메뉴 건너뛰기




Volumn 413, Issue 2, 2011, Pages 372-389

RGK family G-domain:GTP analog complex structures and nucleotide-binding properties

Author keywords

conformational switch; crystallography; fluorescence spectroscopy; G protein

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' BETA,GAMMA IMIDOPHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE DERIVATIVE; NUCLEIC ACID BINDING PROTEIN; PROTEIN GEM; PROTEIN RAD; PROTEIN REM 1; PROTEIN REM 2; PROTEIN RGK; RHO KINASE; UNCLASSIFIED DRUG; VOLTAGE GATED CALCIUM CHANNEL;

EID: 80054729017     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.08.017     Document Type: Article
Times cited : (28)

References (42)
  • 1
    • 0027741390 scopus 로고
    • Rad: A member of the ras family overexpressed in muscle of type II diabetic humans
    • Reynet C., and Kahn C.R. Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans Science 262 1993 1441 1444 (Pubitemid 24035065)
    • (1993) Science , vol.262 , Issue.5138 , pp. 1441-1444
    • Reynet, C.1    Kahn, C.R.2
  • 2
    • 0028137073 scopus 로고
    • Gem: An induced, immediate early protein belonging to the Ras family
    • Maguire J., Santoro T., Jensen P., Siebenlist U., Yewdell J., and Kelly K. Gem: an induced, immediate early protein belonging to the Ras family Science 265 1994 241 244 (Pubitemid 24259926)
    • (1994) Science , vol.265 , Issue.5169 , pp. 241-244
    • Maguire, J.1    Santoro, T.2    Jensen, P.3    Siebenlist, U.4    Yewdell, J.5    Kelly, K.6
  • 3
    • 0030803793 scopus 로고    scopus 로고
    • Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation
    • DOI 10.1074/jbc.272.35.21982
    • Finlin B.S., and Andres D.A. Rem is a new member of the Rad- and Gem/Kir Ras-related GTP-binding protein family repressed by lipopolysaccharide stimulation J. Biol. Chem. 272 1997 21982 21988 (Pubitemid 27382820)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.35 , pp. 21982-21988
    • Finlin, B.S.1    Andres, D.A.2
  • 4
    • 0034177553 scopus 로고    scopus 로고
    • Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases
    • DOI 10.1042/0264-6021:3470223
    • Finlin B.S., Shao H., Kadono-Okuda K., Guo N., and Andres D.A. Rem2, a new member of the Rem/Rad/Gem/Kir family of Ras-related GTPases Biochem. J. 347 2000 223 231 (Pubitemid 30199062)
    • (2000) Biochemical Journal , vol.347 , Issue.1 , pp. 223-231
    • Finlin, B.S.1    Shao, H.2    Kadono-Okuda, K.3    Guo, N.4    Andres, D.A.5
  • 5
    • 0029834335 scopus 로고    scopus 로고
    • Calmodulin binds to and inhibits GTP binding of the Ras-like GTPase Kir/Gem
    • DOI 10.1074/jbc.271.41.25067
    • Fischer R., Wei Y., Anagli J., and Berchtold M.W. Calmodulin binds to and inhibits GTP binding of the ras-like GTPase Kir/Gem J. Biol. Chem. 271 1996 25067 25070 (Pubitemid 26337863)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.41 , pp. 25067-25070
    • Fischer, R.1    Wei, Y.2    Anagli, J.3    Berchtold, M.W.4
  • 6
    • 33845313646 scopus 로고    scopus 로고
    • 2 lipids target proteins with polybasic clusters to the plasma membrane
    • DOI 10.1126/science.1134389
    • Heo W.D., Inoue T., Park W.S., Kim M.L., Park B.O., Wandless T.J., and Meyer T. PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane Science 314 2006 1458 1461 (Pubitemid 44871952)
    • (2006) Science , vol.314 , Issue.5804 , pp. 1458-1461
    • Won, D.H.1    Inoue, T.2    Wei, S.P.3    Man, L.K.4    Byung, O.P.5    Wandless, T.J.6    Meyer, T.7
  • 7
    • 34547114253 scopus 로고    scopus 로고
    • ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs
    • DOI 10.1074/jbc.M701347200
    • Bowzard J.B., Cheng D., Peng J., and Kahn R.A. ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs J. Biol. Chem. 282 2007 17568 17580 (Pubitemid 47100320)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17568-17580
    • Bowzard, J.B.1    Cheng, D.2    Peng, J.3    Kahn, R.A.4
  • 10
    • 0037092045 scopus 로고    scopus 로고
    • The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway
    • DOI 10.1083/jcb.200111026
    • Ward Y., Yap S.F., Ravichandran V., Matsumura F., Ito M., Spinelli B., and Kelly K. The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway J. Cell Biol. 157 2002 291 302 (Pubitemid 34839825)
    • (2002) Journal of Cell Biology , vol.157 , Issue.2 , pp. 291-302
    • Ward, Y.1    Yap, S.-F.2    Ravichandran, V.3    Matsumura, F.4    Ito, M.5    Spinelli, B.6    Kelly, K.7
  • 15
    • 33750527124 scopus 로고    scopus 로고
    • 2+ channels by RGK GTPases
    • DOI 10.1085/jgp.200609631
    • 2+ channels by RGK GTPases J. Gen. Physiol. 128 2006 605 613 (Pubitemid 44664637)
    • (2006) Journal of General Physiology , vol.128 , Issue.5 , pp. 605-613
    • Seu, L.1    Pitt, G.S.2
  • 20
    • 33746178724 scopus 로고    scopus 로고
    • Crystal structure of human Rad GTPase of the RGK-family
    • DOI 10.1111/j.1365-2443.2006.00994.x
    • Yanuar A., Sakurai S., Kitano K., and Hakoshima T. Crystal structure of human Rad GTPase of the RGK-family Genes Cells 11 2006 961 968 (Pubitemid 44084030)
    • (2006) Genes to Cells , vol.11 , Issue.8 , pp. 961-968
    • Yanuar, A.1    Sakurai, S.2    Kitano, K.3    Hakoshima, T.4
  • 21
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • DOI 10.1126/science.1062023
    • Vetter I.R., and Wittinghofer A. The guanine nucleotide-binding switch in three dimensions Science 294 2001 1299 1304 (Pubitemid 33063089)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 23
    • 16644370412 scopus 로고    scopus 로고
    • Human RAS superfamily proteins and related GTPases
    • Colicelli J. Human RAS superfamily proteins and related GTPases Sci. STKE 2004 2004 RE13
    • (2004) Sci. STKE , vol.2004 , pp. 13
    • Colicelli, J.1
  • 24
    • 3042681902 scopus 로고    scopus 로고
    • ConSeq: The identification of functionally and structurally important residues in protein sequences
    • DOI 10.1093/bioinformatics/bth070
    • Berezin C., Glaser F., Rosenberg J., Paz I., Pupko T., and Fariselli P. ConSeq: the identification of functionally and structurally important residues in protein sequences Bioinformatics 20 2004 1322 1324 (Pubitemid 38807587)
    • (2004) Bioinformatics , vol.20 , Issue.8 , pp. 1322-1324
    • Berezin, C.1    Glaser, F.2    Rosenberg, J.3    Paz, I.4    Pupko, T.5    Fariselli, P.6    Casadio, R.7    Ben-Tal, N.8
  • 25
    • 0028336790 scopus 로고
    • Fluorescent guanine nucleotide analogs and G protein activation
    • Remmers A.E., Posner R., and Neubig R.R. Fluorescent guanine nucleotide analogs and G protein activation J. Biol. Chem. 269 1994 13771 13778 (Pubitemid 24191119)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.19 , pp. 13771-13778
    • Remmers, A.E.1    Posner, R.2    Neubig, R.R.3
  • 26
    • 33845992204 scopus 로고    scopus 로고
    • Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides
    • DOI 10.1074/jbc.M607461200
    • Pisareva V.P., Pisarev A.V., Hellen C.U., Rodnina M.V., and Pestova T.V. Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotides J. Biol. Chem. 281 2006 40224 40235 (Pubitemid 46043300)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 40224-40235
    • Pisareva, V.P.1    Pisarev, A.V.2    Hellen, C.U.T.3    Rodnina, M.V.4    Pestova, T.V.5
  • 27
    • 0024522512 scopus 로고
    • The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-ras. The stereochemical course of the GTPase reaction
    • Feuerstein J., Goody R.S., and Webb M.R. The mechanism of guanosine nucleotide hydrolysis by p21 c-Ha-ras. The stereochemical course of the GTPase reaction J. Biol. Chem. 264 1989 6188 6190 (Pubitemid 19106690)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.11 , pp. 6188-6190
    • Feuerstein, J.1    Goody, R.S.2    Webb, M.R.3
  • 28
    • 0025337447 scopus 로고
    • Kinetics of interaction of nucleotides with nucleotide-free H-ras p21
    • DOI 10.1021/bi00477a025
    • John J., Sohmen R., Feuerstein J., Linke R., Wittinghofer A., and Goody R.S. Kinetics of interaction of nucleotides with nucleotide-free H-ras p21 Biochemistry 29 1990 6058 6065 (Pubitemid 20201412)
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 6058-6065
    • John, J.1    Sohmen, R.2    Feuerstein, J.3    Linke, R.4    Wittinghofer, A.5    Goody, R.S.6
  • 31
    • 0003000807 scopus 로고    scopus 로고
    • Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases
    • Feig L.A. Tools of the trade: use of dominant-inhibitory mutants of Ras-family GTPases Nat. Cell Biol. 1 1999 E25 E27
    • (1999) Nat. Cell Biol. , vol.1
    • Feig, L.A.1
  • 32
    • 0031026430 scopus 로고    scopus 로고
    • A decrease in the intracellular guanosine 5'-triphosphate concentration is necessary for granulocytic differentiation of HL-60 cells, but growth cessation and differentiation are not associated with a change in the activation state of ras, the transforming principle of HL-60 cells
    • Pilz R.B., Huvar I., Scheele J.S., Van den Berghe G., and Boss G.R. A decrease in the intracellular guanosine 5′-triphosphate concentration is necessary for granulocytic differentiation of HL-60 cells, but growth cessation and differentiation are not associated with a change in the activation state of Ras, the transforming principle of HL-60 cells Cell Growth Differ. 8 1997 53 59 (Pubitemid 27030238)
    • (1997) Cell Growth and Differentiation , vol.8 , Issue.1 , pp. 53-59
    • Pilz, R.B.1    Huvar, I.2    Scheele, J.S.3    Van Den Berghe, G.4    Boss, G.R.5
  • 34
    • 0030806158 scopus 로고    scopus 로고
    • - to the GDP-bound state, in the absence of GTPase-activating proteins
    • DOI 10.1074/jbc.272.37.23138
    • - to the GDP-bound state, in the absence of GTPase-activating proteins J. Biol. Chem. 272 1997 23138 23143 (Pubitemid 27392443)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.37 , pp. 23138-23143
    • Diaz, J.F.1    Sillen, A.2    Engelborghs, Y.3
  • 35
    • 0020475170 scopus 로고
    • Fluorescence quenching of liver alcohol dehydrogenase by acrylamide
    • Eftink M.R., and Selvidge L.A. Fluorescence quenching of liver alcohol dehydrogenase by acrylamide Biochemistry 21 1982 117 125
    • (1982) Biochemistry , vol.21 , pp. 117-125
    • Eftink, M.R.1    Selvidge, L.A.2
  • 36
    • 0037308836 scopus 로고    scopus 로고
    • Ras-effector interactions: After one decade
    • DOI 10.1016/S0959-440X(02)00007-6
    • Herrmann C. Ras-effector interactions: after one decade Curr. Opin. Struct. Biol. 13 2003 122 129 (Pubitemid 36170264)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.1 , pp. 122-129
    • Herrmann, C.1
  • 37
    • 36749036721 scopus 로고    scopus 로고
    • Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf
    • DOI 10.1016/j.str.2007.10.011, PII S096921260700408X
    • Buhrman G., Wink G., and Mattos C. Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf Structure 15 2007 1618 1629 (Pubitemid 350213406)
    • (2007) Structure , vol.15 , Issue.12 , pp. 1618-1629
    • Buhrman, G.1    Wink, G.2    Mattos, C.3
  • 38
    • 0028935733 scopus 로고
    • Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity
    • Zhu J., Reynet C., Caldwell J.S., and Kahn C.R. Characterization of Rad, a new member of Ras/GTPase superfamily, and its regulation by a unique GTPase-activating protein (GAP)-like activity J. Biol. Chem. 270 1995 4805 4812
    • (1995) J. Biol. Chem. , vol.270 , pp. 4805-4812
    • Zhu, J.1    Reynet, C.2    Caldwell, J.S.3    Kahn, C.R.4
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.