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Volumn 23, Issue 20, 2004, Pages 3909-3917

Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5

Author keywords

Crystal structure; GAT domain; GGA proteins; Intracellular trafficking; Rabaptin5

Indexed keywords

ARF PROTEIN; CARRIER PROTEIN; PROTEIN GGA1; RAB PROTEIN; RABAPTIN5; TETRAMER; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 8144231396     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600411     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 0034752915 scopus 로고    scopus 로고
    • GGA proteins: New players in the sorting game
    • Boman AL (2001) GGA proteins: new players in the sorting game. J Cell Sci 114: 3413-3418
    • (2001) J Cell Sci , vol.114 , pp. 3413-3418
    • Boman, A.L.1
  • 2
    • 0034036097 scopus 로고    scopus 로고
    • A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi
    • Boman AL, Zhang C, Zhu X, Kahn RA (2000) A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi. Mol Biol Cell 11: 1241-1255
    • (2000) Mol Biol Cell , vol.11 , pp. 1241-1255
    • Boman, A.L.1    Zhang, C.2    Zhu, X.3    Kahn, R.A.4
  • 4
    • 0037343940 scopus 로고    scopus 로고
    • The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs
    • Collins BM, Watson PJ, Owen DJ (2003) The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs. Dev Cell 4: 321-332
    • (2003) Dev Cell , vol.4 , pp. 321-332
    • Collins, B.M.1    Watson, P.J.2    Owen, D.J.3
  • 7
    • 0032036435 scopus 로고    scopus 로고
    • Two distinct effectors of the small GTPase Rab5 cooperate in endocytic membrane fusion
    • Gournier H, Stenmark H, Rybin V, Lippe R, Zerial M (1998) Two distinct effectors of the small GTPase Rab5 cooperate in endocytic membrane fusion. EMBO J 17: 1930-1940
    • (1998) EMBO J , vol.17 , pp. 1930-1940
    • Gournier, H.1    Stenmark, H.2    Rybin, V.3    Lippe, R.4    Zerial, M.5
  • 8
    • 0034599537 scopus 로고    scopus 로고
    • A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome
    • Hirst J, Lui WW, Bright NA, Totty N, Seaman MN, Robinson MS (2000) A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome. J Cell Biol 149: 67-80
    • (2000) J Cell Biol , vol.149 , pp. 67-80
    • Hirst, J.1    Lui, W.W.2    Bright, N.A.3    Totty, N.4    Seaman, M.N.5    Robinson, M.S.6
  • 10
    • 0037067227 scopus 로고    scopus 로고
    • Multiple Rabaptin-5-like transcripts
    • Korobko EV, Kiselev SL, Korobko IV (2002) Multiple Rabaptin-5-like transcripts. Gene 292: 191-197
    • (2002) Gene , vol.292 , pp. 191-197
    • Korobko, E.V.1    Kiselev, S.L.2    Korobko, I.V.3
  • 11
    • 0024574171 scopus 로고
    • Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen
    • Lin XL, Wong RN, Tang J (1989) Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen. J Biol Chem 264: 4482-4489
    • (1989) J Biol Chem , vol.264 , pp. 4482-4489
    • Lin, X.L.1    Wong, R.N.2    Tang, J.3
  • 12
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas A (1996) Coiled coils: new structures and new functions. Trends Biochem Sci 21: 375-382
    • (1996) Trends Biochem Sci , vol.21 , pp. 375-382
    • Lupas, A.1
  • 13
    • 0037413690 scopus 로고    scopus 로고
    • Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex
    • Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (2003) Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex. EMBO J 22: 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
  • 14
    • 3843118843 scopus 로고    scopus 로고
    • The tri-helical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites
    • Mattera R, Puertollano R, Smith WJ, Bonifacino JS (2004) The tri-helical bundle subdomain of the GGA proteins interacts with multiple partners through overlapping but distinct sites. J Biol Chem 279: 31409-31418
    • (2004) J Biol Chem , vol.279 , pp. 31409-31418
    • Mattera, R.1    Puertollano, R.2    Smith, W.J.3    Bonifacino, J.S.4
  • 15
    • 0042991385 scopus 로고    scopus 로고
    • Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3
    • Miller GJ, Mattera R, Bonifacino JS, Hurley JH (2003) Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3. Nat Struct Biol 10: 599-606
    • (2003) Nat Struct Biol , vol.10 , pp. 599-606
    • Miller, G.J.1    Mattera, R.2    Bonifacino, J.S.3    Hurley, J.H.4
  • 16
    • 0032555493 scopus 로고    scopus 로고
    • Molecules in the ARF orbit
    • Moss J, Vaughan M (1998) Molecules in the ARF orbit. J Biol Chem 273: 21431-21434
    • (1998) J Biol Chem , vol.273 , pp. 21431-21434
    • Moss, J.1    Vaughan, M.2
  • 17
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren IM, Thornton JM (2003) Diversity of protein-protein interactions. EMBO J 22: 3486-3492
    • (2003) EMBO J , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 0034629469 scopus 로고    scopus 로고
    • Vear, a novel Golgi-associated protein with VHS and gamma-adaptin 'ear' domains
    • Poussu A, Lohi O, Lento VP (2000) Vear, a novel Golgi-associated protein with VHS and gamma-adaptin 'ear' domains. J Biol Chem 275: 7176-7183
    • (2000) J Biol Chem , vol.275 , pp. 7176-7183
    • Poussu, A.1    Lohi, O.2    Lento, V.P.3
  • 21
    • 1542714469 scopus 로고    scopus 로고
    • Interactions of GGA3 with the ubiquitin sorting machinery
    • Puertollano R, Bonifacino JS (2004) Interactions of GGA3 with the ubiquitin sorting machinery. Nat Cell Biol 6: 244-251
    • (2004) Nat Cell Biol , vol.6 , pp. 244-251
    • Puertollano, R.1    Bonifacino, J.S.2
  • 24
    • 0036479314 scopus 로고    scopus 로고
    • A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5
    • Saito K, Murai J, Kajiho H, Kontani K, Kurosu H, Katada T (2002) A novel binding protein composed of homophilic tetramer exhibits unique properties for the small GTPase Rab5. J Biol Chem 277: 3412-3418
    • (2002) J Biol Chem , vol.277 , pp. 3412-3418
    • Saito, K.1    Murai, J.2    Kajiho, H.3    Kontani, K.4    Kurosu, H.5    Katada, T.6
  • 28
    • 0036221890 scopus 로고    scopus 로고
    • gamma-Adaptin interacts directly with Rabaptin-5 through its ear domain
    • Shiba Y, Takatsu H, Shin HW, Nakayama K (2002) gamma-Adaptin interacts directly with Rabaptin-5 through its ear domain. J Biochem (Tokyo) 131: 327-336
    • (2002) J Biochem (Tokyo) , vol.131 , pp. 327-336
    • Shiba, Y.1    Takatsu, H.2    Shin, H.W.3    Nakayama, K.4
  • 29
    • 0028791634 scopus 로고
    • Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion
    • Stenmark H, Vitale G, Ullrich O, Zerial M (1995) Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 83: 423-432
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 30
    • 0037446843 scopus 로고    scopus 로고
    • Structure of the GAT domain of human GGA1: A syntaxin amino-terminal domain fold in an endosomal trafficking adaptor
    • Suer S, Misra S, Saidi LF, Hurley JH (2003) 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: 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
  • 31
    • 0034685644 scopus 로고    scopus 로고
    • Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin
    • Takatsu H, Yoshino K, Nakayama K (2000) Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin. Biochem Biophys Res Commun 271: 719-725
    • (2000) Biochem Biophys Res Commun , vol.271 , pp. 719-725
    • Takatsu, H.1    Yoshino, K.2    Nakayama, K.3
  • 32
    • 0037101770 scopus 로고    scopus 로고
    • GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors
    • Takatsu H, Yoshino K, Toda K, Nakayama K (2002) GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. Biochem J 365: 369-378
    • (2002) Biochem J , vol.365 , pp. 369-378
    • Takatsu, H.1    Yoshino, K.2    Toda, K.3    Nakayama, K.4
  • 35
    • 0344844494 scopus 로고    scopus 로고
    • The interaction of the human GGA1 GAT domain with Rabaptin-5 is mediated by residues on its three-helix bundle
    • Zhai P, He X, Liu J, Wakeham N, Zhu G, Li G, Tang J, Zhang XC (2003) The interaction of the human GGA1 GAT domain with Rabaptin-5 is mediated by residues on its three-helix bundle. Biochemistry 42: 13901-13908
    • (2003) Biochemistry , vol.42 , pp. 13901-13908
    • Zhai, P.1    He, X.2    Liu, J.3    Wakeham, N.4    Zhu, G.5    Li, G.6    Tang, J.7    Zhang, X.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.