메뉴 건너뛰기




Volumn 195, Issue 4, 2011, Pages 605-615

An intramolecular salt bridge drives the soluble domain of GTP-bound atlastin into the postfusion conformation

Author keywords

[No Author keywords available]

Indexed keywords

ATLASTIN; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 81355147407     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201105006     Document Type: Article
Times cited : (30)

References (22)
  • 1
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann, O., and B. Walz. 2001. Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int. Rev. Cytol. 205:149-214. http://dx.doi.org/10.1016/S0074-7696(01)05004-5.
    • (2001) Int. Rev. Cytol. , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 2
    • 79952774592 scopus 로고    scopus 로고
    • Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes
    • Bian, X., R.W. Klemm, T.Y. Liu, M. Zhang, S. Sun, X. Sui, X. Liu, T.A. Rapoport, and J. Hu. 2011. Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes. Proc. Natl. Acad. Sci. USA. 108:3976-3981. http://dx.doi.org/10.1073/pnas.1101643108.
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 3976-3981
    • Bian, X.1    Klemm, R.W.2    Liu, T.Y.3    Zhang, M.4    Sun, S.5    Sui, X.6    Liu, X.7    Rapoport, T.A.8    Hu, J.9
  • 3
    • 79952298783 scopus 로고    scopus 로고
    • Structural basis for the nucleo- tide-dependent dimerization of the large G protein atlastin-1/SPG3A
    • Byrnes, L.J., and H. Sondermann. 2011. Structural basis for the nucleo- tide-dependent dimerization of the large G protein atlastin-1/SPG3A. Proc. Natl. Acad. Sci. USA. 108:2216-2221. http://dx.doi.org/10.1073/pnas.1012792108.
    • (2011) Proc. Natl. Acad. Sci. USA. , vol.108 , pp. 2216-2221
    • Byrnes, L.J.1    Sondermann, H.2
  • 4
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie, J.S., S. Acharya, M. Leonard, S.L. Schmid, and F. Dyda. 2010. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature. 465:435-440. http://dx.doi.org/10.1038/nature09032.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 5
    • 79952297530 scopus 로고    scopus 로고
    • Structural insights into membrane fusion at the endoplasmic reticulum
    • Daumke, O., and G.J. Praefcke. 2011. Structural insights into membrane fusion at the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA. 108:2175-2176. http://dx.doi.org/10.1073/pnas.1019194108.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 2175-2176
    • Daumke, O.1    Praefcke, G.J.2
  • 6
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated proces- sive cleavage of GTP to GMP
    • Ghosh, A., G.J. Praefcke, L. Renault, A. Wittinghofer, and C. Herrmann. 2006. How guanylate-binding proteins achieve assembly-stimulated proces- sive cleavage of GTP to GMP. Nature. 440:101-104. http://dx.doi.org/10.1038/nature04510.
    • (2006) Nature , vol.440 , pp. 101-104
    • Ghosh, A.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 7
    • 68049096310 scopus 로고    scopus 로고
    • A class of dynamin-like GTPases involved in the generation of the tubular ER network
    • Hu, J., Y. Shibata, P.P. Zhu, C. Voss, N. Rismanchi, W.A. Prinz, T.A. Rapoport, and C. Blackstone. 2009. A class of dynamin-like GTPases involved in the generation of the tubular ER network. Cell. 138:549-561. http://dx.doi.org/10.1016/j.cell.2009.05.025.
    • (2009) Cell , vol.138 , pp. 549-561
    • Hu, J.1    Shibata, Y.2    Zhu, P.P.3    Voss, C.4    Rismanchi, N.5    Prinz, W.A.6    Rapoport, T.A.7    Blackstone, C.8
  • 8
    • 0024456323 scopus 로고
    • Construction of the endoplas- mic reticulum
    • Lee, C., M. Ferguson, and L.B. Chen. 1989. Construction of the endoplas- mic reticulum. J. Cell Biol. 109:2045-2055. http://dx.doi.org/10.1083/jcb.109.5.2045.
    • (1989) J. Cell Biol. , vol.109 , pp. 2045-2055
    • Lee, C.1    Ferguson, M.2    Chen, L.B.3
  • 9
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated soft- ware for high-resolution single-particle reconstructions
    • Ludtke, S.J., P.R. Baldwin, and W. Chiu. 1999. EMAN: semiautomated soft- ware for high-resolution single-particle reconstructions. J. Struct. Biol. 128:82-97. http://dx.doi.org/10.1006/jsbi.1999.4174.
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 10
    • 79960580492 scopus 로고    scopus 로고
    • Membrane fusion by the GTPase atlastin requires a conserved C-terminal cytoplasmic tail and dimerization through the middle domain
    • Moss, T.J., C. Andreazza, A. Verma, A. Daga, and J.A. McNew. 2011. Membrane fusion by the GTPase atlastin requires a conserved C-terminal cytoplasmic tail and dimerization through the middle domain. Proc. Natl. Acad. Sci. USA. 108:11133-11138. http://dx.doi.org/10.1073/pnas.1105056108.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 11133-11138
    • Moss, T.J.1    Andreazza, C.2    Verma, A.3    Daga, A.4    McNew, J.A.5
  • 11
    • 0024206251 scopus 로고
    • Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism
    • Neal, S.E., J.F. Eccleston, A. Hall, and M.R. Webb. 1988. Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism. J. Biol. Chem. 263:19718-19722..
    • (1988) J. Biol. Chem. , vol.263 , pp. 19718-19722
    • Neal, S.E.1    Eccleston, J.F.2    Hall, A.3    Webb, M.R.4
  • 12
    • 0035503309 scopus 로고    scopus 로고
    • Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms
    • Niemann, H.H., M.L. Knetsch, A. Scherer, D.J. Manstein, and F.J. Kull. 2001. Crystal structure of a dynamin GTPase domain in both nucleotide-free and GDP-bound forms. EMBO J. 20:5813-5821. http://dx.doi.org/10.1093/emboj/20.21.5813.
    • (2001) EMBO J , vol.20 , pp. 5813-5821
    • Niemann, H.H.1    Knetsch, M.L.2    Scherer, A.3    Manstein, D.J.4    Kull, F.J.5
  • 15
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules? Nat
    • Praefcke, G.J., and H.T. McMahon. 2004. The dynamin superfamily: universal membrane tubulation and fission molecules? Nat. Rev. Mol. Cell Biol. 5:133-147. http://dx.doi.org/10.1038/nrm1313.
    • (2004) Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 16
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • Prakash, B., G.J. Praefcke, L. Renault, A. Wittinghofer, and C. Herrmann. 2000. Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature. 403:567-571. http://dx.doi.org/10.1038/35000617.
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 17
    • 44349157134 scopus 로고    scopus 로고
    • Atlastin GTPases are required for Golgi apparatus and ER morphogenesis
    • Rismanchi, N., C. Soderblom, J. Stadler, P.P. Zhu, and C. Blackstone. 2008. Atlastin GTPases are required for Golgi apparatus and ER morphogenesis. Hum. Mol. Genet. 17:1591-1604. http://dx.doi.org/10.1093/hmg/ddn046.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 1591-1604
    • Rismanchi, N.1    Soderblom, C.2    Stadler, J.3    Zhu, P.P.4    Blackstone, C.5
  • 18
    • 0037452537 scopus 로고    scopus 로고
    • A molecular motor or a regulator? Dynamin's in a class of its own
    • Song, B.D., and S.L. Schmid. 2003. A molecular motor or a regulator? Dynamin's in a class of its own. Biochemistry. 42:1369-1376. http://dx.doi.org/10.1021/bi027062h.
    • (2003) Biochemistry , vol.42 , pp. 1369-1376
    • Song, B.D.1    Schmid, S.L.2
  • 19
    • 4644314874 scopus 로고    scopus 로고
    • Dynamin GTPase domain mu- tants that differentially affect GTP binding, GTP hydrolysis, and clath- rin-mediated endocytosis
    • Song, B.D., M. Leonard, and S.L. Schmid. 2004. Dynamin GTPase domain mu- tants that differentially affect GTP binding, GTP hydrolysis, and clath- rin-mediated endocytosis. J. Biol. Chem. 279:40431-40436. http://dx.doi.org/10.1074/jbc.M407007200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40431-40436
    • Song, B.D.1    Leonard, M.2    Schmid, S.L.3
  • 20
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide- dependent conformational changes in dynamin: evidence for a mecha- nochemical molecular spring
    • Stowell, M.H., B. Marks, P. Wigge, and H.T. McMahon. 1999. Nucleotide- dependent conformational changes in dynamin: evidence for a mecha- nochemical molecular spring. Nat. Cell Biol. 1:27-32. http://dx.doi.org/10.1038/8997.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 27-32
    • Stowell, M.H.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 21
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron mi- croscopy
    • Tang, G., L. Peng, P.R. Baldwin, D.S. Mann, W. Jiang, I. Rees, and S.J. Ludtke. 2007. EMAN2: an extensible image processing suite for electron mi- croscopy. J. Struct. Biol. 157:38-46. http://dx.doi.org/10.1016/j.jsb.2006.05.009.
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 22
    • 0742281520 scopus 로고    scopus 로고
    • Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin
    • Zhu, P.P., A. Patterson, B. Lavoie, J. Stadler, M. Shoeb, R. Patel, and C. Blackstone. 2003. Cellular localization, oligomerization, and membrane association of the hereditary spastic paraplegia 3A (SPG3A) protein atlastin. J. Biol. Chem. 278:49063-49071. http://dx.doi.org/10.1074/jbc.M306702200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49063-49071
    • Zhu, P.P.1    Patterson, A.2    Lavoie, B.3    Stadler, J.4    Shoeb, M.5    Patel, R.6    Blackstone, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.