메뉴 건너뛰기




Volumn 279, Issue 2, 2012, Pages 203-210

The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis

Author keywords

dynamin; GTPase; guanine cap; guanylate binding protein; interferons

Indexed keywords

ARGININE; ASPARTIC ACID; DIMER; GUANINE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN 1; GUANOSINE TRIPHOSPHATE; LYSINE; OLIGOMER; UNCLASSIFIED DRUG;

EID: 84855454189     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08415.x     Document Type: Article
Times cited : (33)

References (29)
  • 1
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne HR, Sanders DA, &, McCormick F, (1990) The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348, 125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, &, McCormick F, (1991) The GTPase superfamily: conserved structure and molecular mechanism. Nature 349, 117-127. (Pubitemid 21912023)
    • (1991) Nature , vol.349 , Issue.6305 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 3
    • 0034253196 scopus 로고    scopus 로고
    • Small G-protein networks: Their crosstalk and signal cascades
    • Matozaki T, Nakanishi H, &, Takai Y, (2000) Small G-protein networks: their crosstalk and signal cascades. Cell Signal 12, 515-524.
    • (2000) Cell Signal , vol.12 , pp. 515-524
    • Matozaki, T.1    Nakanishi, H.2    Takai, Y.3
  • 4
    • 33745685058 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling: Getting inside the cell
    • Koelle MR, (2006) Heterotrimeric G protein signaling: getting inside the cell. Cell 126, 25-27.
    • (2006) Cell , vol.126 , pp. 25-27
    • Koelle, M.R.1
  • 6
    • 0033105560 scopus 로고    scopus 로고
    • Functional diversity in the dynamin family
    • DOI 10.1016/S0962-8924(98)01490-1, PII S0962892498014901
    • van der Bliek AM, (1999) Functional diversity in the dynamin family. Trends Cell Biol 9, 96-102. (Pubitemid 29151785)
    • (1999) Trends in Cell Biology , vol.9 , Issue.3 , pp. 96-102
    • Van Der Bliek, A.M.1
  • 7
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • DOI 10.1038/nrm1313
    • Praefcke GJ, &, McMahon HT, (2004) The dynamin superfamily: universal membrane tubulation and fission molecules? Nat Rev Mol Cell Biol 5, 133-147. (Pubitemid 38160256)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.2 , pp. 133-147
    • Praefcke, G.J.K.1    McMahon, H.T.2
  • 8
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • DOI 10.1126/science.1062023
    • Vetter IR, &, Wittinghofer A, (2001) The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304. (Pubitemid 33063089)
    • (2001) Science , vol.294 , Issue.5545 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 9
    • 0028795913 scopus 로고
    • Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase
    • Herrmann C, Martin GA, &, Wittinghofer A, (1995) Quantitative analysis of the complex between p21ras and the Ras-binding domain of the human Raf-1 protein kinase. J Biol Chem 270, 2901-2905.
    • (1995) J Biol Chem , vol.270 , pp. 2901-2905
    • Herrmann, C.1    Martin, G.A.2    Wittinghofer, A.3
  • 10
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • DOI 10.1016/j.cell.2007.05.018, PII S0092867407006551
    • Bos JL, Rehmann H, &, Wittinghofer A, (2007) GEFs and GAPs: critical elements in the control of small G proteins. Cell 129, 865-877. (Pubitemid 46802708)
    • (2007) Cell , vol.129 , Issue.5 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 11
    • 0033231549 scopus 로고    scopus 로고
    • C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane
    • Labrousse AM, Zappaterra MD, Rube DA, &, van der Bliek AM, (1999) C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial outer membrane. Mol Cell 4, 815-826.
    • (1999) Mol Cell , vol.4 , pp. 815-826
    • Labrousse, A.M.1    Zappaterra, M.D.2    Rube, D.A.3    Van Der Bliek, A.M.4
  • 13
    • 0033616531 scopus 로고    scopus 로고
    • Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus
    • DOI 10.1006/viro.1999.9614
    • Anderson SL, Carton JM, Lou J, Xing L, &, Rubin BY, (1999) Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology 256, 8-14. (Pubitemid 29391821)
    • (1999) Virology , vol.256 , Issue.1 , pp. 8-14
    • Anderson, S.L.1    Carton, J.M.2    Lou, J.3    Xing, L.4    Rubin, B.Y.5
  • 15
    • 0042525961 scopus 로고    scopus 로고
    • The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression
    • DOI 10.1093/emboj/cdg382
    • Guenzi E, Töpolt K, Lubeseder-Martellato C, Jörg A, Naschberger E, Benelli R, Albini A, &, Stürzl M, (2003) The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression. EMBO J 22, 3772-3782. (Pubitemid 36975706)
    • (2003) EMBO Journal , vol.22 , Issue.15 , pp. 3772-3782
    • Guenzi, E.1    Topolt, K.2    Lubeseder-Martellato, C.3    Jorg, A.4    Naschberger, E.5    Benelli, R.6    Albini, A.7    Sturzl, M.8
  • 16
    • 79955777383 scopus 로고    scopus 로고
    • A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection
    • Kim BH, Shenoy AR, Kumar P, Das R, Tiwari S, &, MacMicking JD, (2011) A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science 332, 717-721.
    • (2011) Science , vol.332 , pp. 717-721
    • Kim, B.H.1    Shenoy, A.R.2    Kumar, P.3    Das, R.4    Tiwari, S.5    MacMicking, J.D.6
  • 17
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • DOI 10.1038/35000617
    • Prakash B, Praecke GJ, Renault L, Wittinghofer A, &, Herrmann C, (2000) Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature 403, 567-571. (Pubitemid 30082205)
    • (2000) Nature , vol.403 , Issue.6769 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.K.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 18
    • 0028243476 scopus 로고
    • The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP
    • Schwemmle M, &, Staeheli P, (1994) The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP. J Biol Chem 269, 11299-11305. (Pubitemid 24200342)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.15 , pp. 11299-11305
    • Schwemmlel, M.1    Staeheli, P.2
  • 19
    • 0033578805 scopus 로고    scopus 로고
    • Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif
    • DOI 10.1006/jmbi.1999.3062
    • Praefcke GJ, Geyer M, Schwemmle M, Kalbitzer HR, &, Herrmann C, (1999) Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif. J Mol Biol 292, 321-332. (Pubitemid 29435769)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 321-332
    • Praefcke, G.J.K.1    Geyer, M.2    Schwemmle, M.3    Robert Kalbitzer, H.4    Herrmann, C.5
  • 20
    • 33749390771 scopus 로고    scopus 로고
    • Transient kinetic investigation of GTP hydrolysis catalyzed by interferon-γ-induced hGBP1 (human guanylate binding protein 1)
    • DOI 10.1074/jbc.M604911200
    • Kunzelmann S, Praefcke GJ, &, Herrmann C, (2006) Transient kinetic investigation of GTP hydrolysis catalyzed by interferon-γ-induced hGBP1 (human guanylate binding protein 1). J Biol Chem 281, 28627-28635. (Pubitemid 44507005)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28627-28635
    • Kunzelmann, S.1    Praefcke, G.J.K.2    Herrmann, C.3
  • 21
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
    • DOI 10.1038/nature04510, PII N04510
    • Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, &, Herrmann C, (2006) How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature 440, 101-104. (Pubitemid 43336275)
    • (2006) Nature , vol.440 , Issue.7080 , pp. 101-104
    • Ghosh, A.1    Praefcke, G.J.K.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 22
    • 7044239234 scopus 로고    scopus 로고
    • Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis
    • DOI 10.1016/j.jmb.2004.09.026, PII S0022283604011684
    • Praefcke GJ, Kloep S, Benscheid U, Lilie H, Prakash R, &, Herrmann C, (2004) Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis. J Mol Biol 344, 257-269. (Pubitemid 39422386)
    • (2004) Journal of Molecular Biology , vol.344 , Issue.1 , pp. 257-269
    • Praefcke, G.J.K.1    Kloep, S.2    Benscheid, U.3    Lilie, H.4    Prakash, B.5    Herrmann, C.6
  • 23
    • 30544454966 scopus 로고    scopus 로고
    • Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1)
    • Kunzelmann S, Praefcke GJ, &, Herrmann C, (2005) Nucleotide binding and self-stimulated GTPase activity of human guanylate-binding protein 1 (hGBP1). Methods Enzymol 404, 512-527.
    • (2005) Methods Enzymol , vol.404 , pp. 512-527
    • Kunzelmann, S.1    Praefcke, G.J.2    Herrmann, C.3
  • 24
    • 77949585672 scopus 로고    scopus 로고
    • Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant
    • Wehner M, &, Herrmann C, (2010) Biochemical properties of the human guanylate binding protein 5 and a tumor-specific truncated splice variant. FEBS J 277, 1597-1605.
    • (2010) FEBS J , vol.277 , pp. 1597-1605
    • Wehner, M.1    Herrmann, C.2
  • 25
    • 67349158233 scopus 로고    scopus 로고
    • Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis
    • Vöpel T, Kunzelmann S, &, Herrmann C, (2009) Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis. FEBS Lett 583, 1923-1927.
    • (2009) FEBS Lett , vol.583 , pp. 1923-1927
    • Vöpel, T.1    Kunzelmann, S.2    Herrmann, C.3
  • 27
    • 77958471709 scopus 로고    scopus 로고
    • Dimerization and its role in GMP formation by human guanylate binding proteins
    • Abdullah N, Balakumari M, &, Sau AK, (2010) Dimerization and its role in GMP formation by human guanylate binding proteins. Biophys J 99, 2235-2244.
    • (2010) Biophys J , vol.99 , pp. 2235-2244
    • Abdullah, N.1    Balakumari, M.2    Sau, A.K.3
  • 29
    • 77956849101 scopus 로고    scopus 로고
    • Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase
    • Fres JM, Müller S, &, Praefcke GJ, (2010) Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase. J Lipid Res 51, 2454-2459.
    • (2010) J Lipid Res , vol.51 , pp. 2454-2459
    • Fres, J.M.1    Müller, S.2    Praefcke, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.