Organization and Function of the Rab Prenylation and Recycling Machinery

Enzymes

Volumn 29, Issue , 2011, Pages 147-162

  Alexandrov, Kirill ^a   Wu, Yaowen ^b   Blankenfeldt, Wulf ^c   Waldmann, Herbert ^b   Goody, Roger S ^b  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^c UNIVERSITY OF BAYREUTH   (Germany)

Author keywords

Guanine nucleotide exchange factor; Protein prenylation; Protein prenyltransferases; RabGTPases

Indexed keywords

EID: 79960241386     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-381339-8.00008-1     Document Type: Chapter

References (43)

1. Brighouse A., Dacks J.B., Field M.C. Rab protein evolution and the history of the eukaryotic endomembrane system. Cell Mol Life Sci 2010, 67:3449-3465.
2. Nguyen U.T., Goody R.S., Alexandrov K. Understanding and exploiting protein prenyltransferases. Chembiochem 2010, 11:1194-1201.
3. Seabra M.C., Mules E.H., Hume A.N. Rab GTPases, intracellular traffic and disease. Trends Mol Med 2002, 8:23-30.
4. Anant J.S., et al. Mechanism of Rab geranylgeranylation: formation of the catalytic ternary complex. Biochemistry 1998, 37:12559-12568.
5. Wu Y.W., Goody R.S., Abagyan R., Alexandrov K. Structure of the disordered C terminus of Rab7 GTPase induced by binding to the Rab geranylgeranyl transferase catalytic complex reveals the mechanism of Rab prenylation. J Biol Chem 2009, 284:13185-13192.
6. Thoma N.H., Iakovenko A., Kalinin A., Waldmann H., Goody R.S., Alexandrov K. Allosteric regulation of substrate binding and product release in geranylgeranyltransferase type II. Biochemistry 2001, 40:268-274.
7. Baron R.A., Seabra M.C. Rab geranylgeranylation occurs preferentially via the pre-formed REP-RGGT complex and is regulated by geranylgeranyl pyrophosphate. Biochem J 2008, 415:67-75.
8. Rak A., Pylypenko O., Niculae A., Pyatkov K., Goody R.S., Alexandrov K. Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease. Cell 2004, 117:749-760.
9. Pylypenko O., et al. Structure of rab escort protein-1 in complex with rab geranylgeranyltransferase. MolCell 2003, 11:483-494.
10. Guo Z., et al. Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation. EMBO J 2008, 27:2444-2456.
11. Zhang H., Seabra M.C., Deisenhofer J. Crystal structure of Rab geranylgeranyltransferase at 2.0Å resolution. Structure 2000, 8:241-251.
12. Goody R.S., Rak A., Alexandrov K. The structural and mechanistic basis for recycling of Rab proteins between membrane compartments. Cell Mol Life Sci 2005, 62:1657-1670.
13. Alexandrov K., Simon I., Iakovenko A., Holz B., Goody R.S., Scheidig A.J. Moderate discrimination of REP-1 between Rab7×GDP and Rab7×GTP arises from a difference of an order of magnitude in dissociation rates. FEBS Lett 1998, 425:460-464.
14. Seabra M.C. Nucleotide dependence of Rab geranylgeranylation. Rab escort protein interacts preferentially with GDP-bound Rab. J Biol Chem 1996, 271:14398-14404.
15. Wu Y.W., Oesterlin L.K., Tan K.T., Waldmann H., Alexandrov K., Goody R.S. Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes. Nat Chem Biol 2010, 6:534-540.
16. Guo Z., et al. Development of selective RabGGTase inhibitors and crystal structure of a RabGGTase-inhibitor complex. Angew Chem Int Ed Engl 2008, 47:3747-3750.
17. Thoma N.H., Niculae A., Goody R.S., Alexandrov K. Double prenylation by RabGGTase can proceed without dissociation of the mono-prenylated intermediate. J Biol Chem 2001, 276:48631-48636.
18. Alexandrov K., Horiuchi H., Steele-Mortimer O., Seabra M.C., Zerial M. Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J 1994, 13:5262-5273.
19. Rak A., et al. Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 2003, 302:646-650.
20. 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 2007, 104:12294-12299.
21. Ignatev A., Kravchenko S., Rak A., Goody R.S., Pylypenko O. A structural model of the GDP dissociation inhibitor rab membrane extraction mechanism. J Biol Chem 2008, 283:18377-18384.
22. Luan P., Balch W.E., Emr S.D., Burd C.G. Molecular dissection of guanine nucleotide dissociation inhibitor function in vivo. Rab-independent binding to membranes and role of Rab recycling factors. J Biol Chem 1999, 274:14806-14817.
23. Schalk I., et al. Structure and mutational analysis of Rab GDP-dissociation inhibitor. Nature 1996, 381:42-48.
24. Pylypenko O., et al. Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling. EMBO J 2006, 25:13-23.
25. Shen F., Seabra M.C. Mechanism of digeranylgeranylation of Rab proteins. Formation of a complex between monogeranylgeranyl-Rab and Rab escort protein. J Biol Chem 1996, 271:3692-3698.
26. Luan P., et al. A new functional domain of guanine nucleotide dissociation inhibitor (alpha-GDI) involved in Rab recycling. Traffic 2000, 1:270-281.
27. Chavrier P., Gorvel J.P., Stelzer E., Simons K., Gruenberg J., Zerial M. Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 1991, 353:769-772.
28. Ali B.R., Wasmeier C., Lamoreux L., Strom M., Seabra M.C. Multiple regions contribute to membrane targeting of Rab GTPases. J Cell Sci 2004, 117:6401-6412.
29. Aivazian D., Serrano R.L., Pfeffer S. TIP47 is a key effector for Rab9 localization. J Cell Biol 2006, 173:917-926.
30. Sivars U., Aivazian D., Pfeffer S. Purification and properties of Yip3/PRA1 as a Rab GDI displacement factor. Methods Enzymol 2005, 403:348-356.
31. Sivars U., Aivazian D., Pfeffer S.R. Yip3 catalyses the dissociation of endosomal Rab-GDI complexes. Nature 2003, 425(6960):856-859.
32. Figueroa C., Taylor J., Vojtek A.B. Prenylated Rab acceptor protein is a receptor for prenylated small GTPases. J Biol Chem 2001, 276:28219-28225.
33. Soldati T., Shapiro A.D., Svejstrup A.B., Pfeffer S.R. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 1994, 369:76-78.
34. Ullrich O., Horiuchi H., Bucci C., Zerial M. Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange. Nature 1994, 368:157-160.
35. Ingmundson A., Delprato A., Lambright D.G., Roy C.R. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 2007, 450:365-369.
36. Machner M.P., Isberg R.R. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 2007, 318:974-977.
37. 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 2009, 36:1060-1072.
38. D'Adamo P., et al. Mutations in GDI1 are responsible for X-linked non-specific mental retardation. Nat Genet 1998, 19:134-139.
39. Seabra M.C. New insights into the pathogenesis of choroideremia: a tale of two REPs. Ophthalmic Genet 1996, 17:43-46.
40. Seabra M.C., Ho Y.K., Anant J.S. Deficient geranylgeranylation of Ram/Rab27 in choroideremia. J Biol Chem 1995, 270:24420-24427.
41. Larijani B., Hume A.N., Tarafder A.K., Seabra M.C. Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases. J Biol Chem 2003, 278:46798-46804.
42. Strunnikova N.V., et al. Loss-of-function mutations in Rab escort protein 1 (REP-1) affect intracellular transport in fibroblasts and monocytes of choroideremia patients. PLoS ONE 2009, 4:e8402.
43. Dacks J.B., Field M.C. Evolution of the eukaryotic membrane-trafficking system: origin, tempo and mode. J Cell Sci 2007, 120:2977-2985.