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Volumn 381, Issue 2, 2008, Pages 258-266

Flow cytometry for real-time measurement of guanine nucleotide binding and exchange by Ras-like GTPases

Author keywords

Actin remodeling; Fluorescent GTP analogues; Membrane trafficking; Nucleotide binding and exchange; Rab and Rho GTPases

Indexed keywords

BINDING ENERGY; DISSOCIATION; ION EXCHANGE; POSITIVE IONS; PROTEINS;

EID: 50049120233     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.06.039     Document Type: Article
Times cited : (20)

References (49)
  • 4
    • 41149162021 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics by Arf-family GTPases
    • Myers K.R., and Casanova J.E. Regulation of actin cytoskeleton dynamics by Arf-family GTPases. Trends Cell Biol. 18 (2008) 184-192
    • (2008) Trends Cell Biol. , vol.18 , pp. 184-192
    • Myers, K.R.1    Casanova, J.E.2
  • 6
    • 6944246275 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease: An update
    • Shy M.E. Charcot-Marie-Tooth disease: An update. Curr. Opin. Neurol. 17 (2004) 579-585
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 579-585
    • Shy, M.E.1
  • 7
    • 0036488510 scopus 로고    scopus 로고
    • Rho-GTPases and cancer
    • Sahai E., and Marshall C.J. Rho-GTPases and cancer. Cancer 2 (2002) 133-142
    • (2002) Cancer , vol.2 , pp. 133-142
    • Sahai, E.1    Marshall, C.J.2
  • 8
    • 0344851707 scopus 로고    scopus 로고
    • Rab proteins and endocytic trafficking: Potential targets for therapeutic intervention
    • Stein M.P., Dong J., and Wandinger-Ness A. Rab proteins and endocytic trafficking: Potential targets for therapeutic intervention. Adv. Drug Deliv. Rev. 55 (2003) 1421-1437
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1421-1437
    • Stein, M.P.1    Dong, J.2    Wandinger-Ness, A.3
  • 9
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter I.R., and Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 294 (2001) 1299-1304
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 10
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., and McCormick F. The GTPase superfamily: Conserved structure and molecular mechanism. Nature 349 (1991) 117-127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 11
    • 0029831063 scopus 로고    scopus 로고
    • Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions
    • Simon I., Zerial M., and Goody R.S. Kinetics of interaction of Rab5 and Rab7 with nucleotides and magnesium ions. J. Biol. Chem. 271 (1996) 20470-20478
    • (1996) J. Biol. Chem. , vol.271 , pp. 20470-20478
    • Simon, I.1    Zerial, M.2    Goody, R.S.3
  • 12
    • 0031048762 scopus 로고    scopus 로고
    • Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs
    • Neu M., Brachvogel V., Oschkinat H., Zerial M., and Metcalf P. Rab7: NMR and kinetics analysis of intact and C-terminal truncated constructs. Proteins 27 (1997) 204-209
    • (1997) Proteins , vol.27 , pp. 204-209
    • Neu, M.1    Brachvogel, V.2    Oschkinat, H.3    Zerial, M.4    Metcalf, P.5
  • 13
    • 41049085170 scopus 로고    scopus 로고
    • Choose your own path: Specificity in Ras GTPase signaling
    • Goldfinger L.E. Choose your own path: Specificity in Ras GTPase signaling. Mol. Biosyst. 4 (2008) 293-299
    • (2008) Mol. Biosyst. , vol.4 , pp. 293-299
    • Goldfinger, L.E.1
  • 14
    • 0030471082 scopus 로고    scopus 로고
    • B cell antigen receptor signaling links biochemical changes in the class II peptide-loading compartment to enhanced processing
    • Xu X., Press B., Wagle N.M., Cho H., Wandinger-Ness A., and Pierce S.K. B cell antigen receptor signaling links biochemical changes in the class II peptide-loading compartment to enhanced processing. Intl. Immunol. 8 (1996) 1867-1876
    • (1996) Intl. Immunol. , vol.8 , pp. 1867-1876
    • Xu, X.1    Press, B.2    Wagle, N.M.3    Cho, H.4    Wandinger-Ness, A.5    Pierce, S.K.6
  • 16
    • 34247333875 scopus 로고    scopus 로고
    • Differential dynamics of Rab3A and Rab27A on secretory granules
    • Handley M.T., Haynes L.P., and Burgoyne R.D. Differential dynamics of Rab3A and Rab27A on secretory granules. J. Cell Sci. 120 (2007) 973-984
    • (2007) J. Cell Sci. , vol.120 , pp. 973-984
    • Handley, M.T.1    Haynes, L.P.2    Burgoyne, R.D.3
  • 17
    • 39549098329 scopus 로고    scopus 로고
    • Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease
    • Spinosa M.R., Progida C., De Luca A., Colucci A.M., Alifano P., and Bucci C. Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J. Neurosci. 28 (2008) 1640-1648
    • (2008) J. Neurosci. , vol.28 , pp. 1640-1648
    • Spinosa, M.R.1    Progida, C.2    De Luca, A.3    Colucci, A.M.4    Alifano, P.5    Bucci, C.6
  • 18
    • 0025300680 scopus 로고
    • Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic
    • Kabcenell A.K., Goud B., Northup J.K., and Novick P.J. Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic. J. Biol. Chem. 265 (1990) 9366-9372
    • (1990) J. Biol. Chem. , vol.265 , pp. 9366-9372
    • Kabcenell, A.K.1    Goud, B.2    Northup, J.K.3    Novick, P.J.4
  • 19
    • 33645742291 scopus 로고    scopus 로고
    • Nucleotide exchange via local protein unfolding: Structure of Rab8 in complex with MSS4
    • Itzen A., Pylypenko O., Goody R.S., Alexandrov K., and Rak A. Nucleotide exchange via local protein unfolding: Structure of Rab8 in complex with MSS4. EMBO J. 25 (2006) 1445-1455
    • (2006) EMBO J. , vol.25 , pp. 1445-1455
    • Itzen, A.1    Pylypenko, O.2    Goody, R.S.3    Alexandrov, K.4    Rak, A.5
  • 20
    • 0035311495 scopus 로고    scopus 로고
    • Fluorescent BODIPY-GTP analogs: Real-time measurement of nucleotide binding to G proteins
    • McEwen D.P., Gee K.R., Kang H.C., and Neubig R.R. Fluorescent BODIPY-GTP analogs: Real-time measurement of nucleotide binding to G proteins. Anal. Biochem. 291 (2001) 109-117
    • (2001) Anal. Biochem. , vol.291 , pp. 109-117
    • McEwen, D.P.1    Gee, K.R.2    Kang, H.C.3    Neubig, R.R.4
  • 21
    • 1542327701 scopus 로고    scopus 로고
    • Spontaneous nucleotide exchange in low molecular weight GTPases by fluorescently labeled -phosphate-linked GTP analogs
    • Korlach J., Baird D.W., Heikal A.A., Gee K.R., Hoffman G.R., and Webb W.W. Spontaneous nucleotide exchange in low molecular weight GTPases by fluorescently labeled -phosphate-linked GTP analogs. Proc. Natl. Acad. Sci. USA 101 (2004) 2800-2805
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2800-2805
    • Korlach, J.1    Baird, D.W.2    Heikal, A.A.3    Gee, K.R.4    Hoffman, G.R.5    Webb, W.W.6
  • 22
    • 27744476758 scopus 로고    scopus 로고
    • Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors
    • Hemsath L., and Ahmadian M.R. Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors. Methods 37 (2005) 173-182
    • (2005) Methods , vol.37 , pp. 173-182
    • Hemsath, L.1    Ahmadian, M.R.2
  • 23
    • 0029585762 scopus 로고
    • Rab 7: An important regulator of late endocytic membrane traffic
    • Feng Y., Press B., and Wandinger-Ness A. Rab 7: An important regulator of late endocytic membrane traffic. J. Cell Biol. 131 (1995) 1435-1452
    • (1995) J. Cell Biol. , vol.131 , pp. 1435-1452
    • Feng, Y.1    Press, B.2    Wandinger-Ness, A.3
  • 24
    • 0032498795 scopus 로고    scopus 로고
    • Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment
    • Press B., Feng Y., Hoflack B., and Wandinger-Ness A. Mutant Rab7 causes the accumulation of cathepsin D and cation-independent mannose 6-phosphate receptor in an early endocytic compartment. J. Cell Biol. 140 (1998) 1075-1089
    • (1998) J. Cell Biol. , vol.140 , pp. 1075-1089
    • Press, B.1    Feng, Y.2    Hoflack, B.3    Wandinger-Ness, A.4
  • 25
    • 36549019071 scopus 로고    scopus 로고
    • RILP is required for the proper morphology and function of late endosomes
    • Progida C., Malerod L., Stuffers S., Brech A., Bucci C., and Stenmark H. RILP is required for the proper morphology and function of late endosomes. J. Cell Sci. 120 (2007) 3729-3737
    • (2007) J. Cell Sci. , vol.120 , pp. 3729-3737
    • Progida, C.1    Malerod, L.2    Stuffers, S.3    Brech, A.4    Bucci, C.5    Stenmark, H.6
  • 26
    • 0031042589 scopus 로고    scopus 로고
    • Rab7: Crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp
    • Brachvogel V., Neu M., and Metcalf P. Rab7: Crystallization of intact and C-terminal truncated constructs complexed with GDP and GppNHp. Proteins 27 (1997) 210-212
    • (1997) Proteins , vol.27 , pp. 210-212
    • Brachvogel, V.1    Neu, M.2    Metcalf, P.3
  • 27
    • 0035139854 scopus 로고    scopus 로고
    • Fluorescence methods for monitoring interactions of Rab proteins with nucleotides, Rab escort protein, and geranylgeranyltransferase
    • Alexandrov K., Scheidig A.J., and Goody R.S. Fluorescence methods for monitoring interactions of Rab proteins with nucleotides, Rab escort protein, and geranylgeranyltransferase. Methods Enzymol. 329 (2001) 14-31
    • (2001) Methods Enzymol. , vol.329 , pp. 14-31
    • Alexandrov, K.1    Scheidig, A.J.2    Goody, R.S.3
  • 28
    • 0037288228 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of monoprenylated Rab7 GTPase in complex with Rab escort protein 1
    • Rak A., Pylypenko O., Niculae A., Goody R.S., and Alexandrov K. Crystallization and preliminary X-ray diffraction analysis of monoprenylated Rab7 GTPase in complex with Rab escort protein 1. J. Struct. Biol. 141 (2003) 93-95
    • (2003) J. Struct. Biol. , vol.141 , pp. 93-95
    • Rak, A.1    Pylypenko, O.2    Niculae, A.3    Goody, R.S.4    Alexandrov, K.5
  • 29
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley A.J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 16 (2006) 522-529
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 30
    • 33745784661 scopus 로고    scopus 로고
    • Glutathione-S-transferase-green fluorescent protein fusion protein reveals slow dissociation from high site density beads and measures free GSH
    • Tessema M., Simons P.C., Cimino D.F., Sanchez L., Waller A., Posner R.G., Wandinger-Ness A., Prossnitz E.R., and Sklar L.A. Glutathione-S-transferase-green fluorescent protein fusion protein reveals slow dissociation from high site density beads and measures free GSH. Cytometry A 69 (2006) 326-334
    • (2006) Cytometry A , vol.69 , pp. 326-334
    • Tessema, M.1    Simons, P.C.2    Cimino, D.F.3    Sanchez, L.4    Waller, A.5    Posner, R.G.6    Wandinger-Ness, A.7    Prossnitz, E.R.8    Sklar, L.A.9
  • 31
    • 32344440349 scopus 로고    scopus 로고
    • Interaction and functional analyses of human VPS34/p150 phosphatidylinositol 3-kinase complex with Rab7
    • Stein M.P., Cao C., Tessema M., Feng Y., Romero E., Welford A., and Wandinger-Ness A. Interaction and functional analyses of human VPS34/p150 phosphatidylinositol 3-kinase complex with Rab7. Methods Enzymol. 403 (2005) 628-649
    • (2005) Methods Enzymol. , vol.403 , pp. 628-649
    • Stein, M.P.1    Cao, C.2    Tessema, M.3    Feng, Y.4    Romero, E.5    Welford, A.6    Wandinger-Ness, A.7
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0000652708 scopus 로고    scopus 로고
    • Ligand receptor dynamics at streptavidin-coated particle surfaces: A flow cytometric and spectrofluorimetric study
    • Buranda T., Jones G.M., Nolan J.P., Keij J., Lopez G.P., and Sklar L.A. Ligand receptor dynamics at streptavidin-coated particle surfaces: A flow cytometric and spectrofluorimetric study. J. Phys. Chem. B 103 (1999) 3399-3410
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3399-3410
    • Buranda, T.1    Jones, G.M.2    Nolan, J.P.3    Keij, J.4    Lopez, G.P.5    Sklar, L.A.6
  • 36
    • 0031829517 scopus 로고    scopus 로고
    • The emergence of flow cytometry for sensitive, real-time measurements of molecular interactions
    • Nolan J.P., and Sklar L.A. The emergence of flow cytometry for sensitive, real-time measurements of molecular interactions. Nat. Biotechnol. 16 (1998) 633-638
    • (1998) Nat. Biotechnol. , vol.16 , pp. 633-638
    • Nolan, J.P.1    Sklar, L.A.2
  • 37
    • 34147140936 scopus 로고    scopus 로고
    • The development of quantum dot calibration beads and quantitative multicolor bioassays in flow cytometry and microscopy
    • Wu Y., Campos S.K., Lopez G.P., Ozbun M.A., Sklar L.A., and Buranda T. The development of quantum dot calibration beads and quantitative multicolor bioassays in flow cytometry and microscopy. Anal. Biochem. 364 (2007) 180-192
    • (2007) Anal. Biochem. , vol.364 , pp. 180-192
    • Wu, Y.1    Campos, S.K.2    Lopez, G.P.3    Ozbun, M.A.4    Sklar, L.A.5    Buranda, T.6
  • 38
    • 0017669854 scopus 로고
    • Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography
    • Simons P.C., and Vander Jagt D.L. Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem. 82 (1977) 334-341
    • (1977) Anal. Biochem. , vol.82 , pp. 334-341
    • Simons, P.C.1    Vander Jagt, D.L.2
  • 39
    • 0021336303 scopus 로고
    • The kinetics of competitive radioligand binding predicted by the law of mass action
    • Motulsky H.J., and Mahan L.C. The kinetics of competitive radioligand binding predicted by the law of mass action. Mol. Pharmacol. 25 (1984) 1-9
    • (1984) Mol. Pharmacol. , vol.25 , pp. 1-9
    • Motulsky, H.J.1    Mahan, L.C.2
  • 42
    • 0034682668 scopus 로고    scopus 로고
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins
    • 2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J. Biol. Chem. 275 (2000) 25299-25307
    • (2000) J. Biol. Chem. , vol.275 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 43
    • 14044276363 scopus 로고    scopus 로고
    • Mechanism of the guanine nucleotide exchange reaction of Ras GTPase: Evidence for a GTP/GDP displacement model
    • Zhang B., Zhang Y., Shacter E., and Zheng Y. Mechanism of the guanine nucleotide exchange reaction of Ras GTPase: Evidence for a GTP/GDP displacement model. Biochemistry 44 (2005) 2566-2576
    • (2005) Biochemistry , vol.44 , pp. 2566-2576
    • Zhang, B.1    Zhang, Y.2    Shacter, E.3    Zheng, Y.4
  • 44
    • 34247596532 scopus 로고    scopus 로고
    • Structural basis for Rab GTPase activation by VPS9 domain exchange factors
    • Delprato A., and Lambright D.G. Structural basis for Rab GTPase activation by VPS9 domain exchange factors. Nat. Struct. Mol. Biol. 14 (2007) 406-412
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 406-412
    • Delprato, A.1    Lambright, D.G.2
  • 45
    • 0024364916 scopus 로고
    • Three states for the formyl peptide receptor on intact cells
    • Sklar L.A., Mueller H., Omann G., and Oades Z. Three states for the formyl peptide receptor on intact cells. J. Biol. Chem. 264 (1989) 8483-8486
    • (1989) J. Biol. Chem. , vol.264 , pp. 8483-8486
    • Sklar, L.A.1    Mueller, H.2    Omann, G.3    Oades, Z.4
  • 46
    • 0028211237 scopus 로고
    • Determination of guanine and its nucleosides and nucleotides in human erythrocytes by high-performance liquid chromatography with postcolumn fluorescence derivatization using phenylglyoxal reagent
    • Yonekura S., Iwasaki M., Kai M., and Ohkura Y. Determination of guanine and its nucleosides and nucleotides in human erythrocytes by high-performance liquid chromatography with postcolumn fluorescence derivatization using phenylglyoxal reagent. J. Chromatogr. B 654 (1994) 19-24
    • (1994) J. Chromatogr. B , vol.654 , pp. 19-24
    • Yonekura, S.1    Iwasaki, M.2    Kai, M.3    Ohkura, Y.4
  • 47
    • 0033150255 scopus 로고    scopus 로고
    • A twenty strain survey and backcross localization of the erythrocytic GTP concentration determining locus Gtpc on mouse chromosome 9
    • Wiebe G.J., Fung E., Biddle F.G., and Snyder F.F. A twenty strain survey and backcross localization of the erythrocytic GTP concentration determining locus Gtpc on mouse chromosome 9. Genome 42 (1999) 447-452
    • (1999) Genome , vol.42 , pp. 447-452
    • Wiebe, G.J.1    Fung, E.2    Biddle, F.G.3    Snyder, F.F.4
  • 48
    • 0035369256 scopus 로고    scopus 로고
    • Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: Sugar nucleotide contents in cultured insect cells and mammalian cells
    • Tomiya N., Ailor E., Lawrence S.M., Betenbaugh M.J., and Lee Y.C. Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: Sugar nucleotide contents in cultured insect cells and mammalian cells. Anal. Biochem. 293 (2001) 129-137
    • (2001) Anal. Biochem. , vol.293 , pp. 129-137
    • Tomiya, N.1    Ailor, E.2    Lawrence, S.M.3    Betenbaugh, M.J.4    Lee, Y.C.5
  • 49
    • 34247857367 scopus 로고    scopus 로고
    • Development and validation of an assay for the quantification of 11 nucleotides using LC/LC-electrospray ionization-MS
    • Klawitter J., Schmitz V., Klawitter J., Leibfritz D., and Christians U. Development and validation of an assay for the quantification of 11 nucleotides using LC/LC-electrospray ionization-MS. Anal. Biochem. 365 (2007) 230-239
    • (2007) Anal. Biochem. , vol.365 , pp. 230-239
    • Klawitter, J.1    Schmitz, V.2    Klawitter, J.3    Leibfritz, D.4    Christians, U.5


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