메뉴 건너뛰기




Volumn 13, Issue 3, 2014, Pages 363-375

Role of phosphatidylserine in phospholipid flippase-mediated vesicle transport in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CDC50 PROTEIN, S CEREVISIAE; CHO1 PROTEIN, S CEREVISIAE; PHOSPHATIDYLSERINE; PHOSPHATIDYLSERINE SYNTHASE; PHOSPHOLIPID TRANSFER PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84894829344     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00279-13     Document Type: Article
Times cited : (27)

References (69)
  • 1
    • 36549076985 scopus 로고    scopus 로고
    • On the origin of lipid asymmetry: The flip side of ion transport
    • Lenoir G, Williamson P, Holthuis JC. 2007. On the origin of lipid asymmetry: the flip side of ion transport. Curr. Opin. Chem. Biol. 11:654-661. http://dx.doi.org/10.1016/j.cbpa.2007.09.008.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 654-661
    • Lenoir, G.1    Williamson, P.2    Holthuis, J.C.3
  • 2
    • 84862230494 scopus 로고    scopus 로고
    • Phospholipid flippases: Building asymmetric membranes and transport vesicles
    • Sebastian TT, Baldridge RD, Xu P, Graham TR. 2012. Phospholipid flippases: building asymmetric membranes and transport vesicles. Biochim. Biophys. Acta 1821:1068-1077. http://dx.doi.org/10.1016/j. bbalip.2011.12.007.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1068-1077
    • Sebastian, T.T.1    Baldridge, R.D.2    Xu, P.3    Graham, T.R.4
  • 3
    • 79251530748 scopus 로고    scopus 로고
    • Functions of phospholipid flippases
    • Tanaka K, Fujimura-Kamada K, Yamamoto T. 2011. Functions of phospholipid flippases. J. Biochem. 149:131-143. http://dx.doi.org/10.1093/jb /mvq140.
    • (2011) J. Biochem. , vol.149 , pp. 131-143
    • Tanaka, K.1    Fujimura-Kamada, K.2    Yamamoto, T.3
  • 4
    • 33847628162 scopus 로고    scopus 로고
    • Phospholipid flippases
    • Daleke DL. 2007. Phospholipid flippases. J. Biol. Chem. 282:821-825. http://dx.doi.org/10.1074/jbc.R600035200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 821-825
    • Daleke, D.L.1
  • 5
    • 84876313014 scopus 로고    scopus 로고
    • P4 ATPases: Flippases in health and disease
    • van der Mark VA, Elferink RP, Paulusma CC. 2013. P4 ATPases: flippases in health and disease. Int. J. Mol. Sci. 14:7897-7922. http://dx.doi. org/10.3390/ijms14047897.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 7897-7922
    • van der Mark, V.A.1    Elferink, R.P.2    Paulusma, C.C.3
  • 6
    • 3042728119 scopus 로고    scopus 로고
    • Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccha-romyces cerevisiae
    • Saito K, Fujimura-Kamada K, Furuta N, Kato U, Umeda M, Tanaka K. 2004. Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccha-romyces cerevisiae. Mol. Biol. Cell 15:3418-3432. http://dx.doi.org/10. 1091/mbc.E03-11-0829.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3418-3432
    • Saito, K.1    Fujimura-Kamada, K.2    Furuta, N.3    Kato, U.4    Umeda, M.5    Tanaka, K.6
  • 7
    • 33846177595 scopus 로고    scopus 로고
    • Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway
    • Furuta N, Fujimura-Kamada K, Saito K, Yamamoto T, Tanaka K. 2007. Endocytic recycling in yeast is regulated by putative phospholipid translocases and the Ypt31p/32p-Rcy1p pathway. Mol. Biol. Cell 18:295-312. http://dx.doi.org/10.1091/mbc.E06-05-0461.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 295-312
    • Furuta, N.1    Fujimura-Kamada, K.2    Saito, K.3    Yamamoto, T.4    Tanaka, K.5
  • 8
    • 0036732873 scopus 로고    scopus 로고
    • An essential subfamily of Drs2prelated P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system
    • Hua Z, Fatheddin P, Graham TR. 2002. An essential subfamily of Drs2prelated P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol. Biol. Cell 13:3162-3177. http://dx.doi.org/10.1091/mbc.E02-03-0172.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3162-3177
    • Hua, Z.1    Fatheddin, P.2    Graham, T.R.3
  • 9
    • 0037345029 scopus 로고    scopus 로고
    • Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
    • Pomorski T, Lombardi R, Riezman H, Devaux PF, van Meer G, Holthuis JC. 2003. Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol. Biol. Cell 14:1240-1254. http://dx. doi.org/10.1091/mbc.E02-08-0501.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1240-1254
    • Pomorski, T.1    Lombardi, R.2    Riezman, H.3    Devaux, P.F.4    van Meer, G.5    Holthuis, J.C.6
  • 10
    • 0344443667 scopus 로고    scopus 로고
    • Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Hua Z, Graham TR. 2003. Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum. Mol. Biol. Cell 14:4971-4983. http://dx.doi.org/10.1091/mbc.E03-07-0463.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4971-4983
    • Hua, Z.1    Graham, T.R.2
  • 11
    • 4344677343 scopus 로고    scopus 로고
    • Molecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system
    • Wicky S, Schwarz H, Singer-Krüger B. 2004. Molecular interactions of yeast Neo1p, an essential member of the Drs2 family of aminophospholipid translocases, and its role in membrane trafficking within the endomembrane system. Mol. Cell. Biol. 24:7402-7418. http://dx.doi.org/10. 1128/MCB.24.17.7402-7418.2004.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7402-7418
    • Wicky, S.1    Schwarz, H.2    Singer-Krüger, B.3
  • 12
    • 3242669517 scopus 로고    scopus 로고
    • Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function
    • Natarajan P, Wang J, Hua Z, Graham TR. 2004. Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc. Natl. Acad. Sci. U. S. A. 101:10614-10619. http://dx.doi.org/10.1073/pnas.0404146101.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10614-10619
    • Natarajan, P.1    Wang, J.2    Hua, Z.3    Graham, T.R.4
  • 13
    • 33745413294 scopus 로고    scopus 로고
    • Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles
    • Alder-Baerens N, Lisman Q, Luong L, Pomorski T, Holthuis JC. 2006. Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol. Biol. Cell 17:1632-1642. http://dx.doi.org/10.1091/mbc.E05-10-0912.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1632-1642
    • Alder-Baerens, N.1    Lisman, Q.2    Luong, L.3    Pomorski, T.4    Holthuis, J.C.5
  • 14
    • 70349731740 scopus 로고    scopus 로고
    • Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast
    • Zhou X, Graham TR. 2009. Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast. Proc. Natl. Acad. Sci. U. S. A. 106:16586-16591. http://dx.doi.org/10.1073 /pnas.0904293106.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16586-16591
    • Zhou, X.1    Graham, T.R.2
  • 15
    • 0037020182 scopus 로고    scopus 로고
    • A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae
    • Kato U, Emoto K, Fredriksson C, Nakamura H, Ohta A, Kobayashi T, Murakami-Murofushi K, Umeda M. 2002. A novel membrane protein, Ros3p, is required for phospholipid translocation across the plasma membrane in Saccharomyces cerevisiae. J. Biol. Chem. 277:37855-37862. http: //dx.doi.org/10.1074/jbc.M205564200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37855-37862
    • Kato, U.1    Emoto, K.2    Fredriksson, C.3    Nakamura, H.4    Ohta, A.5    Kobayashi, T.6    Murakami-Murofushi, K.7    Umeda, M.8
  • 16
    • 0033552605 scopus 로고    scopus 로고
    • Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function
    • Chen CY, Ingram MF, Rosal PH, Graham TR. 1999. Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J. Cell Biol. 147:1223-1236. http://dx.doi.org/10.1083/jcb. 147.6.1223.
    • (1999) J. Cell Biol. , vol.147 , pp. 1223-1236
    • Chen, C.Y.1    Ingram, M.F.2    Rosal, P.H.3    Graham, T.R.4
  • 17
    • 0037125940 scopus 로고    scopus 로고
    • Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo
    • Gall WE, Geething NC, Hua Z, Ingram MF, Liu K, Chen SI, Graham TR. 2002. Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo. Curr. Biol. 12:1623-1627. http://dx.doi.org/10.1016/S0960-9822(02)01148-X.
    • (2002) Curr. Biol. , vol.12 , pp. 1623-1627
    • Gall, W.E.1    Geething, N.C.2    Hua, Z.3    Ingram, M.F.4    Liu, K.5    Chen, S.I.6    Graham, T.R.7
  • 18
    • 33846217048 scopus 로고    scopus 로고
    • The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN
    • Sakane H, Yamamoto T, Tanaka K. 2006. The functional relationship between the Cdc50p-Drs2p putative aminophospholipid translocase and the Arf GAP Gcs1p in vesicle formation in the retrieval pathway from yeast early endosomes to the TGN. Cell Struct. Funct 31:87-108. http://dx.doi. org/10.1247/csf.06021.
    • (2006) Cell Struct. Funct , vol.31 , pp. 87-108
    • Sakane, H.1    Yamamoto, T.2    Tanaka, K.3
  • 19
    • 53849132778 scopus 로고    scopus 로고
    • P4-ATPase requirement for AP-1/clathrin function in protein transport from the trans-Golgi network and early endosomes
    • Liu K, Surendhran K, Nothwehr SF, Graham TR. 2008. P4-ATPase requirement for AP-1/clathrin function in protein transport from the trans-Golgi network and early endosomes. Mol. Biol. Cell 19:3526-3535. http://dx.doi.org/10.1091/mbc.E08-01-0025.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3526-3535
    • Liu, K.1    Surendhran, K.2    Nothwehr, S.F.3    Graham, T.R.4
  • 20
    • 79960742369 scopus 로고    scopus 로고
    • Endocytic sorting of transmembrane protein cargo
    • Kelly BT, Owen DJ. 2011. Endocytic sorting of transmembrane protein cargo. Curr. Opin. Cell Biol. 23:404-412. http://dx.doi.org/10.1016/j.ceb. 2011.03.004.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 404-412
    • Kelly, B.T.1    Owen, D.J.2
  • 21
    • 77955052751 scopus 로고    scopus 로고
    • Interplay of proteins and lipids in generating membrane curvature
    • Graham TR, Kozlov MM. 2010. Interplay of proteins and lipids in generating membrane curvature. Curr. Opin. Cell Biol. 22:430-436. http://dx. doi.org/10.1016/j.ceb.2010.05.002.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 430-436
    • Graham, T.R.1    Kozlov, M.M.2
  • 23
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • In Fink GR (ed), Academic Press, Inc., San Diego, CA
    • Guthrie C. 1991. Guide to yeast genetics and molecular biology. In Fink GR (ed), Methods in enzymology, vol 194, p 21-37. Academic Press, Inc., San Diego, CA.
    • (1991) Methods in enzymology , vol.194 , pp. 21-37
    • Guthrie, C.1
  • 24
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/ single-stranded carrier DNA/polyethylene glycol method
    • Gietz RD, Woods RA. 2002. Transformation of yeast by lithium acetate/ single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350:87-96. http://dx.doi.org/10.1016/S0076-6879(02)50957-5.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 25
    • 0026703547 scopus 로고
    • A simple and efficient procedure for transformation of yeasts
    • Elble R. 1992. A simple and efficient procedure for transformation of yeasts. Biotechniques 13:18-20.
    • (1992) Biotechniques , vol.13 , pp. 18-20
    • Elble, R.1
  • 26
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine MS, McKenzie A, Demarini DJ, Shah NG, Wach A, Brachat A, Philippsen P, Pringle JR. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast 14:953-961. http://dx.doi.org/10.1002/(SICI)1097-0061(199807)14:10 953::AID-YEA293_3.3.CO;2-L.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 27
    • 84873308688 scopus 로고    scopus 로고
    • Phospholipid flippases Lem3p-Dnf1p and Lem3p-Dnf2p are involved in the sorting of the tryptophan permease Tat2p in yeast
    • Hachiro T, Yamamoto T, Nakano K, Tanaka K. 2013. Phospholipid flippases Lem3p-Dnf1p and Lem3p-Dnf2p are involved in the sorting of the tryptophan permease Tat2p in yeast. J. Biol. Chem. 288:3594-3608. http://dx.doi.org/10.1074/jbc.M112.416263.
    • (2013) J. Biol. Chem. , vol.288 , pp. 3594-3608
    • Hachiro, T.1    Yamamoto, T.2    Nakano, K.3    Tanaka, K.4
  • 28
    • 0032873415 scopus 로고    scopus 로고
    • Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae
    • Goldstein AL, McCusker JH. 1999. Three new dominant drug resistance cassettes for gene disruption in Saccharomyces cerevisiae. Yeast 15:1541-1553. http://dx.doi.org/10.1002/(SICI)1097-0061(199910)15:14 1541:: AID-YEA476_3.0.CO;2-K.
    • (1999) Yeast , vol.15 , pp. 1541-1553
    • Goldstein, A.L.1    McCusker, J.H.2
  • 29
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung T, Gilbert GE, Shi J, Silvius J, Kapus A, Grinstein S. 2008. Membrane phosphatidylserine regulates surface charge and protein localization. Science 319:210-213. http://dx.doi.org/10.1126/science.1152066.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 30
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59. http://dx.doi.org/10.1016/0378-1119(89)90358-2.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 0023615620 scopus 로고
    • Plasmid construction by homologous recombination in yeast
    • Ma H, Kunes S, Schatz PJ, Botstein D. 1987. Plasmid construction by homologous recombination in yeast. Gene 58:201-216. http://dx.doi.org /10.1016/0378-1119(87)90376-3.
    • (1987) Gene , vol.58 , pp. 201-216
    • Ma, H.1    Kunes, S.2    Schatz, P.J.3    Botstein, D.4
  • 32
    • 0018608548 scopus 로고
    • Sterile host yeasts (SHY): A eukaryotic system of biological containment for recombinant DNA experiments
    • Botstein D, Falco SC, Stewart SE, Brennan M, Scherer S, Stinchcomb DT, Struhl K, Davis RW. 1979. Sterile host yeasts (SHY): a eukaryotic system of biological containment for recombinant DNA experiments. Gene 8:17-24. http://dx.doi.org/10.1016/0378-1119(79)90004-0.
    • (1979) Gene , vol.8 , pp. 17-24
    • Botstein, D.1    Falco, S.C.2    Stewart, S.E.3    Brennan, M.4    Scherer, S.5    Stinchcomb, D.T.6    Struhl, K.7    Davis, R.W.8
  • 33
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh EG, Dyer WJ. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917. http://dx.doi.org/10. 1139/o59-099.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 34
    • 37049010139 scopus 로고    scopus 로고
    • Membrane-active compounds activate the transcription factors Pdr1 and Pdr3 connecting pleiotropic drug resistance and membrane lipid homeostasis in Saccharomyces cerevisiae
    • Schüller C, Mamnun YM, Wolfger H, Rockwell N, Thorner J, Kuchler K. 2007. Membrane-active compounds activate the transcription factors Pdr1 and Pdr3 connecting pleiotropic drug resistance and membrane lipid homeostasis in Saccharomyces cerevisiae. Mol. Biol. Cell 18:4932-4944. http://dx.doi.org/10.1091/mbc.E07-06-0610.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4932-4944
    • Schüller, C.1    Mamnun, Y.M.2    Wolfger, H.3    Rockwell, N.4    Thorner, J.5    Kuchler, K.6
  • 35
    • 0037086034 scopus 로고    scopus 로고
    • Phospholipid composition of cell-derived microparticles determined by onedimensional high-performance thin-layer chromatography
    • Weerheim AM, Kolb AM, Sturk A, Nieuwland R. 2002. Phospholipid composition of cell-derived microparticles determined by onedimensional high-performance thin-layer chromatography. Anal. Biochem. 302:191-198. http://dx.doi.org/10.1006/abio.2001.5552.
    • (2002) Anal. Biochem. , vol.302 , pp. 191-198
    • Weerheim, A.M.1    Kolb, A.M.2    Sturk, A.3    Nieuwland, R.4
  • 36
    • 44949237144 scopus 로고    scopus 로고
    • Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry
    • Nakano K, Yamamoto T, Kishimoto T, Noji T, Tanaka K. 2008. Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol. Biol. Cell 19:1783-1797. http://dx.doi.org/10.1091/mbc.E07-07-0646.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1783-1797
    • Nakano, K.1    Yamamoto, T.2    Kishimoto, T.3    Noji, T.4    Tanaka, K.5
  • 37
    • 84855791501 scopus 로고    scopus 로고
    • Involvement of Golgi-associated retrograde protein complex in the recycling of the putative Dnf aminophospholipid flippases in yeast
    • Takagi K, Iwamoto K, Kobayashi S, Horiuchi H, Fukuda R, Ohta A. 2012. Involvement of Golgi-associated retrograde protein complex in the recycling of the putative Dnf aminophospholipid flippases in yeast. Biochem. Biophys. Res. Commun. 417:490-494. http://dx.doi.org/10. 1016/j.bbrc.2011.11.147.
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 490-494
    • Takagi, K.1    Iwamoto, K.2    Kobayashi, S.3    Horiuchi, H.4    Fukuda, R.5    Ohta, A.6
  • 39
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis JC, Nichols BJ, Dhruvakumar S, Pelham HR. 1998. Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 17:113-126. http://dx.doi.org/10.1093/emboj/17.1.113.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.4
  • 40
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou S, Pelham HR. 2001. An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO J. 20:5991-5998. http://dx.doi.org/10.1093/emboj/20.21.5991.
    • (2001) EMBO J. , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 41
    • 79959457450 scopus 로고    scopus 로고
    • Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae
    • Carman GM, Han GS. 2011. Regulation of phospholipid synthesis in the yeast Saccharomyces cerevisiae. Annu. Rev. Biochem. 80:859-883. http: //dx.doi.org/10.1146/annurev-biochem-060409-092229.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 859-883
    • Carman, G.M.1    Han, G.S.2
  • 42
    • 77951710195 scopus 로고    scopus 로고
    • Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae
    • Shindiapina P, Barlowe C. 2010. Requirements for transitional endoplasmic reticulum site structure and function in Saccharomyces cerevisiae. Mol. Biol. Cell 21:1530-1545. http://dx.doi.org/10.1091/mbc.E09-07-0605.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1530-1545
    • Shindiapina, P.1    Barlowe, C.2
  • 43
    • 0021089013 scopus 로고
    • Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase
    • Letts VA, Klig LS, Bae-Lee M, Carman GM, Henry SA. 1983. Isolation of the yeast structural gene for the membrane-associated enzyme phosphatidylserine synthase. Proc. Natl. Acad. Sci. U. S. A. 80:7279-7283. http: //dx.doi.org/10.1073/pnas.80.23.7279.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 7279-7283
    • Letts, V.A.1    Klig, L.S.2    Bae-Lee, M.3    Carman, G.M.4    Henry, S.A.5
  • 44
    • 21844441146 scopus 로고    scopus 로고
    • Phosphatidylinositol biosynthesis: Biochemistry and regulation
    • Gardocki ME, Jani N, Lopes JM. 2005. Phosphatidylinositol biosynthesis: biochemistry and regulation. Biochim. Biophys. Acta 1735:89-100. http://dx.doi.org/10.1016/j.bbalip.2005.05.006.
    • (2005) Biochim. Biophys. Acta , vol.1735 , pp. 89-100
    • Gardocki, M.E.1    Jani, N.2    Lopes, J.M.3
  • 45
    • 0032577480 scopus 로고    scopus 로고
    • Scanning alanine mutagenesis of the CDP-alcohol phosphotransferase motif of Saccharomyces cerevisiae cholinephosphotransferase
    • Williams JG, McMaster CR. 1998. Scanning alanine mutagenesis of the CDP-alcohol phosphotransferase motif of Saccharomyces cerevisiae cholinephosphotransferase. J. Biol. Chem. 273:13482-13487. http://dx.doi.org /10.1074/jbc.273.22.13482.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13482-13487
    • Williams, J.G.1    McMaster, C.R.2
  • 46
    • 27444446738 scopus 로고    scopus 로고
    • Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine and cardiolipin biosynthetic pathways in Saccharomyces cerevisiae
    • Gohil VM, Thompson MN, Greenberg ML. 2005. Synthetic lethal interaction of the mitochondrial phosphatidylethanolamine and cardiolipin biosynthetic pathways in Saccharomyces cerevisiae. J. Biol. Chem. 280: 35410-35416. http://dx.doi.org/10.1074/jbc.M505478200.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35410-35416
    • Gohil, V.M.1    Thompson, M.N.2    Greenberg, M.L.3
  • 47
    • 84856137855 scopus 로고    scopus 로고
    • Phosphatidylserine is polarized and required for proper Cdc42 localization and for development of cell polarity
    • Fairn GD, Hermansson M, Somerharju P, Grinstein S. 2011. Phosphatidylserine is polarized and required for proper Cdc42 localization and for development of cell polarity. Nat. Cell Biol. 13:1424-1430. http://dx.doi. org/10.1038/ncb2351.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1424-1430
    • Fairn, G.D.1    Hermansson, M.2    Somerharju, P.3    Grinstein, S.4
  • 48
    • 79960279832 scopus 로고    scopus 로고
    • Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding
    • Pranke IM, Morello V, Bigay J, Gibson K, Verbavatz JM, Antonny B, Jackson CL. 2011. Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding. J. Cell Biol. 194:89-103. http://dx.doi.org/10.1083/jcb.201011118.
    • (2011) J. Cell Biol. , vol.194 , pp. 89-103
    • Pranke, I.M.1    Morello, V.2    Bigay, J.3    Gibson, K.4    Verbavatz, J.M.5    Antonny, B.6    Jackson, C.L.7
  • 49
    • 0018940962 scopus 로고
    • Yeast mutant defective in phosphatidylserine synthesis
    • Atkinson K, Fogel S, Henry SA. 1980. Yeast mutant defective in phosphatidylserine synthesis. J. Biol. Chem. 255:6653-6661.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6653-6661
    • Atkinson, K.1    Fogel, S.2    Henry, S.A.3
  • 50
    • 33748323071 scopus 로고    scopus 로고
    • Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p
    • Costaguta G, Duncan MC, Fernández GE, Huang GH, Payne GS. 2006. Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p. Mol. Biol. Cell 17:3907-3920. http://dx.doi.org/10.1091/mbc.E06-05-0410.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3907-3920
    • Costaguta, G.1    Duncan, M.C.2    Fernández, G.E.3    Huang, G.H.4    Payne, G.S.5
  • 51
    • 0027422574 scopus 로고
    • Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele
    • Trotter PJ, Pedretti J, Voelker DR. 1993. Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation of mutants, cloning of the gene, and creation of a null allele. J. Biol. Chem. 268:21416-21424.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21416-21424
    • Trotter, P.J.1    Pedretti, J.2    Voelker, D.R.3
  • 52
    • 0027423244 scopus 로고
    • Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant
    • Clancey CJ, Chang SC, Dowhan W. 1993. Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from Saccharomyces cerevisiae by complementation of an Escherichia coli mutant. J. Biol. Chem. 268: 24580-24590.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24580-24590
    • Clancey, C.J.1    Chang, S.C.2    Dowhan, W.3
  • 53
    • 76049118071 scopus 로고    scopus 로고
    • Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance
    • Gulshan K, Shahi P, Moye-Rowley WS. 2010. Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance. Mol. Biol. Cell 21:443-455. http://dx.doi.org/10.1091/mbc. E09-06-0519.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 443-455
    • Gulshan, K.1    Shahi, P.2    Moye-Rowley, W.S.3
  • 54
    • 0028932671 scopus 로고
    • Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae
    • Trotter PJ, Voelker DR. 1995. Identification of a non-mitochondrial phosphatidylserine decarboxylase activity (PSD2) in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 270:6062-6070. http://dx.doi.org/10.1074 /jbc.270.11.6062.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6062-6070
    • Trotter, P.J.1    Voelker, D.R.2
  • 55
    • 0030671394 scopus 로고    scopus 로고
    • The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase
    • Saba JD, Nara F, Bielawska A, Garrett S, Hannun YA. 1997. The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase. J. Biol. Chem. 272:26087-26090. http://dx.doi.org/10.1074/jbc.272. 42.26087.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26087-26090
    • Saba, J.D.1    Nara, F.2    Bielawska, A.3    Garrett, S.4    Hannun, Y.A.5
  • 56
    • 0035930634 scopus 로고    scopus 로고
    • Phosphatidylethanolamine has an essential role in Saccharomyces cerevisiae that is independent of its ability to form hexagonal phase structures
    • Storey MK, Clay KL, Kutateladze T, Murphy RC, Overduin M, Voelker DR. 2001. Phosphatidylethanolamine has an essential role in Saccharomyces cerevisiae that is independent of its ability to form hexagonal phase structures. J. Biol. Chem. 276:48539-48548. http://dx.doi.org/10.1074 /jbc.M109043200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48539-48548
    • Storey, M.K.1    Clay, K.L.2    Kutateladze, T.3    Murphy, R.C.4    Overduin, M.5    Voelker, D.R.6
  • 57
    • 58049203860 scopus 로고    scopus 로고
    • The putative aminophospholipid translocases, DNF1 and DNF2, are not required for 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine flip across the plasma membrane of Saccharomyces cerevisiae
    • Stevens HC, Malone L, Nichols JW. 2008. The putative aminophospholipid translocases, DNF1 and DNF2, are not required for 7-nitrobenz-2-oxa-1,3-diazol-4-yl-phosphatidylserine flip across the plasma membrane of Saccharomyces cerevisiae. J. Biol. Chem. 283:35060-35069. http://dx.doi. org/10.1074/jbc.M802379200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 35060-35069
    • Stevens, H.C.1    Malone, L.2    Nichols, J.W.3
  • 58
    • 84857129152 scopus 로고    scopus 로고
    • Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
    • Baldridge RD, Graham TR. 2012. Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases. Proc. Natl. Acad. Sci. U. S. A. 109:E290-E298. http://dx.doi.org/10.1073 /pnas.1115725109.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109
    • Baldridge, R.D.1    Graham, T.R.2
  • 60
    • 84874774910 scopus 로고    scopus 로고
    • The functions of anionic phospholipids during clathrin-mediated endocytosis site initiation and vesicle formation
    • Sun Y, Drubin DG. 2012. The functions of anionic phospholipids during clathrin-mediated endocytosis site initiation and vesicle formation. J. Cell Sci. 125:6157-6165. http://dx.doi.org/10.1242/jcs.115741.
    • (2012) J. Cell Sci. , vol.125 , pp. 6157-6165
    • Sun, Y.1    Drubin, D.G.2
  • 61
    • 28644442089 scopus 로고    scopus 로고
    • Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast
    • Kishimoto T, Yamamoto T, Tanaka K. 2005. Defects in structural integrity of ergosterol and the Cdc50p-Drs2p putative phospholipid translocase cause accumulation of endocytic membranes, onto which actin patches are assembled in yeast. Mol. Biol. Cell 16:5592-5609. http://dx.doi. org/10.1091/mbc.E05-05-0452.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5592-5609
    • Kishimoto, T.1    Yamamoto, T.2    Tanaka, K.3
  • 63
    • 79959397904 scopus 로고    scopus 로고
    • Mechanisms of membrane curvature sensing
    • Antonny B. 2011. Mechanisms of membrane curvature sensing. Annu. Rev. Biochem. 80:101-123. http://dx.doi.org/10.1146/annurev-biochem-052809-155121.
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 101-123
    • Antonny, B.1
  • 64
    • 84878600305 scopus 로고    scopus 로고
    • Identification of a second amphipathic lipid-packing sensor-like motif that contributes to Gcs1p function in the early endosome-to-TGN pathway
    • Zendeh-boodi Z, Yamamoto T, Sakane H, Tanaka K. 2013. Identification of a second amphipathic lipid-packing sensor-like motif that contributes to Gcs1p function in the early endosome-to-TGN pathway. J. Biochem. 153:573-587. http://dx.doi.org/10.1093/jb/mvt025.
    • (2013) J. Biochem. , vol.153 , pp. 573-587
    • Zendeh-boodi, Z.1    Yamamoto, T.2    Sakane, H.3    Tanaka, K.4
  • 65
    • 84884402285 scopus 로고    scopus 로고
    • Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport
    • Xu P, Baldridge RD, Chi RJ, Burd CG, Graham TR. 2013. Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport. J. Cell Biol. 202:875-886. http://dx.doi.org /10.1083/jcb.201305094.
    • (2013) J. Cell Biol. , vol.202 , pp. 875-886
    • Xu, P.1    Baldridge, R.D.2    Chi, R.J.3    Burd, C.G.4    Graham, T.R.5
  • 66
    • 77952718617 scopus 로고    scopus 로고
    • A flippase-independent function of ATP8B1, the protein affected in familial intrahepatic cholestasis type 1, is required for apical protein expression and microvillus formation in polarized epithelial cells
    • Verhulst PM, van der Velden LM, Oorschot V, van Faassen EE, Klumperman J, Houwen RH, Pomorski TG, Holthuis JC, Klomp LW. 2010. A flippase-independent function of ATP8B1, the protein affected in familial intrahepatic cholestasis type 1, is required for apical protein expression and microvillus formation in polarized epithelial cells. Hepatology 51: 2049-2060. http://dx.doi.org/10.1002/hep.23586.
    • (2010) Hepatology , vol.51 , pp. 2049-2060
    • Verhulst, P.M.1    van der Velden, L.M.2    Oorschot, V.3    van Faassen, E.E.4    Klumperman, J.5    Houwen, R.H.6    Pomorski, T.G.7    Holthuis, J.C.8    Klomp, L.W.9
  • 67
    • 33646054255 scopus 로고    scopus 로고
    • Mutational analysis of the Lem3p-Dnf1p putative phospholipidtranslocating P-type ATPase reveals novel regulatory roles for Lem3p and a carboxyl-terminal region of Dnf1p independent of the phospholipidtranslocating activity of Dnf1p in yeast
    • Noji T, Yamamoto T, Saito K, Fujimura-Kamada K, Kondo S, Tanaka K. 2006. Mutational analysis of the Lem3p-Dnf1p putative phospholipidtranslocating P-type ATPase reveals novel regulatory roles for Lem3p and a carboxyl-terminal region of Dnf1p independent of the phospholipidtranslocating activity of Dnf1p in yeast. Biochem. Biophys. Res. Commun. 344:323-331. http://dx.doi.org/10.1016/j.bbrc.2006.03.095.
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 323-331
    • Noji, T.1    Yamamoto, T.2    Saito, K.3    Fujimura-Kamada, K.4    Kondo, S.5    Tanaka, K.6
  • 68
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski RS, Hieter P. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 69
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz RD, Sugino A. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534. http://dx.doi.org/10.1016/0378-1119(88)90185-0.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.