메뉴 건너뛰기




Volumn 21, Issue 7, 2013, Pages 1203-1213

Structure of Osh3 reveals a conserved mode of phosphoinositide binding in oxysterol-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LIPID TRANSFER PROTEIN; OXYSTEROL; OXYSTEROL BINDING PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PROTEIN OSH3; UNCLASSIFIED DRUG;

EID: 84879814659     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.05.007     Document Type: Article
Times cited : (105)

References (34)
  • 2
    • 4344641314 scopus 로고    scopus 로고
    • A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution
    • C.T. Beh, and J. Rine A role for yeast oxysterol-binding protein homologs in endocytosis and in the maintenance of intracellular sterol-lipid distribution J. Cell Sci. 117 2004 2983 2996
    • (2004) J. Cell Sci. , vol.117 , pp. 2983-2996
    • Beh, C.T.1    Rine, J.2
  • 3
    • 0035108917 scopus 로고    scopus 로고
    • Overlapping functions of the yeast oxysterol-binding protein homologues
    • C.T. Beh, L. Cool, J. Phillips, and J. Rine Overlapping functions of the yeast oxysterol-binding protein homologues Genetics 157 2001 1117 1140
    • (2001) Genetics , vol.157 , pp. 1117-1140
    • Beh, C.T.1    Cool, L.2    Phillips, J.3    Rine, J.4
  • 7
    • 38549169589 scopus 로고    scopus 로고
    • Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling
    • G.D. Fairn, and C.R. McMaster Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling Cell. Mol. Life Sci. 65 2008 228 236
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 228-236
    • Fairn, G.D.1    McMaster, C.R.2
  • 8
    • 80052630805 scopus 로고    scopus 로고
    • Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM
    • A.G. Georgiev, D.P. Sullivan, M.C. Kersting, J.S. Dittman, C.T. Beh, and A.K. Menon Osh proteins regulate membrane sterol organization but are not required for sterol movement between the ER and PM Traffic 12 2011 1341 1355
    • (2011) Traffic , vol.12 , pp. 1341-1355
    • Georgiev, A.G.1    Sullivan, D.P.2    Kersting, M.C.3    Dittman, J.S.4    Beh, C.T.5    Menon, A.K.6
  • 9
    • 84866434896 scopus 로고    scopus 로고
    • Multi-site phosphorylation of oxysterol binding protein (OSBP) regulates sterol binding and activation of Sphingomyelin synthesis
    • A. Goto, X. Liu, C.A. Robinson, and N.D. Ridgway Multi-site phosphorylation of oxysterol binding protein (OSBP) regulates sterol binding and activation of Sphingomyelin synthesis Mol Biol Cell 23 2012 3624 3635
    • (2012) Mol Biol Cell , vol.23 , pp. 3624-3635
    • Goto, A.1    Liu, X.2    Robinson, C.A.3    Ridgway, N.D.4
  • 10
    • 34248202149 scopus 로고    scopus 로고
    • A large number of novel coding small open reading frames in the intergenic regions of the Arabidopsis thaliana genome are transcribed and/or under purifying selection
    • K. Hanada, X. Zhang, J.O. Borevitz, W.H. Li, and S.H. Shiu A large number of novel coding small open reading frames in the intergenic regions of the Arabidopsis thaliana genome are transcribed and/or under purifying selection Genome Res. 17 2007 632 640
    • (2007) Genome Res. , vol.17 , pp. 632-640
    • Hanada, K.1    Zhang, X.2    Borevitz, J.O.3    Li, W.H.4    Shiu, S.H.5
  • 11
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Y.J. Im, S. Raychaudhuri, W.A. Prinz, and J.H. Hurley Structural mechanism for sterol sensing and transport by OSBP-related proteins Nature 437 2005 154 158
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 12
    • 33746939368 scopus 로고    scopus 로고
    • Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae
    • K.G. Kozminski, G. Alfaro, S. Dighe, and C.T. Beh Homologues of oxysterol-binding proteins affect Cdc42p- and Rho1p-mediated cell polarization in Saccharomyces cerevisiae Traffic 7 2006 1224 1242
    • (2006) Traffic , vol.7 , pp. 1224-1242
    • Kozminski, K.G.1    Alfaro, G.2    Dighe, S.3    Beh, C.T.4
  • 14
    • 33845698910 scopus 로고    scopus 로고
    • Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation
    • E. Lessmann, M. Ngo, M. Leitges, S. Minguet, N.D. Ridgway, and M. Huber Oxysterol-binding protein-related protein (ORP) 9 is a PDK-2 substrate and regulates Akt phosphorylation Cell. Signal. 19 2007 384 392
    • (2007) Cell. Signal. , vol.19 , pp. 384-392
    • Lessmann, E.1    Ngo, M.2    Leitges, M.3    Minguet, S.4    Ridgway, N.D.5    Huber, M.6
  • 15
    • 4444307875 scopus 로고    scopus 로고
    • Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions
    • T. Levine Short-range intracellular trafficking of small molecules across endoplasmic reticulum junctions Trends Cell Biol. 14 2004 483 490
    • (2004) Trends Cell Biol. , vol.14 , pp. 483-490
    • Levine, T.1
  • 16
    • 0035163224 scopus 로고    scopus 로고
    • Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction
    • T.P. Levine, and S. Munro Dual targeting of Osh1p, a yeast homologue of oxysterol-binding protein, to both the Golgi and the nucleus-vacuole junction Mol. Biol. Cell 12 2001 1633 1644
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1633-1644
    • Levine, T.P.1    Munro, S.2
  • 17
    • 0038558194 scopus 로고    scopus 로고
    • A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP
    • C.J. Loewen, A. Roy, and T.P. Levine A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP EMBO J. 22 2003 2025 2035
    • (2003) EMBO J. , vol.22 , pp. 2025-2035
    • Loewen, C.J.1    Roy, A.2    Levine, T.P.3
  • 19
    • 84883453530 scopus 로고    scopus 로고
    • Insights into the mechanisms of sterol transport between organelles. Cellular and molecular life sciences
    • 10.1007/s00018-012-1247-3
    • B. Mesmin, B. Antonny, and G. Drin Insights into the mechanisms of sterol transport between organelles. Cellular and molecular life sciences Cell. Mol. Life Sci. 2013 10.1007/s00018-012-1247-3
    • (2013) Cell. Mol. Life Sci.
    • Mesmin, B.1    Antonny, B.2    Drin, G.3
  • 20
    • 77954469729 scopus 로고    scopus 로고
    • Functional implications of sterol transport by the oxysterol-binding protein gene family
    • M.H. Ngo, T.R. Colbourne, and N.D. Ridgway Functional implications of sterol transport by the oxysterol-binding protein gene family Biochem. J. 429 2010 13 24
    • (2010) Biochem. J. , vol.429 , pp. 13-24
    • Ngo, M.H.1    Colbourne, T.R.2    Ridgway, N.D.3
  • 21
    • 77957352699 scopus 로고    scopus 로고
    • The diverse functions of oxysterol-binding proteins
    • S. Raychaudhuri, and W.A. Prinz The diverse functions of oxysterol-binding proteins Annu. Rev. Cell Dev. Biol. 26 2010 157 177
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 157-177
    • Raychaudhuri, S.1    Prinz, W.A.2
  • 22
    • 33645727511 scopus 로고    scopus 로고
    • Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides
    • S. Raychaudhuri, Y.J. Im, J.H. Hurley, and W.A. Prinz Nonvesicular sterol movement from plasma membrane to ER requires oxysterol-binding protein-related proteins and phosphoinositides J. Cell Biol. 173 2006 107 119
    • (2006) J. Cell Biol. , vol.173 , pp. 107-119
    • Raychaudhuri, S.1    Im, Y.J.2    Hurley, J.H.3    Prinz, W.A.4
  • 23
    • 0026564767 scopus 로고
    • Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding
    • N.D. Ridgway, P.A. Dawson, Y.K. Ho, M.S. Brown, and J.L. Goldstein Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding J. Cell Biol. 116 1992 307 319
    • (1992) J. Cell Biol. , vol.116 , pp. 307-319
    • Ridgway, N.D.1    Dawson, P.A.2    Ho, Y.K.3    Brown, M.S.4    Goldstein, J.L.5
  • 25
    • 79551674131 scopus 로고    scopus 로고
    • Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites
    • C.J. Stefan, A.G. Manford, D. Baird, J. Yamada-Hanff, Y. Mao, and S.D. Emr Osh proteins regulate phosphoinositide metabolism at ER-plasma membrane contact sites Cell 144 2011 389 401
    • (2011) Cell , vol.144 , pp. 389-401
    • Stefan, C.J.1    Manford, A.G.2    Baird, D.3    Yamada-Hanff, J.4    Mao, Y.5    Emr, S.D.6
  • 26
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • F.R. Taylor, S.E. Saucier, E.P. Shown, E.J. Parish, and A.A. Kandutsch Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase J. Biol. Chem. 259 1984 12382 12387
    • (1984) J. Biol. Chem. , vol.259 , pp. 12382-12387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3    Parish, E.J.4    Kandutsch, A.A.5
  • 27
    • 0033229885 scopus 로고    scopus 로고
    • Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. density
    • T.C. Terwilliger, and J. Berendzen Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. density Acta Crystallogr. D Biol. Crystallogr. 55 1999 1872 1877
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1872-1877
    • Terwilliger, T.C.1    Berendzen, J.2
  • 28
    • 84870920662 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of the oxysterol-binding protein Osh3 from Saccharomyces cerevisiae
    • J. Tong, H. Yang, S. Ha, Y. Lee, S.H. Eom, and Y.J. Im Crystallization and preliminary X-ray crystallographic analysis of the oxysterol-binding protein Osh3 from Saccharomyces cerevisiae Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 2012 1498 1502
    • (2012) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.68 , pp. 1498-1502
    • Tong, J.1    Yang, H.2    Ha, S.3    Lee, Y.4    Eom, S.H.5    Im, Y.J.6
  • 32
    • 14644391519 scopus 로고    scopus 로고
    • OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation
    • P.Y. Wang, J. Weng, and R.G. Anderson OSBP is a cholesterol-regulated scaffolding protein in control of ERK 1/2 activation Science 307 2005 1472 1476
    • (2005) Science , vol.307 , pp. 1472-1476
    • Wang, P.Y.1    Weng, J.2    Anderson, R.G.3
  • 33
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • M. West, N. Zurek, A. Hoenger, and G.K. Voeltz A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature J. Cell Biol. 193 2011 333 346
    • (2011) J. Cell Biol. , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.