Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes (original) (raw)

References

1. Pfeffer, S.R. Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol. 11, 487–491 (2001).
   Article CAS PubMed Google Scholar
2. Zerial, M. & McBride, H. Rab proteins as membrane organizers. Nat. Rev. Mol. Cell Biol. 2, 107–117 (2001).
   Article CAS PubMed Google Scholar
3. Anant, J.S. et al. Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex. Biochemistry 37, 12559–12568 (1998).
   Article CAS PubMed Google Scholar
4. Goldberg, J. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95, 237–248 (1998).
   Article CAS PubMed Google Scholar
5. Goody, R.S., Rak, A. & Alexandrov, K. The structural and mechanistic basis for recycling of Rab proteins between membrane compartments. Cell. Mol. Life Sci. 62, 1657–1670 (2005).
   Article CAS PubMed Google Scholar
6. Rak, A. et al. Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 302, 646–650 (2003).
   Article CAS PubMed Google Scholar
7. Wu, Y.W., Tan, K.T., Waldmann, H., Goody, R.S. & Alexandrov, K. Interaction analysis of prenylated Rab GTPase with Rab escort protein and GDP dissociation inhibitor explains the need for both regulators. Proc. Natl. Acad. Sci. USA 104, 12294–12299 (2007).
   Article CAS PubMed PubMed Central Google Scholar
8. Sivars, U., Aivazian, D. & Pfeffer, S.R. Yip3 catalyses the dissociation of endosomal Rab-GDI complexes. Nature 425, 856–859 (2003).
   Article CAS PubMed Google Scholar
9. Sivars, U., Aivazian, D. & Pfeffer, S. Purification and properties of Yip3-PRA1 as a Rab GDI displacement factor. Methods Enzymol. 403, 348–356 (2005).
   Article CAS PubMed Google Scholar
10. Figueroa, C., Taylor, J. & Vojtek, A.B. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J. Biol. Chem. 276, 28219–28225 (2001).
    Article CAS PubMed Google Scholar
11. Seabra, M.C. Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab. J. Biol. Chem. 271, 14398–14404 (1996).
    Article CAS PubMed Google Scholar
12. Kalinin, A. et al. Expression of mammalian geranylgeranyltransferase type-II in Escherichia coli and its application for in vitro prenylation of Rab proteins. Protein Expr. Purif. 22, 84–91 (2001).
    Article CAS PubMed Google Scholar
13. Shapiro, A.D. & Pfeffer, S.R. Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides. J. Biol. Chem. 270, 11085–11090 (1995).
    Article CAS PubMed Google Scholar
14. Muir, T.W. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72, 249–289 (2003).
    Article CAS PubMed Google Scholar
15. Gitler, C., Zarmi, B. & Kalef, E. Use of cationic detergents to enhance reactivity of protein sulfhydryls. Methods Enzymol. 251, 366–375 (1995).
    Article CAS PubMed Google Scholar
16. Sanford, J.C., Pan, Y. & Wessling-Resnick, M. Prenylation of Rab5 is dependent on guanine nucleotide binding. J. Biol. Chem. 268, 23773–23776 (1993).
    CAS PubMed Google Scholar
17. Seabra, M.C. Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab. J. Biol. Chem. 271, 14398–14404 (1996).
    Article CAS PubMed Google Scholar
18. Machner, M.P. & Isberg, R.R. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318, 974–977 (2007).
    Article CAS PubMed Google Scholar
19. Ingmundson, A., Delprato, A., Lambright, D.G. & Roy, C.R. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450, 365–369 (2007).
    Article CAS PubMed Google Scholar
20. Schoebel, S., Oesterlin, L.K., Blankenfeldt, W., Goody, R.S. & Itzen, A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol. Cell 36, 1060–1072 (2009).
    Article CAS PubMed Google Scholar
21. Dursina, B.E. et al. A genetically encodable microtag for chemoenzymatic derivatization and purification of recombinant proteins. Protein Expr. Purif. 39, 71–81 (2005).
    Article CAS PubMed Google Scholar
22. Alexandrov, K. et al. Moderate discrimination of REP-1 between Rab7 x GDP and Rab7 x GTP arises from a difference of an order of magnitude in dissociation rates. FEBS Lett. 425, 460–464 (1998).
    Article CAS PubMed Google Scholar
23. Chavrier, P. et al. Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 353, 769–772 (1991).
    Article CAS PubMed Google Scholar
24. Ali, B.R., Wasmeier, C., Lamoreux, L., Strom, M. & Seabra, M.C. Multiple regions contribute to membrane targeting of Rab GTPases. J. Cell Sci. 117, 6401–6412 (2004).
    Article CAS PubMed Google Scholar
25. Ali, B.R. & Seabra, M.C. Targeting of Rab GTPases to cellular membranes. Biochem. Soc. Trans. 33, 652–656 (2005).
    Article CAS PubMed Google Scholar
26. Beranger, F., Paterson, H., Powers, S., de Gunzburg, J. & Hancock, J.F. The effector domain of Rab6, plus a highly hydrophobic C terminus, is required for Golgi apparatus localization. Mol. Cell. Biol. 14, 744–758 (1994).
    Article CAS PubMed PubMed Central Google Scholar
27. Hutt, D.M., Da-Silva, L.F., Chang, L.H., Prosser, D.C. & Ngsee, J.K. PRA1 inhibits the extraction of membrane-bound Rab GTPase by GDI1. J. Biol. Chem. 275, 18511–18519 (2000).
    Article CAS PubMed Google Scholar
28. Soldati, T., Shapiro, A.D., Svejstrup, A.B. & Pfeffer, S.R. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 369, 76–78 (1994).
    Article CAS PubMed Google Scholar
29. Ullrich, O., Horiuchi, H., Bucci, C. & Zerial, M. Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange. Nature 368, 157–160 (1994).
    Article CAS PubMed Google Scholar
30. Pylypenko, O. et al. Structure of doubly prenylated Ypt1-GDI complex and the mechanism of GDI-mediated Rab recycling. EMBO J. 25, 13–23 (2006).
    Article CAS PubMed PubMed Central Google Scholar
31. Sato, Y., Fukai, S., Ishitani, R. & Nureki, O. Crystal structure of the Sec4p.Sec2p complex in the nucleotide exchanging intermediate state. Proc. Natl. Acad. Sci. USA 104, 8305–8310 (2007).
    Article CAS PubMed PubMed Central Google Scholar
32. Lippé, R., Miaczynska, M., Rybin, V., Runge, A. & Zerial, M. Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex. Mol. Biol. Cell 12, 2219–2228 (2001).
    Article PubMed PubMed Central Google Scholar
33. Mattera, R. & Bonifacino, J.S. Ubiquitin binding and conjugation regulate the recruitment of Rabex-5 to early endosomes. EMBO J. 27, 2484–2494 (2008).
    Article CAS PubMed PubMed Central Google Scholar
34. Zhu, H. et al. Rabaptin-5-independent membrane targeting and Rab5 activation by Rabex-5 in the cell. Mol. Biol. Cell 18, 4119–4128 (2007).
    Article CAS PubMed PubMed Central Google Scholar
35. Durek, T. et al. Synthesis of fluorescently labeled mono- and diprenylated Rab7 GTPase. J. Am. Chem. Soc. 126, 16368–16378 (2004).
    Article CAS PubMed Google Scholar
36. Wu, Y.W. et al. A protein fluorescence amplifier: continuous fluorometric assay for rab geranylgeranyltransferase. Chembiochem. 7, 1859–1861 (2006).
    Article CAS PubMed Google Scholar

Download references