메뉴 건너뛰기




Volumn 27, Issue 2, 1997, Pages 204-209

Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs

Author keywords

crystal; GTPase; kinetics; NMR; rab7; targeting; vesicle

Indexed keywords

GUANOSINE TRIPHOSPHATASE; RAB PROTEIN;

EID: 0031048762     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199702)27:2<204::AID-PROT6>3.0.CO;2-F     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H.R., Sanders, D.A., McCormick, F. The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349:117-127, 1991.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0342505368 scopus 로고
    • Small GTPases and their regulators. Part C: Proteins involved in transport
    • Balch, W.E., Der, C.D., Hall, A. Small GTPases and their regulators. Part C: Proteins involved in transport. Methods Enzymol. 255:1995.
    • (1995) Methods Enzymol. , vol.255
    • Balch, W.E.1    Der, C.D.2    Hall, A.3
  • 3
    • 0027436941 scopus 로고
    • Rab proteins and the road maps for intracellular transport
    • Simons, K., Zerial, M. Rab proteins and the road maps for intracellular transport. Neuron 11:789-799, 1993.
    • (1993) Neuron , vol.11 , pp. 789-799
    • Simons, K.1    Zerial, M.2
  • 4
    • 0028107932 scopus 로고
    • Rab GTPases: Master regulators of membrane trafficking
    • Pfeffer, S.R. Rab GTPases: Master regulators of membrane trafficking. Curr. Opin. Cell Biol. 6:522-6, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 522-526
    • Pfeffer, S.R.1
  • 5
    • 0025363426 scopus 로고
    • Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
    • Chavrier, P., Parton, R.G., Hauri, H.P., Simons, K., Zerial, M. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell 62:317-29, 1990.
    • (1990) Cell , vol.62 , pp. 317-329
    • Chavrier, P.1    Parton, R.G.2    Hauri, H.P.3    Simons, K.4    Zerial, M.5
  • 6
    • 0029585762 scopus 로고
    • Rab7: An important regulator of late endocytic membrane traffic
    • Feng, Y.-F., Press, B., Wandinger-Ness, A. Rab7: An important regulator of late endocytic membrane traffic. J. Cell Biol. 1995.
    • (1995) J. Cell Biol.
    • Feng, Y.-F.1    Press, B.2    Wandinger-Ness, A.3
  • 7
    • 0028803110 scopus 로고
    • The rab7 GTPase resides on a vesicular compartment connected to lysosomes
    • Meresse, S., Gorvel, J.-P., Chavrier, P. The rab7 GTPase resides on a vesicular compartment connected to lysosomes. J. Cell Sci. 108:3349-3358, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 3349-3358
    • Meresse, S.1    Gorvel, J.-P.2    Chavrier, P.3
  • 8
    • 0027092937 scopus 로고
    • Endocytosis in yeast: Evidence for the involvement of a small GTP-binding protein (Ypt7p)
    • Wichmann, H., Hengst, L., Gallwitz, D. Endocytosis in yeast: Evidence for the involvement of a small GTP-binding protein (Ypt7p). Cell 71:1131-42, 1992.
    • (1992) Cell , vol.71 , pp. 1131-1142
    • Wichmann, H.1    Hengst, L.2    Gallwitz, D.3
  • 9
    • 0027449288 scopus 로고
    • Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the vacuole in yeast
    • Schimmoller, F., Riezman, H. Involvement of Ypt7p, a small GTPase, in traffic from late endosome to the vacuole in yeast. J. Cell Sci. 1993.
    • (1993) J. Cell Sci.
    • Schimmoller, F.1    Riezman, H.2
  • 10
    • 0029294647 scopus 로고
    • Characterization of membrane-bound small GTP-binding proteins from Nicotiana tabacum
    • Haizel, T., Merkle, T., Turck, F., Nagy, F. Characterization of membrane-bound small GTP-binding proteins from Nicotiana tabacum. Plant Physiol. 108:59-67, 1995.
    • (1995) Plant Physiol. , vol.108 , pp. 59-67
    • Haizel, T.1    Merkle, T.2    Turck, F.3    Nagy, F.4
  • 11
    • 0027570515 scopus 로고
    • Sequence of a novel plant ras-related cDNA from Pisum sativum
    • Drew, J.E., Bown, D., Gatehouse, J.A. Sequence of a novel plant ras-related cDNA from Pisum sativum. Plant Mol. Biol. 21:1195-1199, 1993.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 1195-1199
    • Drew, J.E.1    Bown, D.2    Gatehouse, J.A.3
  • 12
    • 0028090535 scopus 로고
    • Characterization of lysosomal membrane proteins of Dictyostelium discoideum: A complex population of acidic integral membrane glycoproteins, Rab GTP-binding proteins and vacuolar ATPase subunits
    • Temesvari, L., Rodriguez, P.J., Bush, J., Steck, T.L., Cardelli, J. Characterization of lysosomal membrane proteins of Dictyostelium discoideum: A complex population of acidic integral membrane glycoproteins, Rab GTP-binding proteins and vacuolar ATPase subunits. J. Biol. Chem 269: 25719-27, 1994.
    • (1994) J. Biol. Chem , vol.269 , pp. 25719-25727
    • Temesvari, L.1    Rodriguez, P.J.2    Bush, J.3    Steck, T.L.4    Cardelli, J.5
  • 13
    • 0025948794 scopus 로고
    • Hypervariable C-terminal domain of rab proteins acts as a targeting signal
    • 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 353:769-772, 1991.
    • (1991) Nature , vol.353 , pp. 769-772
    • Chavrier, P.1    Gorvel, J.P.2    Stelzer, E.3    Simons, K.4    Gruenberg, J.5    Zerial, M.6
  • 14
    • 0027954202 scopus 로고
    • Distinct structural elements of rab5 define its functional specificity
    • Stenmark, H., Valencia, A., Martinez, O., Ullrich, O., Goud, B., Zerial, M. Distinct structural elements of rab5 define its functional specificity. Embo J. 13:575-83, 1994.
    • (1994) Embo J. , vol.13 , pp. 575-583
    • Stenmark, H.1    Valencia, A.2    Martinez, O.3    Ullrich, O.4    Goud, B.5    Zerial, M.6
  • 15
    • 0027470208 scopus 로고
    • Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4
    • Brennwald, P., Novick, P. Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362:560-563, 1993.
    • (1993) Nature , vol.362 , pp. 560-563
    • Brennwald, P.1    Novick, P.2
  • 16
    • 0028326049 scopus 로고
    • Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange
    • Ullrich, O., Horiuchi, H., Bucci, C., Zerial, M. Membrane association of Rab5 mediated by GDP-dissociation inhibitor and accompanied by GDP/GTP exchange [see comments]. Nature 368:157-160, 1994.
    • (1994) Nature , vol.368 , pp. 157-160
    • Ullrich, O.1    Horiuchi, H.2    Bucci, C.3    Zerial, M.4
  • 17
    • 0028207180 scopus 로고
    • Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange
    • Soldati, T., Shapiro, A.D., Svejstrup, A.B., Pfeffer, S.R. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange [see comments]. Nature 369: 76-78, 1994.
    • (1994) Nature , vol.369 , pp. 76-78
    • Soldati, T.1    Shapiro, A.D.2    Svejstrup, A.B.3    Pfeffer, S.R.4
  • 18
    • 0028168008 scopus 로고
    • A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles
    • Sogaard, M., Tani, K., Ye, R.R., Geromanos, S., Tempst, P., Kirchhausen, T., Rothman, J.E., Sollner, T. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell 78:937-948, 1994.
    • (1994) Cell , vol.78 , pp. 937-948
    • Sogaard, M.1    Tani, K.2    Ye, R.R.3    Geromanos, S.4    Tempst, P.5    Kirchhausen, T.6    Rothman, J.E.7    Sollner, T.8
  • 20
    • 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. Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion. Cell 83:423-432, 1995.
    • (1995) Cell , vol.83 , pp. 423-432
    • Stenmark, H.1    Vitale, G.2    Ullrich, O.3    Zerial, M.4
  • 22
    • 0030046054 scopus 로고    scopus 로고
    • Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides
    • Schmidt, G., Lenzen, C., Simon, I., Deuter, R., Cool, R., Goody, R., Wittinghofer, A. Biochemical and biological consequences of changing the specificity of p21ras from guanosine to xanthosine nucleotides. Oncogene 12:87-96, 1996.
    • (1996) Oncogene , vol.12 , pp. 87-96
    • Schmidt, G.1    Lenzen, C.2    Simon, I.3    Deuter, R.4    Cool, R.5    Goody, R.6    Wittinghofer, A.7
  • 23
    • 0023665149 scopus 로고
    • A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP Regulatory
    • L.
    • Hwang, Y.-W., Miller, D., L. A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP Regulatory Prot. J. Biol. Chem. 262:13081-13085, 1987.
    • (1987) Prot. J. Biol. Chem. , vol.262 , pp. 13081-13085
    • Hwang, Y.-W.1    Miller, D.2
  • 24
    • 0029098572 scopus 로고
    • Requirement of nucleotide exchange factor for Ypt1 GTPase mediated protein transport
    • Jones, S., Litt, R.J., Richardson, C.J., Segev, N. Requirement of nucleotide exchange factor for Ypt1 GTPase mediated protein transport. J. Cell Biol. 130:1051-1061, 1995.
    • (1995) J. Cell Biol. , vol.130 , pp. 1051-1061
    • Jones, S.1    Litt, R.J.2    Richardson, C.J.3    Segev, N.4
  • 25
    • 0342505360 scopus 로고    scopus 로고
    • Rab7: Crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp
    • submitted
    • Brachvogel, V., Neu, M., Metcalf, P. Rab7: Crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp. Proteins (submitted) 1996.
    • (1996) Proteins
    • Brachvogel, V.1    Neu, M.2    Metcalf, P.3
  • 26
    • 0029831063 scopus 로고    scopus 로고
    • Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions
    • Simon, I., Zerial, M., Goody, R.S. Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. Biochemistry 271:20470-20478, 1996.
    • (1996) Biochemistry , vol.271 , pp. 20470-20478
    • Simon, I.1    Zerial, M.2    Goody, R.S.3
  • 28
    • 0025200302 scopus 로고
    • Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line
    • Chavrier, P., Vingron, M., Sander, C., Simons, K., Zerial, M. Molecular cloning of YPT1/SEC4-related cDNAs from an epithelial cell line. Mol. Cell. Biol. 10:6578-6585, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6578-6585
    • Chavrier, P.1    Vingron, M.2    Sander, C.3    Simons, K.4    Zerial, M.5
  • 29
    • 0023464708 scopus 로고
    • Vectors for selective expression of cloned DNAs by T7 RNA polymerase
    • Rosenberg, A.H., Lade, B.N., Chui, D.S., Lin, S.W., Dunn, J.J., Studier, F.W. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene 56:125-135, 1987.
    • (1987) Gene , vol.56 , pp. 125-135
    • Rosenberg, A.H.1    Lade, B.N.2    Chui, D.S.3    Lin, S.W.4    Dunn, J.J.5    Studier, F.W.6
  • 30
    • 0029046847 scopus 로고
    • Electrospray mass spectrometry for protein characterization
    • Mann, M., Wilm, M. Electrospray mass spectrometry for protein characterization. Trends Biochem. Sci. 20:219-224, 1995.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 219-224
    • Mann, M.1    Wilm, M.2
  • 32
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T.W. Physiological concentrations of purines and pyrimidines. Mol. Cell Biochem. 140:1-22, 1994.
    • (1994) Mol. Cell Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 33
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D., Richards, F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:311-333, 1991.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 34
    • 0027531811 scopus 로고
    • Biochemical analysis of rab9, a ras-like GTPase involved in protein transport from late endosomes to the trans Golgi network
    • Shapiro, A., Riederer, M.A., Pfeffer, S.R. Biochemical analysis of rab9, a ras-like GTPase involved in protein transport from late endosomes to the trans Golgi network. J. Biol. Chem. 268:6925-6931, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6925-6931
    • Shapiro, A.1    Riederer, M.A.2    Pfeffer, S.R.3
  • 35
    • 0029064482 scopus 로고
    • Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides
    • Shapiro, A.D., Pfeffer, S.R. Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides. J. Biol. Chem. 270: 11085-11090, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11085-11090
    • Shapiro, A.D.1    Pfeffer, S.R.2
  • 36
    • 0028128334 scopus 로고
    • ARF: A key regulatory switch in membrane traffic and organelle structure
    • Donaldson, J.G., Klausner, R.D. ARF: a key regulatory switch in membrane traffic and organelle structure. Curr. Opin. Cell Biol. 6:527-532, 1994.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 527-532
    • Donaldson, J.G.1    Klausner, R.D.2
  • 37
    • 0028929866 scopus 로고
    • Crystal Structure of the nuclear Ras-related protein Ran in its GDP-bound form
    • Scheffzek, K., Klebe, C., Fritz-Wolf, K., Kabsch, W., Wittinghofer, A. Crystal Structure of the nuclear Ras-related protein Ran in its GDP-bound form. Nature 374:378-381, 1995.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritz-Wolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 38
    • 0028556994 scopus 로고
    • Structure of the human ADP-ribosylation factor 1 complexed with GDP
    • Amor, J.C., Harrison, D.H., Kahn, R.A., Ringe, D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372:704-708, 1994.
    • (1994) Nature , vol.372 , pp. 704-708
    • Amor, J.C.1    Harrison, D.H.2    Kahn, R.A.3    Ringe, D.4
  • 39
    • 0029113233 scopus 로고
    • The structure of rad ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
    • Greasley, S.E., Jhoti, H., Teahan, C., Solari, R., Fensome, A., Thomas, G., Cockcroft, S., Bax, B. The structure of rad ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nature Struct Biol. 2:797-806, 1995.
    • (1995) Nature Struct Biol. , vol.2 , pp. 797-806
    • Greasley, S.E.1    Jhoti, H.2    Teahan, C.3    Solari, R.4    Fensome, A.5    Thomas, G.6    Cockcroft, S.7    Bax, B.8
  • 40
    • 0025117674 scopus 로고
    • Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins
    • Milburn, M.V., Tong, L., deVos, A.M., Brunger, A., Yamaizumi, Z., Nishimura, S., Kim, S.H. Molecular switch for signal transduction: Structural differences between active and inactive forms of protooncogenic ras proteins. Science 247:939-945, 1990.
    • (1990) Science , vol.247 , pp. 939-945
    • Milburn, M.V.1    Tong, L.2    DeVos, A.M.3    Brunger, A.4    Yamaizumi, Z.5    Nishimura, S.6    Kim, S.H.7
  • 41
    • 0026677038 scopus 로고
    • Guanine-nucleotide binding activity, interaction with GTPase-activating protein and solution conformation of the human c-Ha-Ras protein catalytic domain are retained upon deletion of C-terminal 18 ammo acid residues
    • Fujita, Y.J., Ito, Y., Yamasaki, K., Muto, Y., Miyazawa, T., Nishimura, S., Yokoyama, S. Guanine-nucleotide binding activity, interaction with GTPase-activating protein and solution conformation of the human c-Ha-Ras protein catalytic domain are retained upon deletion of C-terminal 18 ammo acid residues. J. Prot. Chem. 11:731-739, 1992.
    • (1992) J. Prot. Chem. , vol.11 , pp. 731-739
    • Fujita, Y.J.1    Ito, Y.2    Yamasaki, K.3    Muto, Y.4    Miyazawa, T.5    Nishimura, S.6    Yokoyama, S.7
  • 42
    • 0024347565 scopus 로고
    • C-terminal truncation of p21Hros preserves crucial kinetic and structural properties
    • John, J., Schlichting, I., Schiltz, E., Rosch, P., Wittinghofer, A. C-terminal truncation of p21Hros preserves crucial kinetic and structural properties. J. Biol. Chem. 264:13086-13092, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13086-13092
    • John, J.1    Schlichting, I.2    Schiltz, E.3    Rosch, P.4    Wittinghofer, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.