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Volumn 15, Issue 6, 2005, Pages 681-689

Membrane recruitment of effector proteins by Arf and Rab GTPases

Author keywords

[No Author keywords available]

Indexed keywords

ARF PROTEIN; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; PHOSPHODIESTERASE; PHOSPHODIESTERASE 6; PROTEIN SUBUNIT; RAB PROTEIN; UNCLASSIFIED DRUG;

EID: 27944510194     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.10.015     Document Type: Review
Times cited : (56)

References (36)
  • 1
    • 3142523461 scopus 로고    scopus 로고
    • COP and clathrin-coated vesicle budding: Different pathways, common approaches
    • H.T. McMahon, and I.G. Mills COP and clathrin-coated vesicle budding: different pathways, common approaches Curr Opin Cell Biol 16 2004 379 391
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 379-391
    • McMahon, H.T.1    Mills, I.G.2
  • 2
  • 4
    • 0035257013 scopus 로고    scopus 로고
    • Rab proteins as membrane organizers
    • M. Zerial, and H. McBride Rab proteins as membrane organizers Nat Rev Mol Cell Biol 2 2001 107 117
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 107-117
    • Zerial, M.1    McBride, H.2
  • 5
    • 1342289620 scopus 로고    scopus 로고
    • The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads
    • K. Nakayama, and S. Wakatsuki The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads Cell Struct Funct 28 2003 431 442
    • (2003) Cell Struct Funct , vol.28 , pp. 431-442
    • Nakayama, K.1    Wakatsuki, S.2
  • 6
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • J.S. Bonifacino The GGA proteins: adaptors on the move Nat Rev Mol Cell Biol 5 2004 23 32
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 7
    • 0037343940 scopus 로고    scopus 로고
    • The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs
    • B.M. Collins, P.J. Watson, and D.J. Owen The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs Dev Cell 4 2003 321 332 The authors report the crystal structure of the GGA1-GAT domain. It consists of four helices, which can be divided into two independent subdomains: N-terminal helix-loop-helix and C-terminal three-helix bundle. They propose a 'beads on a string' model for full-length GGA1. GGA1 could extend over 400 Å as a result of long random coils that loosely connect the folded domains (VHS, GAT and GAE).
    • (2003) Dev Cell , vol.4 , pp. 321-332
    • Collins, B.M.1    Watson, P.J.2    Owen, D.J.3
  • 9
    • 0037446843 scopus 로고    scopus 로고
    • Structure of the GAT domain of human GGA1: A syntaxin amino-terminal domain fold in an endosomal trafficking adaptor
    • S. Suer, S. Misra, L.F. Saidi, and J.H. Hurley Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor Proc Natl Acad Sci USA 100 2003 4451 4456
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 4451-4456
    • Suer, S.1    Misra, S.2    Saidi, L.F.3    Hurley, J.H.4
  • 10
    • 0037407395 scopus 로고    scopus 로고
    • Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport
    • T. Shiba, M. Kawasaki, H. Takatsu, T. Nogi, N. Matsugaki, N. Igarashi, M. Suzuki, R. Kato, K. Nakayama, and S. Wakatsuki Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport Nat Struct Biol 10 2003 386 393 This crystal structure of the free GGA1-GAT domain includes only the C-terminal three-helix bundle (C-GAT), whereas the N-terminal helix-loop-helix subdomain (N-GAT) is almost invisible. It was demonstrated that the helix-loop-helix structure of N-GAT is stabilized upon Arf•1GTP binding and the complex structure was determined.
    • (2003) Nat Struct Biol , vol.10 , pp. 386-393
    • Shiba, T.1    Kawasaki, M.2    Takatsu, H.3    Nogi, T.4    Matsugaki, N.5    Igarashi, N.6    Suzuki, M.7    Kato, R.8    Nakayama, K.9    Wakatsuki, S.10
  • 11
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human ARF6-GTP
    • C.J. O'Neal, M.G. Jobling, R.K. Holmes, and W.G. Hol Structural basis for the activation of cholera toxin by human ARF6-GTP Science 309 2005 1093 1096
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'Neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.G.4
  • 13
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • B. Short, A. Haas, and F.A. Barr Golgins and GTPases, giving identity and structure to the Golgi apparatus Biochim Biophys Acta 1744 2005 383 395
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 14
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
    • B. Panic, O. Perisic, D.B. Veprintsev, R.L. Williams, and S. Munro Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus Mol Cell 12 2003 863 874 This structure provides the first example of the dyad-symmetrical interaction of a small GTPase with its effector. The authors point out that Tyr2177 of the golgin-245 GRIP domain, which interacts with the switch and interswitch regions of Arl1•GTP, is an important determinant of binding specificity. Their insightful schematic diagram of the interaction between effectors and switch regions prompted us to review all reported Arf/Rab-effector interactions.
    • (2003) Mol Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3    Williams, R.L.4    Munro, S.5
  • 15
    • 0842269776 scopus 로고    scopus 로고
    • Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1
    • M. Wu, L. Lu, W. Hong, and H. Song Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1 Nat Struct Mol Biol 11 2004 86 94
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 86-94
    • Wu, M.1    Lu, L.2    Hong, W.3    Song, H.4
  • 18
    • 4744369353 scopus 로고    scopus 로고
    • Structural basis of Rab5-Rabaptin5 interaction in endocytosis
    • G. Zhu, P. Zhai, J. Liu, S. Terzyan, G. Li, and X.C. Zhang Structural basis of Rab5-Rabaptin5 interaction in endocytosis Nat Struct Mol Biol 11 2004 975 983 Rabaptin-5 is a bivalent Rab effector that binds to Rab4 through its N terminus and to Rab5 through its C terminus. The authors revealed that the C-terminal Rab5-binding domain forms a coiled-coil homodimer, with two Rab5 molecules binding independently on either side. Dimerization of Rabaptin-5 is essential for Rab5 binding, because Rab5 interacts with both protomers of the Rabaptin-5 homodimer
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 975-983
    • Zhu, G.1    Zhai, P.2    Liu, J.3    Terzyan, S.4    Li, G.5    Zhang, X.C.6
  • 19
    • 18444381428 scopus 로고    scopus 로고
    • Structural basis for recruitment of RILP by small GTPase Rab7
    • M. Wu, T. Wang, E. Loh, W. Hong, and H. Song Structural basis for recruitment of RILP by small GTPase Rab7 EMBO J 24 2005 1491 1501 The Rab7-binding domain of RILP forms a homodimer, with each protomer adopting a helix-loop-helix structure. Two Rab7 molecules symmetrically interact with both protomers. The interaction is mediated not only by the switch and interswitch regions, but also by the hypervariable RabSF1 and RabSF4 regions.
    • (2005) EMBO J , vol.24 , pp. 1491-1501
    • Wu, M.1    Wang, T.2    Loh, E.3    Hong, W.4    Song, H.5
  • 20
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • C. Ostermeier, and A.T. Brunger Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A Cell 96 1999 363 374
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 21
    • 22944444569 scopus 로고    scopus 로고
    • Structural basis of family-wide Rab GTPase recognition by rabenosyn-5
    • S. Eathiraj, X. Pan, C. Ritacco, and D.G. Lambright Structural basis of family-wide Rab GTPase recognition by rabenosyn-5 Nature 436 2005 415 419 In this recent tour de force, the authors determined crystal structures of eight Rabs bound to GppNHp (Ypt1, Rab4A, Rab6A, Rab9, Rab11A, Rab21, Rab22A and Rab33) and five Rabs bound to GDP (Rab2A, Rab5C, Rab14, Rab21 and Rab23). To assess the different specificities of rabenosyn-5 for individual Rabs, they determined the structure of the Rab4-rabenosyn-5(440-503) and Rab22-rabenosyn-5(728-784) complexes. The structures revealed highly selective recognition by structurally similar effector regions
    • (2005) Nature , vol.436 , pp. 415-419
    • Eathiraj, S.1    Pan, X.2    Ritacco, C.3    Lambright, D.G.4
  • 22
    • 0036172652 scopus 로고    scopus 로고
    • Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes
    • S. de Renzis, B. Sonnichsen, and M. Zerial Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes Nat Cell Biol 4 2002 124 133
    • (2002) Nat Cell Biol , vol.4 , pp. 124-133
    • De Renzis, S.1    Sonnichsen, B.2    Zerial, M.3
  • 24
    • 0038299239 scopus 로고    scopus 로고
    • Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout
    • G.R. Hickson, J. Matheson, B. Riggs, V.H. Maier, A.B. Fielding, R. Prekeris, W. Sullivan, F.A. Barr, and G.W. Gould Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout Mol Biol Cell 14 2003 2908 2920
    • (2003) Mol Biol Cell , vol.14 , pp. 2908-2920
    • Hickson, G.R.1    Matheson, J.2    Riggs, B.3    Maier, V.H.4    Fielding, A.B.5    Prekeris, R.6    Sullivan, W.7    Barr, F.A.8    Gould, G.W.9
  • 25
    • 0037413690 scopus 로고    scopus 로고
    • Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex
    • R. Mattera, C.N. Arighi, R. Lodge, M. Zerial, and J.S. Bonifacino Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex EMBO J 22 2003 78 88
    • (2003) EMBO J , vol.22 , pp. 78-88
    • Mattera, R.1    Arighi, C.N.2    Lodge, R.3    Zerial, M.4    Bonifacino, J.S.5
  • 26
    • 8144231396 scopus 로고    scopus 로고
    • Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5
    • G. Zhu, P. Zhai, X. He, N. Wakeham, K. Rodgers, G. Li, J. Tang, and X.C. Zhang Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5 EMBO J 23 2004 3909 3917 The GAT-binding domain of Rabaptin-5 is a 90-residue single helix that forms a parallel coiled-coil homodimer. The GGA1-GAT domain 'asymmetrically' binds to one side of the N terminus of the Rabaptin-5 homodimer, in contrast to the dyad-symmetrical binding of two Rab5 molecules to the C-terminal end of the Rabaptin-5 homodimer. The two homodimers of the GAT-binding domain of Rabaptin-5 unexpectedly formed a homotetramer at their C termini.
    • (2004) EMBO J , vol.23 , pp. 3909-3917
    • Zhu, G.1    Zhai, P.2    He, X.3    Wakeham, N.4    Rodgers, K.5    Li, G.6    Tang, J.7    Zhang, X.C.8
  • 28
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • R. Puertollano, and J.S. Bonifacino Interactions of GGA3 with the ubiquitin sorting machinery Nat Cell Biol 6 2004 244 251
    • (2004) Nat Cell Biol , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 30
    • 14044278879 scopus 로고    scopus 로고
    • Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins
    • G. Prag, S. Lee, R. Mattera, C.N. Arighi, B.M. Beach, J.S. Bonifacino, and J.H. Hurley Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, γ-ear-containing, ADP-ribosylation-factor-binding proteins Proc Natl Acad Sci USA 102 2005 2334 2339
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2334-2339
    • Prag, G.1    Lee, S.2    Mattera, R.3    Arighi, C.N.4    Beach, B.M.5    Bonifacino, J.S.6    Hurley, J.H.7
  • 34
    • 0042991385 scopus 로고    scopus 로고
    • Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3
    • G.J. Miller, R. Mattera, J.S. Bonifacino, and J.H. Hurley Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3 Nat Struct Biol 10 2003 599 606 In contrast to the ear domains of α-adaptin and β2-adaptin of the AP2 complex, which are composed of two subdomains (the platform and the β sandwich), the GAE (β-adaptin ear) domain consists solely of the β-sandwich domain. GGA-GAE interacts with various accessory proteins, including Rabaptin-5, in a different manner to the α and β2 ears.
    • (2003) Nat Struct Biol , vol.10 , pp. 599-606
    • Miller, G.J.1    Mattera, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 35
    • 0041989753 scopus 로고    scopus 로고
    • Structural basis for binding of accessory proteins by the appendage domain of GGAs
    • B.M. Collins, G.J. Praefcke, M.S. Robinson, and D.J. Owen Structural basis for binding of accessory proteins by the appendage domain of GGAs Nat Struct Biol 10 2003 607 613
    • (2003) Nat Struct Biol , vol.10 , pp. 607-613
    • Collins, B.M.1    Praefcke, G.J.2    Robinson, M.S.3    Owen, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.