In Vitro Methods for CFTR Biogenesis

Methods in Molecular Biology

Volumn 741, Issue , 2011, Pages 233-253

  Matsumura, Yoshihiro ^a   Rooney, LeeAnn ^a   Skach, William R ^a  

^a OREGON HEALTH AND SCIENCE UNIVERSITY   (United States)

Author keywords

Bronchial epithelial cells; canine pancreatic microsomes; cystic fibrosis transmembrane conductance regulator (CFTR); endoplasmic reticulum (ER); in vitro translation; membrane protein; molecular chaperone; protein folding; rabbit reticulocyte lysate (RRL)

Indexed keywords

CAPPED RNA; CELL EXTRACT; INITIATION FACTOR 2; TRANSMEMBRANE CONDUCTANCE REGULATOR;

3' UNTRANSLATED REGION; ANIMAL; ARTICLE; BIOSYNTHESIS; CELL FREE SYSTEM; CELL LINE; CYTOLOGY; DOG; ENDOPLASMIC RETICULUM; GENE EXPRESSION; GENETIC TRANSCRIPTION; GENETICS; HUMAN; INTRACELLULAR MEMBRANE; METABOLISM; MICROSOME; MOUSE; MUTATION; PROTEIN SYNTHESIS; RABBIT; RETICULOCYTE;

3' UNTRANSLATED REGIONS; ANIMALS; CELL EXTRACTS; CELL LINE; CELL-FREE SYSTEM; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; DOGS; ENDOPLASMIC RETICULUM; EUKARYOTIC INITIATION FACTOR-2; GENE EXPRESSION; HUMANS; INTRACELLULAR MEMBRANES; MICE; MICROSOMES; MUTATION; PROTEIN BIOSYNTHESIS; RABBITS; RETICULOCYTES; RNA CAPS; TRANSCRIPTION, GENETIC;

EID: 80051695136     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-117-8_16     Document Type: Chapter

References (27)

1. Skach, W. R. (2009) Cellular mechanisms of membrane protein folding. Nat. Struct. Mol. Biol. 16, 606–612.
2. Oberdorf, J., and Skach, W. R. (2002) In vitro reconstitution of CFTR biogenesis and degradation. Methods Mol. Med. 70, 295–310.
3. Carlson, E., Bays, N., David, L., and Skach, W. R. (2005) Reticulocyte lysate as a model system to study endoplasmic reticulum membrane protein degradation. Methods Mol. Biol. 301, 185–205.
4. Kaufman, R. J. (2004) Regulation of mRNA translation by protein folding in the endoplasmic reticulum. Trends Biochem. Sci. 29, 152–158.
5. Adamson, S. D., Herbert, E., and Godchaux, W. (1968) Factors affecting the rate of protein synthesis in lysate systems from reticulocytes. Arch. Biochem. Biophys. 125, 671–683.
6. Zucker, W. V., and Schulman, H. M. (1968) Stimulation of globin-chain initiation by hemin in the reticulocyte cell-free system. Proc. Natl. Acad. Sci. USA 59, 582–589.
7. Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., and Trachsel, H. (1977) Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell 11, 187–200.
8. Frydman, J., Nimmesgern, E., Ohtsuka, K., and Hartl, F. U. (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370, 111–117.
9. Dalman, F. C., Bresnick, E. H., Patel, P. D., Perdew, G. H., Watson, S. J., Jr., and Pratt, W. B. (1989) Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro. J. Biol. Chem. 264, 19815–19821.
10. Xiong, X., Chong, E., and Skach, W. R. (1999) Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane. J. Biol. Chem. 274, 2616– 2624.
11. Carroll, R., and Lucas-Lenard, J. (1993) Preparation of a cell-free translation system with minimal loss of initiation factor eIF-2/eIF-2B activity. Anal. Biochem. 212, 17–23.
12. Zeenko, V. V., Wang, C., Majumder, M., Komar, A. A., Snider, M. D., Merrick, W. C., et al. (2008) An efficient in vitro translation system from mammalian cells lacking the translational inhibition caused by eIF2 phosphorylation. RNA 14, 593–602.
13. Hartl, F. U., and Hayer-Hartl, M. (2009) Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574–581.
14. Balch, W. E., Morimoto, R. I., Dillin, A., and Kelly, J. W. (2008) Adapting proteostasis for disease intervention. Science 319, 916–919.
15. Hutt, D. M., Powers, E. T., and Balch, W. E. (2009) The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett. 583, 2639–2646.
16. Jackson, R. J., and Hunt, T. (1983) Preparation and use of nuclease-treated rabbit reticulocyte lysates for the translation of eukaryotic messenger RNA. Methods Enzymol. 96, 50–74.
17. Walter, P., and Blobel, G. (1983) Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96, 84–93.
18. Michel, Y. M., Poncet, D., Piron, M., Kean, K. M., and Borman, A. M. (2000) Cap-poly(A) synergy in mammalian cell-free extracts. Investigation of the requirements for poly(A)-mediated stimulation of translation initiation. J. Biol. Chem. 275, 32268– 32276.
19. Melton, D. A., Krieg, P. A., Rebagliati, M. R., Maniatis, T., Zinn, K., and Green, M. R. (1984) Efficient in vitro synthesis of bio-logically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12, 7035–7056.
20. Jagus, R. (1987) Translation in cell-free systems. Methods Enzymol. 152, 267–276.
21. Xiong, X., Bragin, A., Widdicombe, J. H., Cohn, J., and Skach, W. R. (1997) Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator. J. Clin. Invest. 100, 1079–1088.
22. Lu, Y., Xiong, X., Helm, A., Kimani, K., Bragin, A., and Skach, W. R. (1998) Co-and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly. J. Biol. Chem. 273, 568–576.
23. Carveth, K., Buck, T., Anthony, V., and Skach, W. R. (2002) Cooperativity and flexibility of cystic fibrosis transmembrane conductance regulator transmembrane segments participate in membrane localization of a charged residue. J. Biol. Chem. 277, 39507–39514.
24. Scheuner, D., Song, B., McEwen, E., Liu, C., Laybutt, R., Gillespie, P., et al. (2001) Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol. Cell 7, 1165–1176.
25. Gruenert, D. C., Willems, M., Cassiman, J. J., and Frizzell, R. A. (2004) Established cell lines used in cystic fibrosis research. J. Cyst. Fibros. 3, 191–196.
26. Jackson, R. J., Campbell, E. A., Herbert, P., and Hunt, T. (1983) The preparation and properties of gel-filtered rabbit-reticulocyte lysate protein-synthesis systems. Eur. J. Biochem. 131, 289–301.
27. Kaderbhai, M. A., Harding, V. J., Karim, A., Austen, B. M., and Kaderbhai, N. N. (1995) Sheep pancreatic microsomes as an alternative to the dog source for studying protein translocation. Biochem. J. 306, 57–61.