A ribosome-associating factor chaperones tail-anchored membrane proteins

Nature

Volumn 466, Issue 7310, 2010, Pages 1120-1124

  Mariappan, Malaiyalam ^a   Li, Xingzhe ^a,b   Stefanovic, Sandra ^a   Sharma, Ajay ^a   Mateja, Agnieszka ^c   Keenan, Robert J ^c   Hegde, Ramanujan S ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

^b PEKING UNIVERSITY HEALTH SCIENCE CENTER   (China)

^c UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BAT3 PROTEIN; CHAPERONE; MEMBRANE PROTEIN; TRC35 PROTEIN; TRC40 PROTEIN; UBL4A PROTEIN; UNCLASSIFIED DRUG;

CELL ORGANELLE; MEMBRANE; PROTEIN; YEAST;

ARTICLE; CONTROLLED STUDY; PRIORITY JOURNAL; PROTEIN DEPLETION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN SYNTHESIS; PROTEIN TARGETING; RIBOSOME;

CARRIER PROTEINS; ENDOPLASMIC RETICULUM; HUMANS; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; PROTEIN TRANSPORT; RIBOSOMES; SIGNAL RECOGNITION PARTICLE; UBIQUITINS;

EID: 77956183398     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature09296     Document Type: Article

References (30)

1. 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).
2. Stefanovic, S. & Hegde, R. S. Identification of a targeting factor for posttranslational membrane protein insertion into the ER. Cell 128, 1147-1159 (2007).
3. Schuldiner, M. et al. The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134, 634-645 (2008).
4. 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).
5. Jonikas, M. C. et al. Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323, 1693-1697 (2009).
6. Copic, A. et al. Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics 182, 757-769 (2009).
7. Costanzo, M. et al. The genetic landscape of a cell. Science 327, 425-431 (2010).
8. 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).
9. Bozkurt, G. et al. The structure of Get4 reveals an a-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis. FEBS Lett. 584, 1509-1514 (2010).
10. 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. USA 107, 12127-12132 (2010).
11. Leznicki, P., Clancy, A., Schwappach, B. & High, S. Bat3 promotes the membrane integration of tail-anchored proteins. J. Cell Sci. 123, 2170-2178 (2010).
12. Ito, T. et al. A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc. Natl Acad. Sci. USA 98, 4569-4574 (2001).
13. Krogan, N. J. et al. Global landscape of protein complexes in the yeast Saccharomyces cerevisiae. Nature 440, 637-643 (2006).
14. 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. USA 106, 1398-1403 (2009).
15. Lodish, H. F. & Jacobsen, M. Regulation of hemoglobin synthesis: equal rates of translation and termination of a-and b-globin chains. J. Biol. Chem. 247, 3622-3629 (1972).
16. 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).
17. Cao, J. & Geballe, A. P. Coding sequence-dependent ribosomal arrest at termination of translation. Mol. Cell. Biol. 16, 603-608 (1996).
18. Mateja, A. et al. The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461, 361-366 (2009).
19. Bozkurt, G. et al. Structural insights into tail-anchored protein binding and membrane insertion by Get3. Proc. Natl Acad. Sci. USA 106, 21131-21136 (2009).
20. 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. USA 106, 14849-14854 (2009).
21. Yamagata, A. et al. Structural insight into the membrane insertion of tail-anchored proteins by Get3. Genes Cells 15, 29-41 (2010).
22. 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 ONE 4, e8061 (2009).
23. 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).
24. Halic, M. et al. Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature 427, 808-814 (2004).
25. 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).
26. 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. USA 98, 3762-3767 (2001).
27. Kramer, G., Boehringer, D., Ban, N. & Bukau, B. The ribosome as a platform for cotranslational processing, folding and targeting of newly synthesized proteins. Nature Struct. Mol. Biol. 16, 589-597 (2009).
28. 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).
29. 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).
30. 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).