nachury, M. V., Spiliotis, E. T., et al. (2010). A septin diffusion barrier at the base of the primary cilium maintains ciliary membrane protein distribution. Science, 329(5990), 436-439. http://dx.doi.org/10.1126/science.1191054.
12. Jacoby, M., Cox, J. J., Gayral, S., Hampshire, D. J., Ayub, M., Blockmans, M., & Schurmans, S. (2009). INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse. Nature Genetics, 41(9), 1027-1031. http://dx.doi.org/10.1038/ng.427.
13. Kee, H. L., Dishinger, J. F., Blasius, T. L., Liu, C.-J., Margolis, B., & Verhey, K. J. (2012). A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia. Nature Cell Biology, 14(4), 431-437. http://dx.doi.org/10.1038/ncb2450.
14. Kirchhofer, A., Helma, J., Schmidthals, K., Frauer, C., Cui, S., Karcher, A., & Rothbauer, U. (2010). Modulation of protein properties in living cells using nanobodies. Nature Structural & Molecular Biology, 17(1), 133-138. http://dx.doi.org/10.1038/nsmb.1727.
15. Mukhopadhyay, S., Wen, X., Chih, B., Nelson, C. D., Lane, W. S., Scales, S. J., et al. (2010). TULP3 bridges the IFT-A complex and membrane phosphoinositides to promote trafficking of G protein-coupled receptors into primary cilia. Genes and Development, 24(19), 2180-2193. http://dx.doi.org/10.1101/gad.1966210.
16. Nachury, M. V. (2014). How do cilia organize signalling cascades? Philosophical Transactions of the Royal Society of London, Series B: Biological Sciences, 369(1650) http://dx.doi.org/10.1098/rstb.2013.0465.
17. Nair, K. S., Hanson, S. M., Mendez, A., Gurevich, E. V., Kennedy, M. J., Shestopalov, V. I., & Slepak, V. Z. (2005). Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron, 46(4), 555-567. http://dx.doi.org/10.1016/j.neuron.2005.03.023.
18. Najafi, M., Maza, N. A., & Calvert, P. D. (2012). Steric volume exclusion sets soluble protein concentrations in photoreceptor sensory cilia. Proceedings of the National Academy of Sciences of the USA, 109(1), 203-208. http://dx.doi.org/10.1073/pnas.1115109109.
19. Reiter, J. F., Blacque, O. E., & Leroux, M. R. (2012). The base of the cilium: roles for transition fibres and the transition zone in ciliary formation, maintenance and compartmentalization. EMBO Reports, 13(7), 608-618. http://dx.doi.org/10.1038/embor.2012.73.
20. Ye, F., Breslow, D. K., Koslover, E. F., Spakowitz, A. J., Nelson, W. J., & Nachury, M. V. (2013). Single molecule imaging reveals a major role for diffusion in the exploration of ciliary space by signaling receptors. eLife, 2, e00654. http://dx.doi.org/10.7554/eLife.00654.