TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism

Nature

Volumn 442, Issue 7100, 2006, Pages 303-306

  Pan, Xiaojing ^a   Eathiraj, Sudharshan ^a   Munson, Mary ^a   Lambright, David G ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CONFORMATIONS; CRYSTALLOGRAPHY; FUNCTIONAL ASSESSMENT; HYDROLYSIS; MUTAGENESIS; PHOSPHATES;

DUAL-FINGER MECHANISM; RAB GTPASES; TBC-DOMAIN GAPS; TRANSITION STATE;

ENZYMES;

ALUMINUM FLUORIDE; GLUTAMINE; GUANOSINE TRIPHOSPHATASE;

AMINO ACID; ENZYME ACTIVITY; EUKARYOTE; HYDROLYSIS; MEMBRANE; PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; CYTOKINESIS; ENZYME ACTIVATION; ENZYME ACTIVITY; EUKARYOTE; GENE FUNCTION; GENE MUTATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; YEAST;

EUKARYOTA;

EID: 33746356908     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04847     Document Type: Article

References (30)

1. Segev, N. Ypt/Rab GTPases: regulators of protein trafficking. Sci. STKE 2001, RE11 (2001).
2. Bernards, A. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim. Biophys. Acta 1603, 47-82 (2003).
3. Albert, S., Will, E. & Gallwitz, D. Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase-activating proteins specific for Ypt/Rab transport GTPases. EMBO J. 18, 5216-5225 (1999).
4. Rak, A. et al. Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins. EMBO J. 19, 5105-5113 (2000).
5. Du, L. L. & Novick, P. Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p. Mol. Biol. Cell 12, 1215-1226 (2001).
6. Strom, M., Vollmer, P., Tan, T. J. & Gallwitz, D. A yeast GTPase-activating protein that interacts specifically with a member of the Ypt/Rab family. Nature 361, 736-739 (1993).
7. Du, L. L., Collins, R. N. & Novick, P. J. Identification of a Sec4p GTPase-activating protein (GAP) as a novel member of a Rab GAP family. J. Biol. Chem. 273, 3253-3256 (1998).
8. Albert, S. & Gallwitz, D. Two new members of a family of Ypt/Rab GTPase activating proteins. Promiscuity of substrate recognition. J. Biol. Chem. 274, 33186-33189 (1999).
9. Cuif, M. H. et al. Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome. EMBO J. 18, 1772-1782 (1999).
10. Vollmer, P., Will, E., Scheglmann, D., Strom, M. & Gallwitz, D. Primary structure and biochemical characterization of yeast GTPase-activating proteins with substrate preference for the transport GTPase Ypt7p. Eur. J. Biochem. 260, 284-290 (1999).
11. Lanzetti, L. et al. The Eps8 protein coordinates EGF receptor signalling through Rac and trafficking through Rab5. Nature 408, 374-377 (2000).
12. Will, E. & Gallwitz, D. Biochemical characterization of Gyp6p, a Ypt/Rab-specific GTPase-activating protein from yeast. J. Biol. Chem. 276, 12135-12139 (2001).
13. Gao, X. D. et al. The GAP activity of Msb3p and Msb4p for the Rab GTPase Sec4p is required for efficient exocytosis and actin organization. J. Cell Biol. 162, 635-646 (2003).
14. Haas, A. K., Fuchs, E., Kopajtich, R. & Barr, F. A. A. GTPase-activating protein controls Rab5 function in endocytic trafficking. Nature Cell Biol. 7, 887-893 (2005).
15. Miinea, C. P. et al. AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain. Biochem. J. 391, 87-93 (2005).
16. Lafourcade, C., Galan, J. M., Gloor, Y., Haguenauer-Tsapis, R. & Peter, M. The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p. Mol. Cell. Biol. 24, 3815-3826 (2004).
17. Segev, N., Mulholland, J. & Botstein, D. The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery. Cell 52, 915-924 (1988).
18. Saraste, J., Lahtinen, U. & Goud, B. Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway. J. Cell Sci. 108, 1541-1552 (1995).
19. Zheng, J. Y. et al. A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae. J. Cell Sci. 111, 1061-1069 (1998).
20. -. Nature 372, 276-279 (1994).
21. iα1 and the mechanism of GTP hydrolysis. Science 265, 1405-1412 (1994).
22. Mittal, R., Ahmadian, M. R., Goody, R. S. & Wittinghofer, A. Formation of a transition-state analog of the Ras GTPase reaction by Ras-GDP, tetrafluoroaluminate, and GTPase-activating proteins. Science 273, 115-117 (1996).
23. Scheffzek, K. et al. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 277, 333-338 (1997).
24. Rittinger, K., Walker, P. A., Eccleston, J. F., Smerdon, S. J. & Gamblin, S. J. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Nature 389, 758-762 (1997).
25. Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C. & Cerione, R. A. Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP. Nature Struct. Biol. 5, 1047-1052 (1998).
26. iα1: stabilization of the transition state for GTP hydrolysis. Cell 89, 251-261 (1997).
27. Slep, K. C. et al. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 409, 1071-1077 (2001).
28. Daumke, O., Weyand, M., Chakrabarti, P. P., Vetter, I. R. & Wittinghofer, A. The GTPase-activating protein Rap1GAP uses a catalytic asparagine. Nature 429, 197-201 (2004).
29. Eathiraj, S., Pan, X., Ritacco, C. & Lambright, D. G. Structural basis of family-wide Rab GTPase recognition by rabenosyn-5. Nature 436, 415-419 (2005).
30. De Antoni, A., Schmitzova, J., Trepte, H. H., Gallwitz, D. & Albert, S. Significance of GTP hydrolysis in Ypt1p-regulated endoplasmic reticulum to Golgi transport revealed by the analysis of two novel Ypt1-GAPs. J. Biol. Chem. 277, 41023-41031 (2002).