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Volumn 191, Issue 6, 2010, Pages 1127-1139

Molecular architecture of a dynamin adaptor: Implications for assembly of mitochondrial fission complexes

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; DYNAMIN; FACTOR FOR INVERSION STIMULATION; MITOCHONDRIAL PROTEIN; PROTEIN; PROTEIN FIS 1; PROTEIN MDV 1; UNCLASSIFIED DRUG;

EID: 78650155696     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201005046     Document Type: Article
Times cited : (39)

References (31)
  • 1
    • 73949125579 scopus 로고    scopus 로고
    • A mutation associated with CMT2A neuropathy causes defects in Fzo1 GTP hydrolysis, ubiquitylation, and protein turnover
    • doi:10.1091/mbc.E09-07-0622
    • Amiott, E.A., M.M. Cohen, Y. Saint-Georges, A.M. Weissman, and J.M. Shaw. 2009. A mutation associated with CMT2A neuropathy causes defects in Fzo1 GTP hydrolysis, ubiquitylation, and protein turnover. Mol. Biol. Cell. 20:5026-5035. doi:10.1091/mbc.E09-07-0622
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5026-5035
    • Amiott, E.A.1    Cohen, M.M.2    Saint-Georges, Y.3    Weissman, A.M.4    Shaw, J.M.5
  • 2
    • 33745221197 scopus 로고    scopus 로고
    • Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1
    • doi:10.1074/jbc.M513530200
    • Bhar, D., M.A. Karren, M. Babst, and J.M. Shaw. 2006. Dimeric Dnm1-G385D interacts with Mdv1 on mitochondria and can be stimulated to assemble into fission complexes containing Mdv1 and Fis1. J. Biol. Chem. 281:17312-17320. doi:10.1074/jbc.M513530200
    • (2006) J. Biol. Chem. , vol.281 , pp. 17312-17320
    • Bhar, D.1    Karren, M.A.2    Babst, M.3    Shaw, J.M.4
  • 4
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project 4
    • Collaborative Computational Project 4. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. Biol. Crystallogr. D50:760-763.
    • (1994) Acta Crystallogr. D. Biol. Crystallogr. , vol.D50 , pp. 760-763
  • 5
    • 0141541721 scopus 로고    scopus 로고
    • The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria
    • doi:10.1091/mbc.E03-02-0092
    • Cerveny, K.L., and R.E. Jensen. 2003. The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria. Mol. Biol. Cell. 14:4126-4139. doi:10.1091/mbc.E03-02-0092
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4126-4139
    • Cerveny, K.L.1    Jensen, R.E.2
  • 6
    • 0035149539 scopus 로고    scopus 로고
    • Division of mitochondria requires a novel DMN1-interacting protein, Net2p
    • Cerveny, K.L., J.M. McCaffery, and R.E. Jensen. 2001. Division of mitochondria requires a novel DMN1-interacting protein, Net2p. Mol. Biol. Cell. 12:309-321.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 309-321
    • Cerveny, K.L.1    McCaffery, J.M.2    Jensen, R.E.3
  • 7
    • 27744491193 scopus 로고    scopus 로고
    • Emerging functions of mammalian mitochondrial fusion and fission
    • doi:10.1093/hmg/ddi270
    • Chen, H., and D.C. Chan. 2005. Emerging functions of mammalian mitochondrial fusion and fission. Hum. Mol. Genet. 2:R283-R289. doi:10.1093/hmg/ddi270
    • (2005) Hum. Mol. Genet. , vol.2
    • Chen, H.1    Chan, D.C.2
  • 8
    • 1842481270 scopus 로고    scopus 로고
    • Analysis of heterogeneous interactions
    • doi:10.1016/S0076-6879(04)84013-8
    • Cole, J.L. 2004. Analysis of heterogeneous interactions. Methods Enzymol. 384:212-232. doi:10.1016/S0076-6879(04)84013-8
    • (2004) Methods Enzymol. , vol.384 , pp. 212-232
    • Cole, J.L.1
  • 9
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • doi:10.1107/S0907444904019158
    • Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. doi:10.1107/S0907444904019158
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 10
    • 22944440071 scopus 로고    scopus 로고
    • The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria
    • doi:10.1083/jcb.200503148
    • Griffin, E.E., J. Graumann, and D.C. Chan. 2005. The WD40 protein Caf4p is a component of the mitochondrial fission machinery and recruits Dnm1p to mitochondria. J. Cell Biol. 170:237-248. doi:10.1083/jcb.200503148
    • (2005) J. Cell Biol. , vol.170 , pp. 237-248
    • Griffin, E.E.1    Graumann, J.2    Chan, D.C.3
  • 12
    • 27544450920 scopus 로고    scopus 로고
    • The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly
    • doi:10.1083/jcb.200506158
    • Karren, M.A., E.M. Coonrod, T.K. Anderson, and J.M. Shaw. 2005. The role of Fis1p-Mdv1p interactions in mitochondrial fission complex assembly. J. Cell Biol. 171:291-301. doi:10.1083/jcb.200506158
    • (2005) J. Cell Biol. , vol.171 , pp. 291-301
    • Karren, M.A.1    Coonrod, E.M.2    Anderson, T.K.3    Shaw, J.M.4
  • 13
    • 1442337560 scopus 로고    scopus 로고
    • Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation
    • doi:10.1074/jbc.M308436200
    • Kondo-Okamoto, N., J.M. Shaw, and K. Okamoto. 2003. Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation. J. Biol. Chem. 278:48997-49005. doi:10.1074/jbc.M308436200
    • (2003) J. Biol. Chem. , vol.278 , pp. 48997-49005
    • Kondo-Okamoto, N.1    Shaw, J.M.2    Okamoto, K.3
  • 14
    • 3843075121 scopus 로고    scopus 로고
    • Structural basis of mitochondrial tethering by mitofusin complexes
    • doi:10.1126/science.1099793
    • Koshiba, T., S.A. Detmer, J.T. Kaiser, H. Chen, J.M. McCaffery, and D.C. Chan. 2004. Structural basis of mitochondrial tethering by mitofusin complexes. Science. 305:858-862. doi:10.1126/science.1099793
    • (2004) Science , vol.305 , pp. 858-862
    • Koshiba, T.1    Detmer, S.A.2    Kaiser, J.T.3    Chen, H.4    McCaffery, J.M.5    Chan, D.C.6
  • 15
    • 0034733591 scopus 로고    scopus 로고
    • Rapid and reliable protein extraction from yeast
    • doi:10.1002/1097-0061(20000630)16:9〈857::AID-YEA561〉 3.0.CO;2-B
    • Kushnirov, V.V. 2000. Rapid and reliable protein extraction from yeast. Yeast. 16:857-860. doi:10.1002/1097-0061(20000630)16:9〈857::AID- YEA561〉 3.0.CO;2-B
    • (2000) Yeast , vol.16 , pp. 857-860
    • Kushnirov, V.V.1
  • 16
    • 68949217889 scopus 로고    scopus 로고
    • Mechanistic analysis of a dynamin effector
    • doi:10.1126/science.1176921
    • Lackner, L.L., J.S. Horner, and J. Nunnari. 2009. Mechanistic analysis of a dynamin effector. Science. 325:874-877. doi:10.1126/science.1176921
    • (2009) Science , vol.325 , pp. 874-877
    • Lackner, L.L.1    Horner, J.S.2    Nunnari, J.3
  • 18
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • doi:10.1083/jcb.151.2.367
    • Mozdy, A.D., J.M. McCaffery, and J.M. Shaw. 2000. Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J. Cell Biol. 151:367-380. doi:10.1083/jcb.151.2.367
    • (2000) J. Cell Biol. , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 19
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • doi:10.1107/S0907444996012255
    • Murshudov, G.N., A.A. Vagin, and E.J. Dodson. 1997. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr. 53:240-255. doi:10.1107/S0907444996012255
    • (1997) Acta Crystallogr. D Biol. Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 20
    • 33644865144 scopus 로고    scopus 로고
    • Mdv1 interacts with assembled dnm1 to promote mitochondrial division
    • doi:10.1074/jbc.M507943200
    • Naylor, K., E. Ingerman, V. Okreglak, M. Marino, J.E. Hinshaw, and J. Nunnari. 2006. Mdv1 interacts with assembled dnm1 to promote mitochondrial division. J. Biol. Chem. 281:2177-2183. doi:10.1074/jbc.M507943200
    • (2006) J. Biol. Chem. , vol.281 , pp. 2177-2183
    • Naylor, K.1    Ingerman, E.2    Okreglak, V.3    Marino, M.4    Hinshaw, J.E.5    Nunnari, J.6
  • 21
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • doi:10.1146/annurev.genet.38.072902.093019
    • Okamoto, K., and J.M. Shaw. 2005. Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39:503-536. doi:10.1146/annurev.genet.38.072902.093019
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 22
    • 0032547797 scopus 로고    scopus 로고
    • The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast
    • doi:10.1083/jcb.143.2.333
    • Otsuga, D., B.R. Keegan, E. Brisch, J.W. Thatcher, G.J. Hermann, W. Bleazard, and J.M. Shaw. 1998. The dynamin-related GTPase, Dnm1p, controls mitochondrial morphology in yeast. J. Cell Biol. 143:333-349. doi:10.1083/jcb.143.2.333
    • (1998) J. Cell Biol. , vol.143 , pp. 333-349
    • Otsuga, D.1    Keegan, B.R.2    Brisch, E.3    Thatcher, J.W.4    Hermann, G.J.5    Bleazard, W.6    Shaw, J.M.7
  • 23
    • 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 W. Minor. 1997. Processing of x-ray diffraction data collected in oscillation mode. In Methods in Enzymology. Macromolecular Crystallography, part A. Vol. 276. C.W. Carter, Jr. and R.M. Sweet, editors. Academic Press, New York. 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0036536714 scopus 로고    scopus 로고
    • Mitochondrial dynamics and division in budding yeast
    • doi:10.1016/S0962-8924(01)02246-2
    • Shaw, J.M., and J. Nunnari. 2002. Mitochondrial dynamics and division in budding yeast. Trends Cell Biol. 12:178-184. doi:10.1016/S0962-8924(01)02246-2
    • (2002) Trends Cell Biol. , vol.12 , pp. 178-184
    • Shaw, J.M.1    Nunnari, J.2
  • 25
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • doi:10.1016/j.pep.2005.01.016
    • Studier, F.W. 2005. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41:207-234. doi:10.1016/j.pep.2005.01.016
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 26
    • 20444414879 scopus 로고    scopus 로고
    • Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission
    • doi:10.1074/jbc.M414092200
    • Suzuki, M., A. Neutzner, N. Tjandra, and R.J. Youle. 2005. Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission. J. Biol. Chem. 280:21444-21452. doi:10.1074/jbc. M414092200
    • (2005) J. Biol. Chem. , vol.280 , pp. 21444-21452
    • Suzuki, M.1    Neutzner, A.2    Tjandra, N.3    Youle, R.J.4
  • 27
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • doi:10.1107/S0907444999000839
    • Terwilliger, T.C., and J. Berendzen. 1999. Automated MAD and MIR structure solution. Acta Crystallogr. D Biol. Crystallogr. 55:849-861. doi:10.1107/S0907444999000839
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 28
    • 0034676101 scopus 로고    scopus 로고
    • Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division
    • doi:10.1083/jcb.151.2.353
    • Tieu, Q., and J. Nunnari. 2000. Mdv1p is a WD repeat protein that interacts with the dynamin-related GTPase, Dnm1p, to trigger mitochondrial division. J. Cell Biol. 151:353-366. doi:10.1083/jcb.151.2.353
    • (2000) J. Cell Biol. , vol.151 , pp. 353-366
    • Tieu, Q.1    Nunnari, J.2
  • 29
    • 0036322806 scopus 로고    scopus 로고
    • The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission
    • doi:10 .1083/jcb.200205031
    • Tieu, Q., V. Okreglak, K. Naylor, and J. Nunnari. 2002. The WD repeat protein, Mdv1p, functions as a molecular adaptor by interacting with Dnm1p and Fis1p during mitochondrial fission. J. Cell Biol. 158:445-452. doi:10 .1083/jcb.200205031
    • (2002) J. Cell Biol. , vol.158 , pp. 445-452
    • Tieu, Q.1    Okreglak, V.2    Naylor, K.3    Nunnari, J.4
  • 30
    • 0030987407 scopus 로고    scopus 로고
    • MultiCoil: A program for predicting two- and three-stranded coiled coils
    • doi:10.1002/pro.5560060606
    • Wolf, E., P.S. Kim, and B. Berger. 1997. MultiCoil: a program for predicting two- and three-stranded coiled coils. Protein Sci. 6:1179-1189. doi:10.1002/pro.5560060606
    • (1997) Protein Sci. , vol.6 , pp. 1179-1189
    • Wolf, E.1    Kim, P.S.2    Berger, B.3
  • 31
    • 36749075083 scopus 로고    scopus 로고
    • Structural basis for recruitment of mitochondrial fission complexes by Fis1
    • doi:10.1073/pnas.0706441104
    • Zhang, Y., and D.C. Chan. 2007. Structural basis for recruitment of mitochondrial fission complexes by Fis1. Proc. Natl. Acad. Sci. USA. 104:18526-18530. doi:10.1073/pnas.0706441104
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 18526-18530
    • Zhang, Y.1    Chan, D.C.2


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