Ph.D.:	Hebrew University of Jerusalem, 2002
Phone:	Lab: +972-3-6409828 Fax: +972-3-6406834 Home: +972-77-426-0291
E-mail:	prag@post.tau.ac.il
Room#:	Sherman Building, 612
Lab Home Page:	*Lab Pages/*

Research Interests

Ubiquitylation and deubiquitylation are dynamic regulatory signals that can affect proteins activity, localization and fate. Ubiquitylated proteins are recognized by ubiquitin receptors that transmit the information conferred by the new structure of the ubiquitylated protein. Our lab is focused on the regulation of the ubiquitin signal in protein trafficking - especially in the endocytic and biosynthetic pathways. We are taking Structural, Biochemical and Biophysical approaches to understand the molecular mechanisms of ubiquitin recognition.

Full Publications

Prag G, Greenberg S, Oppenheim AB. Structural principles of prokaryotic gene regulatory proteins and the evolution of repressors and gene activators.
Mol Microbiol., (1997) 26, 619.

H. Giladi, S. Koby, G. Prag, M. Engelhorn, J. Geiselmann and A.B. Oppenheim. Participation of IHF and a distant UP element in the stimulation of the phage lambda PL promoter.
Mol Microbiol., (1998), 30, 443

G. Prag G, Y. Papanikolau, G. Tavlas, C.E. Vorgias, K. Petratos and A.B. Oppenheim. Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540.
J. Mol Biol., (2000), 300, 611.

Y. Papanikolau, G. Prag, G. Tavlas, C.E. Vorgias, A.B. Oppenheim and K. Petratos High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis
Biochemistry, (2001), 40,11338.

G. Prag and A.B. Oppenheim. Conservation of structural elements and catalytic mechanism in the chitinolytic enzymes from Serratia marcescens.
Chitin Enzymology, (2001), 3, 351.

S.C. Shih, G. Prag, S.A. Francis, M.A. Sutanto, J.H. Hurley and L. Hicke. A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain.
EMBO J., (2003), 22, 1273.

G. Prag, S. Misra, E.A. Jones, R. Ghirlando, B.A. Davies, B.F. Horazdovsky and J.H. Hurley. Mechanism of ubiquitin recognition by the CUE domain of Vps9p.
Cell, (2003), 113, 609.

A. Hierro, J. Sun, A.S. Rusnak, J. Kim, G. Prag, S.D. Emr and J.H. Hurley. Structure of the ESCRT-II endosomal trafficking complex
Nature, (2004), 431, 221.

G. Prag, S. Lee, R. Mattera, C.A. Arighi, B.M. Beach, J.S. Bonifacino, and J.H. Hurley. Structural mechanism for ubiquitinated cargo recognition by the GGA proteins
Proc. Natl. Acad. Sci. USA (2005), 102, 2334.

J.H. Hurley, S. Lee and G. Prag. Ubiquitin-binding domains
Biochemical Journal, (2006), 399, 361.

G. Prag, H. Watson, Y.C. Kim, B.M. Beach, R. Ghirlando, G. Hummer, J.S. Bonifacino, and J.H. Hurley. The Vps27/Hse1 complex is a GAT domain-based scaffold for ubiquitindependent sorting
Developmental Cell, (2007), 12, 973.