A ribosome-associating factor chaperones tail-anchored membrane proteins (original) (raw)
References
Rabu, C., Schmid, V., Schwappach, B. & High, S. Biogenesis of tail-anchored proteins: the beginning for the end? J. Cell Sci.122, 3605–3612 (2009) ArticleCAS Google Scholar
Stefanovic, S. & Hegde, R. S. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell128, 1147–1159 (2007) ArticleCAS Google Scholar
Schuldiner, M. et al. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell134, 634–645 (2008) ArticleCAS Google Scholar
Favaloro, V., Spasic, M., Schwappach, B. & Dobberstein, B. Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins. J. Cell Sci.121, 1832–1840 (2008) ArticleCAS Google Scholar
Jonikas, M. C. et al. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science323, 1693–1697 (2009) ArticleADSCAS Google Scholar
Copic, A. et al. Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics182, 757–769 (2009) ArticleCAS Google Scholar
Chang, Y. W. et al. Crystal structure of Get4–Get5 complex and its interactions with Sgt2, Get3, and Ydj1. J. Biol. Chem.285, 9962–9970 (2010) ArticleCAS Google Scholar
Bozkurt, G. et al. The structure of Get4 reveals an α-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis. FEBS Lett.584, 1509–1514 (2010) ArticleCAS Google Scholar
Chartron, J. W., Suloway, C. J. M., Zaslaver, M. & Clemons, W. M., Jr Structural characterization of the Get4/5 complex and its interaction with Get3. Proc. Natl Acad. Sci. USA107, 12127–12132 (2010) ArticleADSCAS Google Scholar
Leznicki, P., Clancy, A., Schwappach, B. & High, S. Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci.123, 2170–2178 (2010) ArticleCAS Google Scholar
Ito, T. et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl Acad. Sci. USA98, 4569–4574 (2001) ArticleADSCAS Google Scholar
Krogan, N. J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature440, 637–643 (2006) ArticleADSCAS Google Scholar
Berndt, U., Oellerer, S., Zhang, Y., Johnson, A. E. & Rospert, S. A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel. Proc. Natl Acad. Sci. USA106, 1398–1403 (2009) ArticleADSCAS Google Scholar
Lodish, H. F. & Jacobsen, M. Regulation of hemoglobin synthesis: equal rates of translation and termination of α- and β-globin chains. J. Biol. Chem.247, 3622–3629 (1972) CASPubMed Google Scholar
Wolin, S. L. & Walter, P. Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate. J. Cell Biol.109, 2617–2622 (1989) ArticleCAS Google Scholar
Cao, J. & Geballe, A. P. Coding sequence-dependent ribosomal arrest at termination of translation. Mol. Cell. Biol.16, 603–608 (1996) ArticleCAS Google Scholar
Mateja, A. et al. The structural basis of tail-anchored membrane protein recognition by Get3. Nature461, 361–366 (2009) ArticleADSCAS Google Scholar
Bozkurt, G. et al. Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc. Natl Acad. Sci. USA106, 21131–21136 (2009) ArticleADSCAS Google Scholar
Suloway, C. J., Chartron, J. W., Zaslaver, M. & Clemons, W. M., Jr Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc. Natl Acad. Sci. USA106, 14849–14854 (2009) ArticleADSCAS Google Scholar
Yamagata, A. et al. Structural insight into the membrane insertion of tail-anchored proteins by Get3. Genes Cells15, 29–41 (2010) ArticleCAS Google Scholar
Hu, J., Li, J., Qian, X., Denic, V. & Sha, B. The crystal structures of yeast Get3 suggest a mechanism for tail-anchored protein membrane insertion. PLoS ONE4, e8061 (2009) ArticleADS Google Scholar
Desmots, F., Russell, H. R., Lee, Y., Boyd, K. & McKinnon, P. J. The Reaper-binding protein Scythe modulates apoptosis and proliferation during mammalian development. Mol. Cell. Biol.25, 10329–10337 (2005) ArticleCAS Google Scholar
Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature427, 808–814 (2004) ArticleADSCAS Google Scholar
Wang, S., Sakai, H. & Wiedmann, M. NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center. J. Cell Biol.130, 519–528 (1995) ArticleCAS Google Scholar
Gautschi, M. et al. RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin. Proc. Natl Acad. Sci. USA98, 3762–3767 (2001) ArticleADSCAS Google Scholar
Kramer, G., Boehringer, D., Ban, N. & Bukau, B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nature Struct. Mol. Biol.16, 589–597 (2009) ArticleCAS Google Scholar
Hobden, A. N. & Cundliffe, E. The mode of action of alpha sarcin and a novel assay of the puromycin reaction. Biochem. J.170, 57–61 (1978) ArticleCAS Google Scholar
High, S., Gorlich, D., Wiedmann, M., Rapoport, T. A. & Dobberstein, B. The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER. J. Cell Biol.113, 35–44 (1991) ArticleCAS Google Scholar
Fons, R. D., Bogert, B. A. & Hegde, R. S. Substrate-specific function of the translocon-associated protein complex during translocation across the ER membrane. J. Cell Biol.160, 529–539 (2003) ArticleCAS Google Scholar