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Volumn 128, Issue 11, 2015, Pages 2021-2032

Inner workings and biological impact of phospholipid flippases

Author keywords

Flippase; Golgi complex; Lipid asymmetry; P type ATPase; Phosphatidylserine; Vesicular transport

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CATION; CLATHRIN; MEMBRANE LIPID; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SPHINGOLIPID; STEROL; PHOSPHOLIPID TRANSFER PROTEIN;

EID: 84930813794     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.102715     Document Type: Note
Times cited : (60)

References (127)
  • 1
    • 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. and Holthuis, J. C. M. (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.
    • (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.M.5
  • 2
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen, K. B. and Palmgren, M. G. (1998). Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101.
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 3
    • 0037938686 scopus 로고    scopus 로고
    • Aminophospholipid asymmetry: a matter of life and death
    • Balasubramanian, K. and Schroit, A. J. (2003). Aminophospholipid asymmetry: a matter of life and death. Annu. Rev. Physiol. 65, 701-734.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 701-734
    • Balasubramanian, K.1    Schroit, A.J.2
  • 4
    • 84857129152 scopus 로고    scopus 로고
    • Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases
    • Baldridge, R. D. and Graham, T. R. (2012). Identification of residues defining phospholipid flippase substrate specificity of type IV P-type ATPases. Proc. Natl. Acad. Sci. USA 109, E290-E298.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E290-E298
    • Baldridge, R.D.1    Graham, T.R.2
  • 5
    • 84873113579 scopus 로고    scopus 로고
    • Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases
    • Baldridge, R. D. and Graham, T. R. (2013). Two-gate mechanism for phospholipid selection and transport by type IV P-type ATPases. Proc. Natl. Acad. Sci. USA 110, E358-E367.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. E358-E367
    • Baldridge, R.D.1    Graham, T.R.2
  • 6
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia, R. and Munro, S. (2005). Organelle identity and the signposts for membrane traffic. Nature 438, 597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 7
    • 84860501617 scopus 로고    scopus 로고
    • Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis
    • Berchtold, D., Piccolis, M., Chiaruttini, N., Riezman, I., Riezman, H., Roux, A., Walther, T. C. and Loewith, R. (2012). Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis. Nat. Cell Biol. 14, 542-547.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 542-547
    • Berchtold, D.1    Piccolis, M.2    Chiaruttini, N.3    Riezman, I.4    Riezman, H.5    Roux, A.6    Walther, T.C.7    Loewith, R.8
  • 8
    • 84869040414 scopus 로고    scopus 로고
    • Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity
    • Bigay, J. and Antonny, B. (2012). Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity. Dev. Cell 23, 886-895.
    • (2012) Dev. Cell , vol.23 , pp. 886-895
    • Bigay, J.1    Antonny, B.2
  • 9
    • 0018730505 scopus 로고
    • ATP-induced endocytosis in human erythrocyte ghosts. Characterization of the process and isolation of the endocytosed vesicles
    • Birchmeier, W., Lanz, J. H., Winterhalter, K. H. and Conrad, M. J. (1979). ATP-induced endocytosis in human erythrocyte ghosts. Characterization of the process and isolation of the endocytosed vesicles. J. Biol. Chem. 254, 9298-9304.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9298-9304
    • Birchmeier, W.1    Lanz, J.H.2    Winterhalter, K.H.3    Conrad, M.J.4
  • 10
    • 0022413533 scopus 로고
    • Assembly of the endoplasmic reticulum phospholipid bilayer: the phosphatidylcholine transporter
    • Bishop, W. R. and Bell, R. M. (1985). Assembly of the endoplasmic reticulum phospholipid bilayer: the phosphatidylcholine transporter. Cell 42, 51-60.
    • (1985) Cell , vol.42 , pp. 51-60
    • Bishop, W.R.1    Bell, R.M.2
  • 11
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A. and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 12
    • 78650357423 scopus 로고    scopus 로고
    • CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery
    • Bryde, S., Hennrich, H., Verhulst, P. M., Devaux, P. F., Lenoir, G. and Holthuis, J. C. M. (2010). CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery. J. Biol. Chem. 285, 40562-40572.
    • (2010) J. Biol. Chem. , vol.285 , pp. 40562-40572
    • Bryde, S.1    Hennrich, H.2    Verhulst, P.M.3    Devaux, P.F.4    Lenoir, G.5    Holthuis, J.C.M.6
  • 13
    • 28044433872 scopus 로고    scopus 로고
    • Two tail-anchored protein variants, differing in transmembrane domain length and intracellular sorting, interact differently with lipids
    • Ceppi, P., Colombo, S., Francolini, M., Raimondo, F., Borgese, N. and Masserini, M. (2005). Two tail-anchored protein variants, differing in transmembrane domain length and intracellular sorting, interact differently with lipids. Proc. Natl. Acad. Sci. USA 102, 16269-16274.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16269-16274
    • Ceppi, P.1    Colombo, S.2    Francolini, M.3    Raimondo, F.4    Borgese, N.5    Masserini, M.6
  • 15
    • 0033552605 scopus 로고    scopus 로고
    • Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function
    • Chen, C. Y., Ingram, M. F., Rosal, P. H. and Graham, T. R. (1999). Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J. Cell Biol. 147, 1223-1236.
    • (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
  • 16
    • 33749531732 scopus 로고    scopus 로고
    • Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane
    • Chen, S., Wang, J., Muthusamy, B. P., Liu, K., Zare, S., Andersen, R. J. and Graham, T. R. (2006). Roles for the Drs2p-Cdc50p complex in protein transport and phosphatidylserine asymmetry of the yeast plasma membrane. Traffic 7, 1503-1517.
    • (2006) Traffic , vol.7 , pp. 1503-1517
    • Chen, S.1    Wang, J.2    Muthusamy, B.P.3    Liu, K.4    Zare, S.5    Andersen, R.J.6    Graham, T.R.7
  • 17
    • 79953056647 scopus 로고    scopus 로고
    • Endocytic sorting and recycling require membrane phosphatidylserine asymmetry maintained by TAT-1/CHAT-1
    • Chen, B., Jiang, Y., Zeng, S., Yan, J., Li, X., Zhang, Y., Zou, W. and Wang, X. (2010). Endocytic sorting and recycling require membrane phosphatidylserine asymmetry maintained by TAT-1/CHAT-1. PLoS Genet. 6, e1001235.
    • (2010) PLoS Genet. , vol.6
    • Chen, B.1    Jiang, Y.2    Zeng, S.3    Yan, J.4    Li, X.5    Zhang, Y.6    Zou, W.7    Wang, X.8
  • 18
    • 79955763752 scopus 로고    scopus 로고
    • Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2
    • Coleman, J. A. and Molday, R. S. (2011). Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2. J. Biol. Chem. 286, 17205-17216.
    • (2011) J. Biol. Chem. , vol.286 , pp. 17205-17216
    • Coleman, J.A.1    Molday, R.S.2
  • 19
    • 70450242726 scopus 로고    scopus 로고
    • Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes
    • Coleman, J. A., Kwok, M. C. M. and Molday, R. S. (2009). Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes. J. Biol. Chem. 284, 32670-32679.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32670-32679
    • Coleman, J.A.1    Kwok, M.C.M.2    Molday, R.S.3
  • 20
    • 84857136080 scopus 로고    scopus 로고
    • Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2
    • Coleman, J. A., Vestergaard, A. L., Molday, R. S., Vilsen, B. and Andersen, J. P. (2012). Critical role of a transmembrane lysine in aminophospholipid transport by mammalian photoreceptor P4-ATPase ATP8A2. Proc. Natl. Acad. Sci. USA 109, 1449-1454.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1449-1454
    • Coleman, J.A.1    Vestergaard, A.L.2    Molday, R.S.3    Vilsen, B.4    Andersen, J.P.5
  • 21
    • 84896898469 scopus 로고    scopus 로고
    • Phospholipid flippase ATP8A2 is required for normal visual and auditory function and photoreceptor and spiral ganglion cell survival
    • Coleman, J. A., Zhu, X., Djajadi, H. R., Molday, L. L., Smith, R. S., Libby, R. T., John, S. W. M. and Molday, R. S. (2014). Phospholipid flippase ATP8A2 is required for normal visual and auditory function and photoreceptor and spiral ganglion cell survival. J. Cell Sci. 127, 1138-1149.
    • (2014) J. Cell Sci. , vol.127 , pp. 1138-1149
    • Coleman, J.A.1    Zhu, X.2    Djajadi, H.R.3    Molday, L.L.4    Smith, R.S.5    Libby, R.T.6    John, S.W.M.7    Molday, R.S.8
  • 22
    • 42549152012 scopus 로고    scopus 로고
    • Role of C. elegans TAT-1 protein in maintaining plasma membrane phosphatidylserine asymmetry
    • Darland-Ransom, M., Wang, X., Sun, C. L., Mapes, J., Gengyo-Ando, K., Mitani, S. and Xue, D. (2008). Role of C. elegans TAT-1 protein in maintaining plasma membrane phosphatidylserine asymmetry. Science 320, 528-531.
    • (2008) Science , vol.320 , pp. 528-531
    • Darland-Ransom, M.1    Wang, X.2    Sun, C.L.3    Mapes, J.4    Gengyo-Ando, K.5    Mitani, S.6    Xue, D.7
  • 23
    • 84863419997 scopus 로고    scopus 로고
    • Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity
    • Das, A., Slaughter, B. D., Unruh, J. R., Bradford, W. D., Alexander, R., Rubinstein, B. and Li, R. (2012). Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity. Nat. Cell Biol. 14, 304-310.
    • (2012) Nat. Cell Biol. , vol.14 , pp. 304-310
    • Das, A.1    Slaughter, B.D.2    Unruh, J.R.3    Bradford, W.D.4    Alexander, R.5    Rubinstein, B.6    Li, R.7
  • 25
    • 63649094705 scopus 로고    scopus 로고
    • Functional significance of E2 state stabilization by specific alpha/beta-subunit interactions of Na, K- and H, K-ATPase
    • Dürr, K. L., Tavraz, N. N., Dempski, R. E., Bamberg, E. and Friedrich, T. (2009). Functional significance of E2 state stabilization by specific alpha/beta-subunit interactions of Na, K- and H, K-ATPase. J. Biol. Chem. 284, 3842-3854.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3842-3854
    • Dürr, K.L.1    Tavraz, N.N.2    Dempski, R.E.3    Bamberg, E.4    Friedrich, T.5
  • 26
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages
    • Fadok, V. A., Voelker, D. R., Campbell, P. A., Cohen, J. J., Bratton, D. L. and Henson, P.M. (1992). Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol. 148, 2207-2216.
    • (1992) J. Immunol. , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.R.2    Campbell, P.A.3    Cohen, J.J.4    Bratton, D.L.5    Henson, P.M.6
  • 28
    • 0032896265 scopus 로고    scopus 로고
    • Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells
    • Farge, E., Ojcius, D. M., Subtil, A. and Dautry-Varsat, A. (1999). Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells. Am. J. Physiol. 276, C725-C733.
    • (1999) Am. J. Physiol. , vol.276 , pp. C725-C733
    • Farge, E.1    Ojcius, D.M.2    Subtil, A.3    Dautry-Varsat, A.4
  • 30
    • 58149352846 scopus 로고    scopus 로고
    • Functional roles of Na, K-ATPase subunits
    • Geering, K. (2008). Functional roles of Na, K-ATPase subunits. Curr. Opin. Nephrol. Hypertens. 17, 526-532.
    • (2008) Curr. Opin. Nephrol. Hypertens. , vol.17 , pp. 526-532
    • Geering, K.1
  • 31
    • 33645294005 scopus 로고    scopus 로고
    • A P-type ATPase required for rice blast disease and induction of host resistance
    • Gilbert, M. J., Thornton, C. R., Wakley, G. E. and Talbot, N. J. (2006). A P-type ATPase required for rice blast disease and induction of host resistance. Nature 440, 535-539.
    • (2006) Nature , vol.440 , pp. 535-539
    • Gilbert, M.J.1    Thornton, C.R.2    Wakley, G.E.3    Talbot, N.J.4
  • 32
    • 0034489811 scopus 로고    scopus 로고
    • Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases
    • Gomès, E., Jakobsen, M. K., Axelsen, K. B., Geisler, M. and Palmgren, M. G. (2000). Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases. Plant Cell 12, 2441-2454.
    • (2000) Plant Cell , vol.12 , pp. 2441-2454
    • Gomès, E.1    Jakobsen, M.K.2    Axelsen, K.B.3    Geisler, M.4    Palmgren, M.G.5
  • 33
    • 62449201602 scopus 로고    scopus 로고
    • Expression of Atp8b3 in murine testis and its characterization as a testis specific P-type ATPase
    • Gong, E. Y., Park, E., Lee, H. J. and Lee, K. (2009). Expression of Atp8b3 in murine testis and its characterization as a testis specific P-type ATPase. Reproduction 137, 345-351.
    • (2009) Reproduction , vol.137 , pp. 345-351
    • Gong, E.Y.1    Park, E.2    Lee, H.J.3    Lee, K.4
  • 35
    • 9644264229 scopus 로고    scopus 로고
    • Flippases and vesicle-mediated protein transport
    • Graham, T. R. (2004). Flippases and vesicle-mediated protein transport. Trends Cell Biol. 14, 670-677.
    • (2004) Trends Cell Biol. , vol.14 , pp. 670-677
    • Graham, T.R.1
  • 37
    • 84901649595 scopus 로고    scopus 로고
    • Lipid flippase modulates olfactory receptor expression and odorant sensitivity in Drosophila
    • Ha, T. S., Xia, R., Zhang, H., Jin, X. and Smith, D. P. (2014). Lipid flippase modulates olfactory receptor expression and odorant sensitivity in Drosophila. Proc. Natl. Acad. Sci. USA 111, 7831-7836.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 7831-7836
    • Ha, T.S.1    Xia, R.2    Zhang, H.3    Jin, X.4    Smith, D.P.5
  • 38
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • Holopainen, J. M., Angelova, M. I. and Kinnunen, P. K. (2000). Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys. J. 78, 830-838.
    • (2000) Biophys. J. , vol.78 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.3
  • 39
    • 84901935763 scopus 로고    scopus 로고
    • Lipid landscapes and pipelines in membrane homeostasis
    • Holthuis, J. C. M. and Menon, A. K. (2014). Lipid landscapes and pipelines in membrane homeostasis. Nature 510, 48-57.
    • (2014) Nature , vol.510 , pp. 48-57
    • Holthuis, J.C.M.1    Menon, A.K.2
  • 40
    • 75649103549 scopus 로고    scopus 로고
    • A putative P-type ATPase, Apt1, is involved in stress tolerance and virulence in Cryptococcus neoformans
    • Hu, G. and Kronstad, J. W. (2010). A putative P-type ATPase, Apt1, is involved in stress tolerance and virulence in Cryptococcus neoformans. Eukaryot. Cell 9, 74-83.
    • (2010) Eukaryot. Cell , vol.9 , pp. 74-83
    • Hu, G.1    Kronstad, J.W.2
  • 41
    • 0344443667 scopus 로고    scopus 로고
    • Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Hua, Z. and Graham, T. R. (2003). Requirement for neo1p in retrograde transport from the Golgi complex to the endoplasmic reticulum. Mol. Biol. Cell 14, 4971-4983.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4971-4983
    • Hua, Z.1    Graham, T.R.2
  • 42
    • 0036732873 scopus 로고    scopus 로고
    • An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system
    • Hua, Z., Fatheddin, P. and Graham, T. R. (2002). An essential subfamily of Drs2p-related P-type ATPases is required for protein trafficking between Golgi complex and endosomal/vacuolar system. Mol. Biol. Cell 13, 3162-3177.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3162-3177
    • Hua, Z.1    Fatheddin, P.2    Graham, T.R.3
  • 43
    • 40849113435 scopus 로고    scopus 로고
    • 2+ ATPase of cardiac sarcoplasmic reticulum: Physiological role and relevance to diseases
    • 2+ ATPase of cardiac sarcoplasmic reticulum: Physiological role and relevance to diseases. Biochem. Biophys. Res. Commun. 369, 182-187.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 182-187
    • Inesi, G.1    Prasad, A.M.2    Pilankatta, R.3
  • 44
    • 84859771332 scopus 로고    scopus 로고
    • Phosphatidylserine stimulation of Drs2p·Cdc50p lipid translocase dephosphorylation is controlled by phosphatidylinositol-4-phosphate
    • Jacquot, A., Montigny, C., Hennrich, H., Barry, R., le Maire, M., Jaxel, C., Holthuis, J., Champeil, P. and Lenoir, G. (2012). Phosphatidylserine stimulation of Drs2p·Cdc50p lipid translocase dephosphorylation is controlled by phosphatidylinositol-4-phosphate. J. Biol. Chem. 287, 13249-13261.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13249-13261
    • Jacquot, A.1    Montigny, C.2    Hennrich, H.3    Barry, R.4    le Maire, M.5    Jaxel, C.6    Holthuis, J.7    Champeil, P.8    Lenoir, G.9
  • 45
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na, K-ATPase
    • Kaplan, J. H. (2002). Biochemistry of Na, K-ATPase. Annu. Rev. Biochem. 71, 511-535.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 46
  • 47
    • 84874092269 scopus 로고    scopus 로고
    • Role for phospholipid flippase complex of ATP8A1 and CDC50A proteins in cell migration
    • Kato, U., Inadome, H., Yamamoto, M., Emoto, K., Kobayashi, T. and Umeda, M. (2013). Role for phospholipid flippase complex of ATP8A1 and CDC50A proteins in cell migration. J. Biol. Chem. 288, 4922-4934.
    • (2013) J. Biol. Chem. , vol.288 , pp. 4922-4934
    • Kato, U.1    Inadome, H.2    Yamamoto, M.3    Emoto, K.4    Kobayashi, T.5    Umeda, M.6
  • 49
    • 84885006979 scopus 로고    scopus 로고
    • Phosphatidylserine-mediated cellular signaling
    • (ed. D. G. S. Capelluto), Dordrecht: Springer
    • Kay, J. G. and Grinstein, S. (2013). Phosphatidylserine-mediated cellular signaling. In Lipid-mediated Protein Signaling (ed. D. G. S. Capelluto), pp. 177-193. Dordrecht: Springer.
    • (2013) In Lipid-mediated Protein Signaling , pp. 177-193
    • Kay, J.G.1    Grinstein, S.2
  • 50
    • 0041589300 scopus 로고    scopus 로고
    • Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane
    • Kol, M. A., van Dalen, A., de Kroon, A. I. P. M. and de Kruijff, B. (2003a). Translocation of phospholipids is facilitated by a subset of membrane-spanning proteins of the bacterial cytoplasmic membrane. J. Biol. Chem. 278, 24586-24593.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24586-24593
    • Kol, M.A.1    van Dalen, A.2    de Kroon, A.I.P.M.3    de Kruijff, B.4
  • 51
    • 0037435555 scopus 로고    scopus 로고
    • Phospholipid flop induced by transmembrane peptides in model membranes is modulated by lipid composition
    • Kol, M. A., van Laak, A. N. C., Rijkers, D. T. S., Killian, J. A., de Kroon, A. I. P. M. and de Kruijff, B. (2003b). Phospholipid flop induced by transmembrane peptides in model membranes is modulated by lipid composition. Biochemistry 42, 231-237.
    • (2003) Biochemistry , vol.42 , pp. 231-237
    • Kol, M.A.1    van Laak, A.N.C.2    Rijkers, D.T.S.3    Killian, J.A.4    de Kroon, A.I.P.M.5    de Kruijff, B.6
  • 52
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure and mechanism of P-type ATPases
    • Kühlbrandt, W. (2004). Biology, structure and mechanism of P-type ATPases. Nat. Rev. Mol. Cell Biol. 5, 282-295.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 55
    • 36549076985 scopus 로고    scopus 로고
    • On the origin of lipid asymmetry: the flip side of ion transport
    • Lenoir, G., Williamson, P. and Holthuis, J. C. (2007). On the origin of lipid asymmetry: the flip side of ion transport. Curr. Opin. Chem. Biol. 11, 654-661.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 654-661
    • Lenoir, G.1    Williamson, P.2    Holthuis, J.C.3
  • 56
    • 67650516832 scopus 로고    scopus 로고
    • Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p
    • Lenoir, G., Williamson, P., Puts, C. F. and Holthuis, J. C. M. (2009). Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p. J. Biol. Chem. 284, 17956-17967.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17956-17967
    • Lenoir, G.1    Williamson, P.2    Puts, C.F.3    Holthuis, J.C.M.4
  • 58
    • 84876565480 scopus 로고    scopus 로고
    • Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutants
    • Li, X., Chen, B., Yoshina, S., Cai, T., Yang, F., Mitani, S. and Wang, X. (2013). Inactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutants. Mol. Biol. Cell 24, 1163-1175.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1163-1175
    • Li, X.1    Chen, B.2    Yoshina, S.3    Cai, T.4    Yang, F.5    Mitani, S.6    Wang, X.7
  • 59
    • 20744432592 scopus 로고    scopus 로고
    • The sphingoid long chain base phytosphingosine activates AGC-type protein kinases in Saccharomyces cerevisiae including Ypk1, Ypk2, and Sch9
    • Liu, K., Zhang, X., Lester, R. L. and Dickson, R. C. (2005). The sphingoid long chain base phytosphingosine activates AGC-type protein kinases in Saccharomyces cerevisiae including Ypk1, Ypk2, and Sch9. J. Biol. Chem. 280, 22679-22687.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22679-22687
    • Liu, K.1    Zhang, X.2    Lester, R.L.3    Dickson, R.C.4
  • 60
    • 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, S. F. and Graham, T. R. (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.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3526-3535
    • Liu, K.1    Surendhran, K.2    Nothwehr, S.F.3    Graham, T.R.4
  • 63
    • 84859729451 scopus 로고    scopus 로고
    • A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase ALA1, localizes to the plasma membrane following association with a ß-subunit
    • López-Marqués, R. L., Poulsen, L. R. and Palmgren, M. G. (2012). A putative plant aminophospholipid flippase, the Arabidopsis P4 ATPase ALA1, localizes to the plasma membrane following association with a ß-subunit. PLoS ONE 7, e33042.
    • (2012) PLoS ONE , vol.7
    • López-Marqués, R.L.1    Poulsen, L.R.2    Palmgren, M.G.3
  • 64
    • 0027236527 scopus 로고
    • An essential role for the extracellular domain of the Na, K-ATPase beta-subunit in cation occlusion
    • Lutsenko, S. and Kaplan, J. H. (1993). An essential role for the extracellular domain of the Na, K-ATPase beta-subunit in cation occlusion. Biochemistry 32, 6737-6743.
    • (1993) Biochemistry , vol.32 , pp. 6737-6743
    • Lutsenko, S.1    Kaplan, J.H.2
  • 65
    • 54449086519 scopus 로고    scopus 로고
    • An unexpectedly high degree of specialization and a widespread involvement in sterol metabolism among the C. elegans putative aminophospholipid translocases
    • Lyssenko, N. N., Miteva, Y., Gilroy, S., Hanna-Rose, W. and Schlegel, R. A. (2008). An unexpectedly high degree of specialization and a widespread involvement in sterol metabolism among the C. elegans putative aminophospholipid translocases. BMC Dev. Biol. 8, 96.
    • (2008) BMC Dev. Biol. , vol.8 , pp. 96
    • Lyssenko, N.N.1    Miteva, Y.2    Gilroy, S.3    Hanna-Rose, W.4    Schlegel, R.A.5
  • 66
    • 84859601572 scopus 로고    scopus 로고
    • Membrane phospholipid asymmetry counters the adverse effects of sterol overloading in the Golgi membrane of Drosophila
    • Ma, Z., Liu, Z. and Huang, X. (2012). Membrane phospholipid asymmetry counters the adverse effects of sterol overloading in the Golgi membrane of Drosophila. Genetics 190, 1299-1308.
    • (2012) Genetics , vol.190 , pp. 1299-1308
    • Ma, Z.1    Liu, Z.2    Huang, X.3
  • 67
    • 84884210112 scopus 로고    scopus 로고
    • Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins
    • Maeda, K., Anand, K., Chiapparino, A., Kumar, A., Poletto, M., Kaksonen, M. and Gavin, A. C. (2013). Interactome map uncovers phosphatidylserine transport by oxysterol-binding proteins. Nature 501, 257-261.
    • (2013) Nature , vol.501 , pp. 257-261
    • Maeda, K.1    Anand, K.2    Chiapparino, A.3    Kumar, A.4    Poletto, M.5    Kaksonen, M.6    Gavin, A.C.7
  • 69
    • 84907862101 scopus 로고    scopus 로고
    • Asymmetric distribution of phosphatidylserine is generated in the absence of phospholipid flippases in Saccharomyces cerevisiae
    • Mioka, T., Fujimura-Kamada, K. and Tanaka, K. (2014). Asymmetric distribution of phosphatidylserine is generated in the absence of phospholipid flippases in Saccharomyces cerevisiae. Microbiology Open 3, 803-821.
    • (2014) Microbiology Open , vol.3 , pp. 803-821
    • Mioka, T.1    Fujimura-Kamada, K.2    Tanaka, K.3
  • 71
    • 0028221363 scopus 로고
    • Incorporation of phospholipid analogues into the plasma membrane affects ATP-induced vesiculation of human erythrocyte ghosts
    • Müller, P., Pomorski, T. and Herrmann, A. (1994). Incorporation of phospholipid analogues into the plasma membrane affects ATP-induced vesiculation of human erythrocyte ghosts. Biochem. Biophys. Res. Commun. 199, 881-887.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 881-887
    • Müller, P.1    Pomorski, T.2    Herrmann, A.3
  • 72
    • 22044446534 scopus 로고    scopus 로고
    • The Golgi apparatus: defining the identity of Golgi membranes
    • Munro, S. (2005). The Golgi apparatus: defining the identity of Golgi membranes. Curr. Opin. Cell Biol. 17, 395-401.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 395-401
    • Munro, S.1
  • 73
    • 67449116832 scopus 로고    scopus 로고
    • Control of protein and sterol trafficking by antagonistic activities of a type IV P-type ATPase and oxysterol binding protein homologue
    • Muthusamy, B. P., Raychaudhuri, S., Natarajan, P., Abe, F., Liu, K., Prinz, W. A. and Graham, T. R. (2009). Control of protein and sterol trafficking by antagonistic activities of a type IV P-type ATPase and oxysterol binding protein homologue. Mo. Biol. Cell 20, 2920-2931.
    • (2009) Mo. Biol. Cell , vol.20 , pp. 2920-2931
    • Muthusamy, B.P.1    Raychaudhuri, S.2    Natarajan, P.3    Abe, F.4    Liu, K.5    Prinz, W.A.6    Graham, T.R.7
  • 74
    • 44949237144 scopus 로고    scopus 로고
    • Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry
    • Nakano, K., Yamamoto, T., Kishimoto, T., Noji, T. and Tanaka, K. (2008). Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid asymmetry. Mol. Bio. Cell 19, 1783-1797.
    • (2008) Mol. Bio. Cell , vol.19 , pp. 1783-1797
    • Nakano, K.1    Yamamoto, T.2    Kishimoto, T.3    Noji, T.4    Tanaka, K.5
  • 75
    • 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. and Graham, T. R. (2004). Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc. Natl. Acad. Sci. USA 101, 10614-10619.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10614-10619
    • Natarajan, P.1    Wang, J.2    Hua, Z.3    Graham, T.R.4
  • 77
    • 0028341564 scopus 로고
    • Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes
    • Newton, A. C. and Keranen, L. M. (1994). Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes. Biochemistry 33, 6651-6658.
    • (1994) Biochemistry , vol.33 , pp. 6651-6658
    • Newton, A.C.1    Keranen, L.M.2
  • 78
    • 81055157713 scopus 로고    scopus 로고
    • Caenorhabditis elegans numb inhibits endocytic recycling by binding TAT-1 aminophospholipid translocase
    • Nilsson, L., Jonsson, E. and Tuck, S. (2011). Caenorhabditis elegans numb inhibits endocytic recycling by binding TAT-1 aminophospholipid translocase. Traffic 12, 1839-1849.
    • (2011) Traffic , vol.12 , pp. 1839-1849
    • Nilsson, L.1    Jonsson, E.2    Tuck, S.3
  • 79
    • 84874110716 scopus 로고    scopus 로고
    • Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion
    • Onat, O. E., Gulsuner, S., Bilguvar, K., Nazli Basak, A., Topaloglu, H., Tan, M., Tan, U., Gunel, M. and Ozcelik, T. (2013). Missense mutation in the ATPase, aminophospholipid transporter protein ATP8A2 is associated with cerebellar atrophy and quadrupedal locomotion. Eur. J. Hum. Genet. 21, 281-285.
    • (2013) Eur. J. Hum. Genet. , vol.21 , pp. 281-285
    • Onat, O.E.1    Gulsuner, S.2    Bilguvar, K.3    Nazli Basak, A.4    Topaloglu, H.5    Tan, M.6    Tan, U.7    Gunel, M.8    Ozcelik, T.9
  • 80
    • 0018369993 scopus 로고
    • Lipid asymmetry in membranes
    • Op den Kamp, J. A. F. (1979). Lipid asymmetry in membranes. Annu. Rev. Biochem. 48, 47-71.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 47-71
    • Op den Kamp, J.A.F.1
  • 83
    • 65649087129 scopus 로고    scopus 로고
    • Activity of the bile salt export pump (ABCB11) is critically dependent on canalicular membrane cholesterol content
    • Paulusma, C. C., de Waart, D. R., Kunne, C., Mok, K. S. and Elferink, R. P. J. O. (2009). Activity of the bile salt export pump (ABCB11) is critically dependent on canalicular membrane cholesterol content. J. Biol. Chem. 284, 9947-9954.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9947-9954
    • Paulusma, C.C.1    de Waart, D.R.2    Kunne, C.3    Mok, K.S.4    Elferink, R.P.J.O.5
  • 84
    • 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, P. F., van Meer, G. and Holthuis, J. C. M. (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.
    • (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.M.6
  • 85
    • 48249091728 scopus 로고    scopus 로고
    • The Arabidopsis P4-ATPase ALA3 localizes to the golgi and requires a beta-subunit to function in lipid translocation and secretory vesicle formation
    • Poulsen, L. R., López-Marqués, R. L., McDowell, S. C., Okkeri, J., Licht, D., Schulz, A., Pomorski, T., Harper, J. F. and Palmgren, M. G. (2008). The Arabidopsis P4-ATPase ALA3 localizes to the golgi and requires a beta-subunit to function in lipid translocation and secretory vesicle formation. Plant Cell 20, 658-676.
    • (2008) Plant Cell , vol.20 , pp. 658-676
    • Poulsen, L.R.1    López-Marqués, R.L.2    McDowell, S.C.3    Okkeri, J.4    Licht, D.5    Schulz, A.6    Pomorski, T.7    Harper, J.F.8    Palmgren, M.G.9
  • 86
    • 67649276931 scopus 로고    scopus 로고
    • Mechanism and significance of P4 ATPase-catalyzed lipid transport: lessons from a Na+/K+-pump
    • Puts, C. F. and Holthuis, J. C. M. (2009). Mechanism and significance of P4 ATPase-catalyzed lipid transport: lessons from a Na+/K+-pump. Biochim. Biophys. Acta 1791, 603-611.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 603-611
    • Puts, C.F.1    Holthuis, J.C.M.2
  • 89
    • 33845987531 scopus 로고    scopus 로고
    • Uptake and utilization of lysophosphatidylethanolamine by Saccharomyces cerevisiae
    • Riekhof, W. R. and Voelker, D. R. (2006). Uptake and utilization of lysophosphatidylethanolamine by Saccharomyces cerevisiae. J. Biol. Chem. 281, 36588-36596.
    • (2006) J. Biol. Chem. , vol.281 , pp. 36588-36596
    • Riekhof, W.R.1    Voelker, D.R.2
  • 90
    • 82755163564 scopus 로고    scopus 로고
    • Protein kinase Ypk1 phosphorylates regulatory proteins Orm1 and Orm2 to control sphingolipid homeostasis in Saccharomyces cerevisiae
    • Roelants, F. M., Breslow, D. K., Muir, A., Weissman, J. S. and Thorner, J. (2011). Protein kinase Ypk1 phosphorylates regulatory proteins Orm1 and Orm2 to control sphingolipid homeostasis in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 108, 19222-19227.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 19222-19227
    • Roelants, F.M.1    Breslow, D.K.2    Muir, A.3    Weissman, J.S.4    Thorner, J.5
  • 91
    • 58149199541 scopus 로고    scopus 로고
    • The C. elegans P4-ATPase TAT-1 regulates lysosome biogenesis and endocytosis
    • Ruaud, A. F., Nilsson, L., Richard, F., Larsen, M. K., Bessereau, J. L. and Tuck, S. (2009). The C. elegans P4-ATPase TAT-1 regulates lysosome biogenesis and endocytosis. Traffic 10, 88-100.
    • (2009) Traffic , vol.10 , pp. 88-100
    • Ruaud, A.F.1    Nilsson, L.2    Richard, F.3    Larsen, M.K.4    Bessereau, J.L.5    Tuck, S.6
  • 92
    • 3042728119 scopus 로고    scopus 로고
    • Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae
    • Saito, K., Fujimura-Kamada, K., Furuta, N., Kato, U., Umeda, M. and Tanaka, K. (2004). Cdc50p, a protein required for polarized growth, associates with the Drs2p P-type ATPase implicated in phospholipid translocation in Saccharomyces cerevisiae. Mol. Biol. Cell 15, 3418-3432.
    • (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
  • 93
    • 35548947966 scopus 로고    scopus 로고
    • Transbilayer phospholipid flipping regulates Cdc42p signaling during polarized cell growth via Rga GTPase-activating proteins
    • Saito, K., Fujimura-Kamada, K., Hanamatsu, H., Kato, U., Umeda, M., Kozminski, K. G. and Tanaka, K. (2007). Transbilayer phospholipid flipping regulates Cdc42p signaling during polarized cell growth via Rga GTPase-activating proteins. Dev. Cell 13, 743-751.
    • (2007) Dev. Cell , vol.13 , pp. 743-751
    • Saito, K.1    Fujimura-Kamada, K.2    Hanamatsu, H.3    Kato, U.4    Umeda, M.5    Kozminski, K.G.6    Tanaka, K.7
  • 94
    • 70149098254 scopus 로고    scopus 로고
    • P-type ATPase TAT-2 negatively regulates monomethyl branched-chain fatty acid mediated function in post-embryonic growth and development in C. elegans
    • Seamen, E., Blanchette, J. M. and Han, M. (2009). P-type ATPase TAT-2 negatively regulates monomethyl branched-chain fatty acid mediated function in post-embryonic growth and development in C. elegans. PLoS Genet. 5, e1000589.
    • (2009) PLoS Genet. , vol.5
    • Seamen, E.1    Blanchette, J.M.2    Han, M.3
  • 95
    • 84901849205 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure
    • Segawa, K., Kurata, S., Yanagihashi, Y., Brummelkamp, T. R., Matsuda, F. and Nagata, S. (2014). Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure. Science 344, 1164-1168.
    • (2014) Science , vol.344 , pp. 1164-1168
    • Segawa, K.1    Kurata, S.2    Yanagihashi, Y.3    Brummelkamp, T.R.4    Matsuda, F.5    Nagata, S.6
  • 96
    • 0021185107 scopus 로고
    • Asymmetric lipid fluidity in human erythrocyte membrane: new spin-label evidence
    • Seigneuret, M., Zachowski, A., Hermann, A. and Devaux, P. F. (1984). Asymmetric lipid fluidity in human erythrocyte membrane: new spin-label evidence. Biochemistry 23, 4271-4275.
    • (1984) Biochemistry , vol.23 , pp. 4271-4275
    • Seigneuret, M.1    Zachowski, A.2    Hermann, A.3    Devaux, P.F.4
  • 97
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe, H. J., Stevens, T. J. and Munro, S. (2010). A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 142, 158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1    Stevens, T.J.2    Munro, S.3
  • 98
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassium pump at 2.4 A resolution
    • Shinoda, T., Ogawa, H., Cornelius, F. and Toyoshima, C. (2009). Crystal structure of the sodium-potassium pump at 2.4 A resolution. Nature 459, 446-450.
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 99
    • 79956363526 scopus 로고    scopus 로고
    • X-linked cholestasis in mouse due to mutations of the P4-ATPase ATP11C
    • Siggs, O. M., Schnabl, B., Webb, B. and Beutler, B. (2011). X-linked cholestasis in mouse due to mutations of the P4-ATPase ATP11C. Proc. Natl. Acad. Sci. USA 108, 7890-7895.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7890-7895
    • Siggs, O.M.1    Schnabl, B.2    Webb, B.3    Beutler, B.4
  • 102
    • 84863650062 scopus 로고    scopus 로고
    • Outside of the box: recent news about phospholipid translocation by P4 ATPases
    • Stone, A. and Williamson, P. (2012). Outside of the box: recent news about phospholipid translocation by P4 ATPases. Journal of Chemical Biology 5, 131-136.
    • (2012) Journal of Chemical Biology , vol.5 , pp. 131-136
    • Stone, A.1    Williamson, P.2
  • 103
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki, J., Umeda, M., Sims, P. J. and Nagata, S. (2010). Calcium-dependent phospholipid scrambling by TMEM16F. Nature 468, 834-838.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1    Umeda, M.2    Sims, P.J.3    Nagata, S.4
  • 104
    • 79953221826 scopus 로고    scopus 로고
    • Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase
    • Takahashi, Y., Fujimura-Kamada, K., Kondo, S. and Tanaka, K. (2011). Isolation and characterization of novel mutations in CDC50, the non-catalytic subunit of the Drs2p phospholipid flippase. J. Biochem. 149, 423-432.
    • (2011) J. Biochem. , vol.149 , pp. 423-432
    • Takahashi, Y.1    Fujimura-Kamada, K.2    Kondo, S.3    Tanaka, K.4
  • 105
    • 80055067373 scopus 로고    scopus 로고
    • ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner
    • Takatsu, H., Baba, K., Shima, T., Umino, H., Kato, U., Umeda, M., Nakayama, K. and Shin, H.-W. (2011). ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner. J. Biol. Chem. 286, 38159-38167.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38159-38167
    • Takatsu, H.1    Baba, K.2    Shima, T.3    Umino, H.4    Kato, U.5    Umeda, M.6    Nakayama, K.7    Shin, H.-W.8
  • 106
    • 84912076652 scopus 로고    scopus 로고
    • Phospholipid flippase activities and substrate specificities of human type IV P-type ATPases localized to the plasma membrane
    • Takatsu, H., Tanaka, G., Segawa, K., Suzuki, J., Nagata, S., Nakayama, K. and Shin, H. W. (2014). Phospholipid flippase activities and substrate specificities of human type IV P-type ATPases localized to the plasma membrane. J. Biol. Chem. 289, 33543-33556.
    • (2014) J. Biol. Chem. , vol.289 , pp. 33543-33556
    • Takatsu, H.1    Tanaka, G.2    Segawa, K.3    Suzuki, J.4    Nagata, S.5    Nakayama, K.6    Shin, H.W.7
  • 107
    • 84894829344 scopus 로고    scopus 로고
    • Role of phosphatidylserine in phospholipid flippase-mediated vesicle transport in Saccharomyces cerevisiae
    • Takeda, M., Yamagami, K. and Tanaka, K. (2014). Role of phosphatidylserine in phospholipid flippase-mediated vesicle transport in Saccharomyces cerevisiae. Eukaryot. Cell 13, 363-375.
    • (2014) Eukaryot. Cell , vol.13 , pp. 363-375
    • Takeda, M.1    Yamagami, K.2    Tanaka, K.3
  • 108
    • 0029992825 scopus 로고    scopus 로고
    • A subfamily of P-type ATPases with aminophospholipid transporting activity
    • Tang, X., Halleck, M. S., Schlegel, R. A. and Williamson, P. (1996). A subfamily of P-type ATPases with aminophospholipid transporting activity. Science 272, 1495-1497.
    • (1996) Science , vol.272 , pp. 1495-1497
    • Tang, X.1    Halleck, M.S.2    Schlegel, R.A.3    Williamson, P.4
  • 109
    • 67349157973 scopus 로고    scopus 로고
    • How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane
    • Toyoshima, C. (2009). How Ca2+-ATPase pumps ions across the sarcoplasmic reticulum membrane. Biochim. Biophys. Acta 1793, 941-946.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 941-946
    • Toyoshima, C.1
  • 110
    • 3242888769 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump with a bound ATP analogue
    • Toyoshima, C. and Mizutani, T. (2004). Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535.
    • (2004) Nature , vol.430 , pp. 529-535
    • Toyoshima, C.1    Mizutani, T.2
  • 113
    • 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, P. M., van der Velden, L. M., Oorschot, V., van Faassen, E. E., Klumperman, J., Houwen, R. H., Pomorski, T. G., Holthuis, J. C. and Klomp, L. W. (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.
    • (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
  • 116
    • 1242295309 scopus 로고    scopus 로고
    • A novel aminophospholipid transporter exclusively expressed in spermatozoa is required for membrane lipid asymmetry and normal fertilization
    • Wang, L., Beserra, C. and Garbers, D. L. (2004). A novel aminophospholipid transporter exclusively expressed in spermatozoa is required for membrane lipid asymmetry and normal fertilization. Dev. Biol. 267, 203-215.
    • (2004) Dev. Biol. , vol.267 , pp. 203-215
    • Wang, L.1    Beserra, C.2    Garbers, D.L.3
  • 117
    • 34347382638 scopus 로고    scopus 로고
    • PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal
    • Wang, J., Sun, H.-Q., Macia, E., Kirchhausen, T., Watson, H., Bonifacino, J. S. and Yin, H. L. (2007). PI4P promotes the recruitment of the GGA adaptor proteins to the trans-Golgi network and regulates their recognition of the ubiquitin sorting signal. Mol. Biol. Cell 18, 2646-2655.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2646-2655
    • Wang, J.1    Sun, H.-Q.2    Macia, E.3    Kirchhausen, T.4    Watson, H.5    Bonifacino, J.S.6    Yin, H.L.7
  • 118
    • 82955227444 scopus 로고    scopus 로고
    • The P4-ATPase TAT-5 inhibits the budding of extracellular vesicles in C. elegans embryos
    • Wehman, A. M., Poggioli, C., Schweinsberg, P., Grant, B. D. and Nance, J. (2011). The P4-ATPase TAT-5 inhibits the budding of extracellular vesicles in C. elegans embryos. Curr. Biol. 21, 1951-1959.
    • (2011) Curr. Biol. , vol.21 , pp. 1951-1959
    • Wehman, A.M.1    Poggioli, C.2    Schweinsberg, P.3    Grant, B.D.4    Nance, J.5
  • 119
    • 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. and 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.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7402-7418
    • Wicky, S.1    Schwarz, H.2    Singer-Krüger, B.3
  • 120
    • 84884402285 scopus 로고    scopus 로고
    • Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport
    • Xu, P., Baldridge, R. D., Chi, R. J., Burd, C. G. and Graham, T. R. (2013). Phosphatidylserine flipping enhances membrane curvature and negative charge required for vesicular transport. J. Cell Biol. 202, 875-886.
    • (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
  • 122
    • 84904171129 scopus 로고    scopus 로고
    • Mice deficient in the putative phospholipid flippase Atp11c exhibit altered erythrocyte shape, anemia and reduced erythrocyte lifespan
    • Yabas, M., Coupland, L. A., Cromer, D., Winterberg, M., Teoh, N. C., D'Rozario, J., Kirk, K., Bröer, S., Parish, C. R. and Enders, A. (2014). Mice deficient in the putative phospholipid flippase Atp11c exhibit altered erythrocyte shape, anemia and reduced erythrocyte lifespan. J. Biol. Chem. 289, 19531-19537.
    • (2014) J. Biol. Chem. , vol.289 , pp. 19531-19537
    • Yabas, M.1    Coupland, L.A.2    Cromer, D.3    Winterberg, M.4    Teoh, N.C.5    D'Rozario, J.6    Kirk, K.7    Bröer, S.8    Parish, C.R.9    Enders, A.10
  • 123
    • 0024340989 scopus 로고
    • Control of transmembrane lipid asymmetry in chromaffin granules by an ATP-dependent protein
    • Zachowski, A., Henry, J.-P. and Devaux, P. F. (1989). Control of transmembrane lipid asymmetry in chromaffin granules by an ATP-dependent protein. Nature 340, 75-76.
    • (1989) Nature , vol.340 , pp. 75-76
    • Zachowski, A.1    Henry, J.-P.2    Devaux, P.F.3
  • 124
    • 70349861777 scopus 로고    scopus 로고
    • Irregular Trichome Branch 2 (ITB2) encodes a putative aminophospholipid translocase that regulates trichome branch elongation in Arabidopsis
    • Zhang, X. and Oppenheimer, D. G. (2009). Irregular Trichome Branch 2 (ITB2) encodes a putative aminophospholipid translocase that regulates trichome branch elongation in Arabidopsis. Plant J. 60, 195-206.
    • (2009) Plant J. , vol.60 , pp. 195-206
    • Zhang, X.1    Oppenheimer, D.G.2
  • 125
    • 70349731740 scopus 로고    scopus 로고
    • Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast
    • Zhou, X. and Graham, T. R. (2009). Reconstitution of phospholipid translocase activity with purified Drs2p, a type-IV P-type ATPase from budding yeast. Proc. Nat. Acad. Sci. USA 106, 16586-16591.
    • (2009) Proc. Nat. Acad. Sci. USA , vol.106 , pp. 16586-16591
    • Zhou, X.1    Graham, T.R.2
  • 126
    • 84887075775 scopus 로고    scopus 로고
    • Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail
    • Zhou, X., Sebastian, T. T. and Graham, T. R. (2013). Auto-inhibition of Drs2p, a yeast phospholipid flippase, by its carboxyl-terminal tail. J. Biol. Chem. 288, 31807-31815.
    • (2013) J. Biol. Chem. , vol.288 , pp. 31807-31815
    • Zhou, X.1    Sebastian, T.T.2    Graham, T.R.3
  • 127
    • 0031043059 scopus 로고    scopus 로고
    • Pathophysiologic implications of membrane phospholipid asymmetry in blood cells
    • Zwaal, R. F. and Schroit, A. J. (1997). Pathophysiologic implications of membrane phospholipid asymmetry in blood cells. Blood 89, 1121-1132.
    • (1997) Blood , vol.89 , pp. 1121-1132
    • Zwaal, R.F.1    Schroit, A.J.2


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