메뉴 건너뛰기




Volumn 112, Issue 25, 2015, Pages E3179-E3188

Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly

Author keywords

Electron microscopy; Interorganelle tether; Membrane contact sites; Membrane protein complex; Phospholipid exchange

Indexed keywords

HOMODIMER; LIPID BINDING PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; PROTEIN MDM12; PROTEIN MDM34; PROTEIN MMM1; SYNAPTOTAGMIN LIKE MITOCHONDRIAL LIPID BINDING PROTEIN; UNCLASSIFIED DRUG; PROTEIN BINDING; SYNAPTOTAGMIN;

EID: 84935013862     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1422363112     Document Type: Article
Times cited : (153)

References (49)
  • 1
    • 84880617115 scopus 로고    scopus 로고
    • Organization and function of membrane contact sites
    • Helle SC, et al. (2013) Organization and function of membrane contact sites. Biochim Biophys Acta 1833(11):2526-2541.
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.11 , pp. 2526-2541
    • Helle, S.C.1
  • 2
    • 80755153578 scopus 로고    scopus 로고
    • Staying in touch: The molecular era of organelle contact sites
    • Elbaz Y, Schuldiner M (2011) Staying in touch: The molecular era of organelle contact sites. Trends Biochem Sci 36(11):616-623.
    • (2011) Trends Biochem Sci , vol.36 , Issue.11 , pp. 616-623
    • Elbaz, Y.1    Schuldiner, M.2
  • 3
    • 84877583065 scopus 로고    scopus 로고
    • Plasma membrane - Endoplasmic reticulum contact sites regulate phosphatidylcholine synthesis
    • Tavassoli S, et al. (2013) Plasma membrane - endoplasmic reticulum contact sites regulate phosphatidylcholine synthesis. EMBO Rep 14(5):434-440.
    • (2013) EMBO Rep , vol.14 , Issue.5 , pp. 434-440
    • Tavassoli, S.1
  • 5
    • 84906318502 scopus 로고    scopus 로고
    • Phospholipid transport via mitochondria
    • Tamura Y, Sesaki H, Endo T (2014) Phospholipid transport via mitochondria. Traffic 15(9):933-945.
    • (2014) Traffic , vol.15 , Issue.9 , pp. 933-945
    • Tamura, Y.1    Sesaki, H.2    Endo, T.3
  • 6
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM)
    • Raturi A, Simmen T (2013) Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM). Biochim Biophys Acta 1833(1):213-224.
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.1 , pp. 213-224
    • Raturi, A.1    Simmen, T.2
  • 7
    • 84876011203 scopus 로고    scopus 로고
    • Endoplasmic reticulum structure and interconnections with other organelles
    • English AR, Voeltz GK (2013) Endoplasmic reticulum structure and interconnections with other organelles. Cold Spring Harb Perspect Biol 5(4):a013227.
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , Issue.4
    • English, A.R.1    Voeltz, G.K.2
  • 8
    • 67749122635 scopus 로고    scopus 로고
    • An ER-mitochondria tethering complex revealed by a synthetic biology screen
    • Kornmann B, et al. (2009) An ER-mitochondria tethering complex revealed by a synthetic biology screen. Science 325(5939):477-481.
    • (2009) Science , vol.325 , Issue.5939 , pp. 477-481
    • Kornmann, B.1
  • 9
    • 80054847097 scopus 로고    scopus 로고
    • Composition and topology of the endoplasmic reticulum-mitochondria encounter structure
    • Stroud DA, et al. (2011) Composition and topology of the endoplasmic reticulum-mitochondria encounter structure. J Mol Biol 413(4):743-750.
    • (2011) J Mol Biol , vol.413 , Issue.4 , pp. 743-750
    • Stroud, D.A.1
  • 10
    • 80052172908 scopus 로고    scopus 로고
    • The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections
    • Kornmann B, Osman C, Walter P (2011) The conserved GTPase Gem1 regulates endoplasmic reticulum-mitochondria connections. Proc Natl Acad Sci USA 108(34):14151-14156.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.34 , pp. 14151-14156
    • Kornmann, B.1    Osman, C.2    Walter, P.3
  • 11
    • 84860916316 scopus 로고    scopus 로고
    • Gem1 and ERMES do not directly affect phosphatidylserine transport from ER to mitochondria or mitochondrial inheritance
    • Nguyen TT, et al. (2012) Gem1 and ERMES do not directly affect phosphatidylserine transport from ER to mitochondria or mitochondrial inheritance. Traffic 13(6):880-890.
    • (2012) Traffic , vol.13 , Issue.6 , pp. 880-890
    • Nguyen, T.T.1
  • 12
    • 84872202122 scopus 로고    scopus 로고
    • ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae
    • Voss C, Lahiri S, Young BP, Loewen CJ, Prinz WA (2012) ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae. J Cell Sci 125(Pt 20):4791-4799.
    • (2012) J Cell Sci , vol.125 , Issue.20 , pp. 4791-4799
    • Voss, C.1    Lahiri, S.2    Young, B.P.3    Loewen, C.J.4    Prinz, W.A.5
  • 13
    • 84904255813 scopus 로고    scopus 로고
    • Cellular metabolism regulates contact sites between vacuoles and mitochondria
    • Hönscher C, et al. (2014) Cellular metabolism regulates contact sites between vacuoles and mitochondria. Dev Cell 30(1):86-94.
    • (2014) Dev Cell , vol.30 , Issue.1 , pp. 86-94
    • Hönscher, C.1
  • 14
    • 84904270185 scopus 로고    scopus 로고
    • A dynamic interface between vacuoles and mitochondria in yeast
    • Elbaz-Alon Y, et al. (2014) A dynamic interface between vacuoles and mitochondria in yeast. Dev Cell 30(1):95-102.
    • (2014) Dev Cell , vol.30 , Issue.1 , pp. 95-102
    • Elbaz-Alon, Y.1
  • 15
    • 33644905848 scopus 로고    scopus 로고
    • Diverse membrane-associated proteins contain a novel SMP domain
    • Lee I, Hong W (2006) Diverse membrane-associated proteins contain a novel SMP domain. FASEB J 20(2):202-206.
    • (2006) FASEB J , vol.20 , Issue.2 , pp. 202-206
    • Lee, I.1    Hong, W.2
  • 16
    • 77955361329 scopus 로고    scopus 로고
    • Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria
    • Kopec KO, Alva V, Lupas AN (2010) Homology of SMP domains to the TULIP superfamily of lipid-binding proteins provides a structural basis for lipid exchange between ER and mitochondria. Bioinformatics 26(16):1927-1931.
    • (2010) Bioinformatics , vol.26 , Issue.16 , pp. 1927-1931
    • Kopec, K.O.1    Alva, V.2    Lupas, A.N.3
  • 17
    • 79960859357 scopus 로고    scopus 로고
    • Bioinformatics of the TULIP domain superfamily
    • Kopec KO, Alva V, Lupas AN (2011) Bioinformatics of the TULIP domain superfamily. Biochem Soc Trans 39(4):1033-1038.
    • (2011) Biochem Soc Trans , vol.39 , Issue.4 , pp. 1033-1038
    • Kopec, K.O.1    Alva, V.2    Lupas, A.N.3
  • 18
    • 84858123139 scopus 로고    scopus 로고
    • A conserved membrane-binding domain targets proteins to organelle contact sites
    • Toulmay A, Prinz WA (2012) A conserved membrane-binding domain targets proteins to organelle contact sites. J Cell Sci 125(Pt 1):49-58.
    • (2012) J Cell Sci , vol.125 , Issue.1 , pp. 49-58
    • Toulmay, A.1    Prinz, W.A.2
  • 19
    • 63649118181 scopus 로고    scopus 로고
    • Crystal structure of Epiphyas postvittana takeout 1 with bound ubiquinone supports a role as ligand carriers for takeout proteins in insects
    • Hamiaux C, Stanley D, Greenwood DR, Baker EN, Newcomb RD (2009) Crystal structure of Epiphyas postvittana takeout 1 with bound ubiquinone supports a role as ligand carriers for takeout proteins in insects. J Biol Chem 284(6):3496-3503.
    • (2009) J Biol Chem , vol.284 , Issue.6 , pp. 3496-3503
    • Hamiaux, C.1    Stanley, D.2    Greenwood, D.R.3    Baker, E.N.4    Newcomb, R.D.5
  • 20
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
    • Beamer LJ, Carroll SF, Eisenberg D (1997) Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 276(5320):1861-1864.
    • (1997) Science , vol.276 , Issue.5320 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 21
    • 33846989758 scopus 로고    scopus 로고
    • Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules
    • Qiu X, et al. (2007) Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules. Nat Struct Mol Biol 14(2):106-113.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.2 , pp. 106-113
    • Qiu, X.1
  • 22
    • 84885865202 scopus 로고    scopus 로고
    • The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity
    • Eckert JK, et al. (2013) The crystal structure of lipopolysaccharide binding protein reveals the location of a frequent mutation that impairs innate immunity. Immunity 39(4):647-660.
    • (2013) Immunity , vol.39 , Issue.4 , pp. 647-660
    • Eckert, J.K.1
  • 23
    • 84903532519 scopus 로고    scopus 로고
    • Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer
    • Schauder CM, et al. (2014) Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature 510(7506):552-555.
    • (2014) Nature , vol.510 , Issue.7506 , pp. 552-555
    • Schauder, C.M.1
  • 24
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ (2009) Protein structure prediction on the Web: A case study using the Phyre server. Nat Protoc 4(3):363-371.
    • (2009) Nat Protoc , vol.4 , Issue.3 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 25
    • 84883233522 scopus 로고    scopus 로고
    • The ancient and widespread nature of the ER-mitochondria encounter structure
    • Wideman JG, Gawryluk RMR, Gray MW, Dacks JB (2013) The ancient and widespread nature of the ER-mitochondria encounter structure. Mol Biol Evol 30(9):2044-2049.
    • (2013) Mol Biol Evol , vol.30 , Issue.9 , pp. 2044-2049
    • Wideman, J.G.1    Gawryluk, R.M.R.2    Gray, M.W.3    Dacks, J.B.4
  • 26
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information
    • Glaser F, et al. (2003) ConSurf: Identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19(1):163-164.
    • (2003) Bioinformatics , vol.19 , Issue.1 , pp. 163-164
    • Glaser, F.1
  • 27
    • 84886402935 scopus 로고    scopus 로고
    • Mdm10 is an ancient eukaryotic porin co-occurring with the ERMES complex
    • Flinner N, et al. (2013) Mdm10 is an ancient eukaryotic porin co-occurring with the ERMES complex. Biochim Biophys Acta 1833(12):3314-3325.
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.12 , pp. 3314-3325
    • Flinner, N.1
  • 28
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-741.
    • (2003) Nature , vol.425 , Issue.6959 , pp. 737-741
    • Ghaemmaghami, S.1
  • 29
    • 0037352568 scopus 로고    scopus 로고
    • Biosynthesis of phosphatidylcholine in bacteria
    • Sohlenkamp C, López-Lara IM, Geiger O (2003) Biosynthesis of phosphatidylcholine in bacteria. Prog Lipid Res 42(2):115-162.
    • (2003) Prog Lipid Res , vol.42 , Issue.2 , pp. 115-162
    • Sohlenkamp, C.1    López-Lara, I.M.2    Geiger, O.3
  • 30
    • 84884965580 scopus 로고    scopus 로고
    • Lipids of mitochondria
    • Horvath SE, Daum G (2013) Lipids of mitochondria. Prog Lipid Res 52(4):590-614.
    • (2013) Prog Lipid Res , vol.52 , Issue.4 , pp. 590-614
    • Horvath, S.E.1    Daum, G.2
  • 31
    • 0031470335 scopus 로고    scopus 로고
    • Import of lipids into mitochondria
    • Daum G, Vance JE (1997) Import of lipids into mitochondria. Prog Lipid Res 36(2-3):103-130.
    • (1997) Prog Lipid Res , vol.36 , Issue.2-3 , pp. 103-130
    • Daum, G.1    Vance, J.E.2
  • 32
    • 0032898199 scopus 로고    scopus 로고
    • Systematic analysis of yeast strains with possible defects in lipid metabolism
    • Daum G, et al. (1999) Systematic analysis of yeast strains with possible defects in lipid metabolism. Yeast 15(7):601-614.
    • (1999) Yeast , vol.15 , Issue.7 , pp. 601-614
    • Daum, G.1
  • 33
    • 60549111243 scopus 로고    scopus 로고
    • Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry
    • Ejsing CS, et al. (2009) Global analysis of the yeast lipidome by quantitative shotgun mass spectrometry. Proc Natl Acad Sci USA 106(7):2136-2141.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.7 , pp. 2136-2141
    • Ejsing, C.S.1
  • 35
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J (1987) Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146(Pt 2):113-136.
    • (1987) J Microsc , vol.146 , Issue.2 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 36
    • 0031967690 scopus 로고    scopus 로고
    • The BPI/LBP family of proteins: A structural analysis of conserved regions
    • Beamer LJ, Carroll SF, Eisenberg D (1998) The BPI/LBP family of proteins: A structural analysis of conserved regions. Protein Sci 7(4):906-914.
    • (1998) Protein Sci , vol.7 , Issue.4 , pp. 906-914
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 37
    • 79960739849 scopus 로고    scopus 로고
    • Lipid transfer and signaling at organelle contact sites: The tip of the iceberg
    • Toulmay A, Prinz WA (2011) Lipid transfer and signaling at organelle contact sites: The tip of the iceberg. Curr Opin Cell Biol 23(4):458-463.
    • (2011) Curr Opin Cell Biol , vol.23 , Issue.4 , pp. 458-463
    • Toulmay, A.1    Prinz, W.A.2
  • 38
    • 84896871426 scopus 로고    scopus 로고
    • MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond
    • Vance JE (2014) MAM (mitochondria-associated membranes) in mammalian cells: Lipids and beyond. Biochim Biophys Acta 1841(4):595-609.
    • (2014) Biochim Biophys Acta , vol.1841 , Issue.4 , pp. 595-609
    • Vance, J.E.1
  • 39
    • 84870793680 scopus 로고    scopus 로고
    • ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology
    • Manford AG, Stefan CJ, Yuan HL, Macgurn JA, Emr SD (2012) ER-to-plasma membrane tethering proteins regulate cell signaling and ER morphology. Dev Cell 23(6):1129-1140.
    • (2012) Dev Cell , vol.23 , Issue.6 , pp. 1129-1140
    • Manford, A.G.1    Stefan, C.J.2    Yuan, H.L.3    Macgurn, J.A.4    Emr, S.D.5
  • 40
    • 77954301751 scopus 로고    scopus 로고
    • Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface
    • Csordás G, et al. (2010) Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface. Mol Cell 39(1):121-132.
    • (2010) Mol Cell , vol.39 , Issue.1 , pp. 121-132
    • Csordás, G.1
  • 41
    • 0347611095 scopus 로고    scopus 로고
    • Molecular machinery for non-vesicular trafficking of ceramide
    • Hanada K, et al. (2003) Molecular machinery for non-vesicular trafficking of ceramide. Nature 426(6968):803-809.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 803-809
    • Hanada, K.1
  • 43
    • 84890558909 scopus 로고    scopus 로고
    • START ships lipids across interorganelle space
    • Alpy F, Tomasetto C (2014) START ships lipids across interorganelle space. Biochimie 96:85-95.
    • (2014) Biochimie , vol.96 , pp. 85-95
    • Alpy, F.1    Tomasetto, C.2
  • 44
    • 78049253482 scopus 로고    scopus 로고
    • Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
    • Egea PF, Stroud RM (2010) Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes. Proc Natl Acad Sci USA 107(40):17182-17187.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.40 , pp. 17182-17187
    • Egea, P.F.1    Stroud, R.M.2
  • 45
    • 84884419175 scopus 로고    scopus 로고
    • Structural insight into the biogenesis of β-barrel membrane proteins
    • Noinaj N, et al. (2013) Structural insight into the biogenesis of β-barrel membrane proteins. Nature 501(7467):385-390.
    • (2013) Nature , vol.501 , Issue.7467 , pp. 385-390
    • Noinaj, N.1
  • 46
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn EM, Patel DR, Lepore BW, Indic M, van den Berg B (2009) Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 458(7236):367-370.
    • (2009) Nature , vol.458 , Issue.7236 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    Van Den Berg, B.5
  • 47
    • 84925782876 scopus 로고    scopus 로고
    • ER-mitochondria contact sites in yeast: Beyond the myths of ERMES
    • Lang A, John Peter AT, Kornmann B (2015) ER-mitochondria contact sites in yeast: Beyond the myths of ERMES. Curr Opin Cell Biol 35:7-12.
    • (2015) Curr Opin Cell Biol , vol.35 , pp. 7-12
    • Lang, A.1    John Peter, A.T.2    Kornmann, B.3
  • 48
    • 84884210112 scopus 로고    scopus 로고
    • Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins
    • Maeda K, et al. (2013) Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501(7466):257-261.
    • (2013) Nature , vol.501 , Issue.7466 , pp. 257-261
    • Maeda, K.1
  • 49
    • 77957134067 scopus 로고    scopus 로고
    • Non-vesicular lipid transport by lipid-transfer proteins and beyond
    • Lev S (2010) Non-vesicular lipid transport by lipid-transfer proteins and beyond. Nat Rev Mol Cell Biol 11(10):739-750.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.10 , pp. 739-750
    • Lev, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.