메뉴 건너뛰기




Volumn 39, Issue 3, 2014, Pages 130-140

Ionic protein-lipid interaction at the plasma membrane: What can the charge do?

Author keywords

Acidic phospholipids; Ca2+; Ionic protein lipid interaction

Indexed keywords

CALCIUM ION; PHOSPHATIDIC ACID; PHOSPHATIDYLGLYCEROL; PHOSPHATIDYLSERINE; TRIPHOSPHOINOSITIDE;

EID: 84896714737     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2014.01.002     Document Type: Review
Times cited : (98)

References (90)
  • 1
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: where they are and how they behave
    • van Meer G., et al. Membrane lipids: where they are and how they behave. Nat. Rev. Mol. Cell Biol. 2008, 9:112-124.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 112-124
    • van Meer, G.1
  • 2
    • 77952944942 scopus 로고    scopus 로고
    • The distribution and function of phosphatidylserine in cellular membranes
    • Leventis P.A., Grinstein S. The distribution and function of phosphatidylserine in cellular membranes. Annu. Rev. Biophys. 2010, 39:407-427.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 407-427
    • Leventis, P.A.1    Grinstein, S.2
  • 3
    • 34249685982 scopus 로고    scopus 로고
    • An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins
    • Kooijman E.E., et al. An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins. J. Biol. Chem. 2007, 282:11356-11364.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11356-11364
    • Kooijman, E.E.1
  • 4
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • Di Paolo G., De Camilli P. Phosphoinositides in cell regulation and membrane dynamics. Nature 2006, 443:651-657.
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 5
    • 70350061531 scopus 로고    scopus 로고
    • Ionization properties of phosphatidylinositol polyphosphates in mixed model membranes
    • Kooijman E.E., et al. Ionization properties of phosphatidylinositol polyphosphates in mixed model membranes. Biochemistry 2009, 48:9360-9371.
    • (2009) Biochemistry , vol.48 , pp. 9360-9371
    • Kooijman, E.E.1
  • 6
    • 84880962133 scopus 로고    scopus 로고
    • Phosphoinositides: tiny lipids with giant impact on cell regulation
    • Balla T. Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol. Rev. 2013, 93:1019-1137.
    • (2013) Physiol. Rev. , vol.93 , pp. 1019-1137
    • Balla, T.1
  • 7
    • 84855807389 scopus 로고    scopus 로고
    • Conditional peripheral membrane proteins: facing up to limited specificity
    • Moravcevic K., et al. Conditional peripheral membrane proteins: facing up to limited specificity. Structure 2012, 20:15-27.
    • (2012) Structure , vol.20 , pp. 15-27
    • Moravcevic, K.1
  • 8
    • 33645274673 scopus 로고    scopus 로고
    • Analyzing phosphoinositides and their interacting proteins
    • Rusten T.E., Stenmark H. Analyzing phosphoinositides and their interacting proteins. Nat. Methods 2006, 3:251-258.
    • (2006) Nat. Methods , vol.3 , pp. 251-258
    • Rusten, T.E.1    Stenmark, H.2
  • 9
    • 48249116482 scopus 로고    scopus 로고
    • 2 is a necessary cofactor for ion channel function: how and why?
    • 2 is a necessary cofactor for ion channel function: how and why?. Annu. Rev. Biophys. 2008, 37:175-195.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 175-195
    • Suh, B.C.1    Hille, B.2
  • 10
    • 78649915767 scopus 로고    scopus 로고
    • Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids
    • Moravcevic K., et al. Kinase associated-1 domains drive MARK/PAR1 kinases to membrane targets by binding acidic phospholipids. Cell 2010, 143:966-977.
    • (2010) Cell , vol.143 , pp. 966-977
    • Moravcevic, K.1
  • 11
    • 84864848873 scopus 로고    scopus 로고
    • 2 are essential but independent lipid determinants of membrane identity
    • 2 are essential but independent lipid determinants of membrane identity. Science 2012, 337:727-730.
    • (2012) Science , vol.337 , pp. 727-730
    • Hammond, G.R.1
  • 12
    • 79961113678 scopus 로고    scopus 로고
    • High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine
    • Fairn G.D., et al. High-resolution mapping reveals topologically distinct cellular pools of phosphatidylserine. J. Cell Biol. 2011, 194:257-275.
    • (2011) J. Cell Biol. , vol.194 , pp. 257-275
    • Fairn, G.D.1
  • 13
    • 84875523175 scopus 로고    scopus 로고
    • 3 is required for syntaxin1A clustering and neurotransmitter release
    • 3 is required for syntaxin1A clustering and neurotransmitter release. Neuron 2013, 77:1097-1108.
    • (2013) Neuron , vol.77 , pp. 1097-1108
    • Khuong, T.M.1
  • 14
    • 84878917689 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment
    • Honigmann A., et al. Phosphatidylinositol 4,5-bisphosphate clusters act as molecular beacons for vesicle recruitment. Nat. Struct. Mol. Biol. 2013, 20:679-686.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 679-686
    • Honigmann, A.1
  • 15
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung T., et al. Membrane phosphatidylserine regulates surface charge and protein localization. Science 2008, 319:210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1
  • 16
    • 82455188329 scopus 로고    scopus 로고
    • Putting the pH into phosphatidic acid signaling
    • Shin J.J., Loewen C.J. Putting the pH into phosphatidic acid signaling. BMC Biol. 2011, 9:85.
    • (2011) BMC Biol. , vol.9 , pp. 85
    • Shin, J.J.1    Loewen, C.J.2
  • 17
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • Cho W., Stahelin R.V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 2006, 1761:838-849.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 18
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • Rizzo M.A., et al. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 2000, 275:23911-23918.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911-23918
    • Rizzo, M.A.1
  • 19
    • 34447568476 scopus 로고    scopus 로고
    • Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos
    • Zhao C., et al. Phospholipase D2-generated phosphatidic acid couples EGFR stimulation to Ras activation by Sos. Nat. Cell Biol. 2007, 9:706-712.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 706-712
    • Zhao, C.1
  • 20
    • 84862555250 scopus 로고    scopus 로고
    • The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid
    • Rodriguez Camargo D.C., et al. The FKBP-rapamycin binding domain of human TOR undergoes strong conformational changes in the presence of membrane mimetics with and without the regulator phosphatidic acid. Biochemistry 2012, 51:4909-4921.
    • (2012) Biochemistry , vol.51 , pp. 4909-4921
    • Rodriguez Camargo, D.C.1
  • 21
    • 81855221892 scopus 로고    scopus 로고
    • Membrane protein sequestering by ionic protein-lipid interactions
    • Van den Bogaart G., et al. Membrane protein sequestering by ionic protein-lipid interactions. Nature 2011, 479:552-555.
    • (2011) Nature , vol.479 , pp. 552-555
    • Van den Bogaart, G.1
  • 22
    • 18944364523 scopus 로고    scopus 로고
    • 2 signaling in lipid domains: a critical re-evaluation
    • 2 signaling in lipid domains: a critical re-evaluation. EMBO J. 2005, 24:1664-1673.
    • (2005) EMBO J. , vol.24 , pp. 1664-1673
    • van Rheenen, J.1
  • 23
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 2008, 9:99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 24
    • 68949108024 scopus 로고    scopus 로고
    • EGFR juxtamembrane domain, membranes, and calmodulin: kinetics of their interaction
    • Sengupta P., et al. EGFR juxtamembrane domain, membranes, and calmodulin: kinetics of their interaction. Biophys. J. 2009, 96:4887-4895.
    • (2009) Biophys. J. , vol.96 , pp. 4887-4895
    • Sengupta, P.1
  • 25
    • 33845313646 scopus 로고    scopus 로고
    • 2 lipids target proteins with polybasic clusters to the plasma membrane
    • 2 lipids target proteins with polybasic clusters to the plasma membrane. Science 2006, 314:1458-1461.
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1
  • 26
    • 84873292211 scopus 로고    scopus 로고
    • Architecture and membrane interactions of the EGF receptor
    • Arkhipov A., et al. Architecture and membrane interactions of the EGF receptor. Cell 2013, 152:557-569.
    • (2013) Cell , vol.152 , pp. 557-569
    • Arkhipov, A.1
  • 27
    • 84873280409 scopus 로고    scopus 로고
    • Conformational coupling across the plasma membrane in activation of the EGF receptor
    • Endres N.F., et al. Conformational coupling across the plasma membrane in activation of the EGF receptor. Cell 2013, 152:543-556.
    • (2013) Cell , vol.152 , pp. 543-556
    • Endres, N.F.1
  • 28
    • 80053131218 scopus 로고    scopus 로고
    • + channel Kir2.2
    • + channel Kir2.2. Nature 2011, 477:495-498.
    • (2011) Nature , vol.477 , pp. 495-498
    • Hansen, S.B.1
  • 29
    • 0037821876 scopus 로고    scopus 로고
    • Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer
    • Zhang W., et al. Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer. J. Biol. Chem. 2003, 278:21459-21466.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21459-21466
    • Zhang, W.1
  • 30
    • 1942519695 scopus 로고    scopus 로고
    • 2 on phospholipid membranes by basic/aromatic regions of proteins
    • 2 on phospholipid membranes by basic/aromatic regions of proteins. Biophys. J. 2004, 86:2188-2207.
    • (2004) Biophys. J. , vol.86 , pp. 2188-2207
    • Gambhir, A.1
  • 31
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif
    • Xu C., et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3epsilon cytoplasmic tyrosine-based motif. Cell 2008, 135:702-713.
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1
  • 32
    • 76549119994 scopus 로고    scopus 로고
    • Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain
    • Chukkapalli V., et al. Opposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:1600-1605.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1600-1605
    • Chukkapalli, V.1
  • 33
    • 77951498245 scopus 로고    scopus 로고
    • Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 Tat by infected T-cells
    • Rayne F., et al. Phosphatidylinositol-(4,5)-bisphosphate enables efficient secretion of HIV-1 Tat by infected T-cells. EMBO J. 2010, 29:1348-1362.
    • (2010) EMBO J. , vol.29 , pp. 1348-1362
    • Rayne, F.1
  • 34
    • 77950421393 scopus 로고    scopus 로고
    • HIV-1 Nef membrane association depends on charge, curvature, composition and sequence
    • Gerlach H., et al. HIV-1 Nef membrane association depends on charge, curvature, composition and sequence. Nat. Chem. Biol. 2010, 6:46-53.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 46-53
    • Gerlach, H.1
  • 35
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 2005, 438:605-611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 36
    • 74049126062 scopus 로고    scopus 로고
    • 2- and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering
    • 2- and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering. J. Cell Biol. 2009, 187:715-731.
    • (2009) J. Cell Biol. , vol.187 , pp. 715-731
    • Saltel, F.1
  • 37
    • 61849116777 scopus 로고    scopus 로고
    • Electrochemical cues regulate assembly of the Frizzled/Dishevelled complex at the plasma membrane during planar epithelial polarization
    • Simons M., et al. Electrochemical cues regulate assembly of the Frizzled/Dishevelled complex at the plasma membrane during planar epithelial polarization. Nat. Cell Biol. 2009, 11:286-294.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 286-294
    • Simons, M.1
  • 38
    • 78649452812 scopus 로고    scopus 로고
    • Structure and control of the actin regulatory WAVE complex
    • Chen Z., et al. Structure and control of the actin regulatory WAVE complex. Nature 2010, 468:533-538.
    • (2010) Nature , vol.468 , pp. 533-538
    • Chen, Z.1
  • 39
    • 65249117435 scopus 로고    scopus 로고
    • Sequential regulation of DOCK2 dynamics by two phospholipids during neutrophil chemotaxis
    • Nishikimi A., et al. Sequential regulation of DOCK2 dynamics by two phospholipids during neutrophil chemotaxis. Science 2009, 324:384-387.
    • (2009) Science , vol.324 , pp. 384-387
    • Nishikimi, A.1
  • 40
    • 78149451596 scopus 로고    scopus 로고
    • Phosphoinositides are essential coactivators for p21-activated kinase 1
    • Strochlic T.I., et al. Phosphoinositides are essential coactivators for p21-activated kinase 1. Mol. Cell 2010, 40:493-500.
    • (2010) Mol. Cell , vol.40 , pp. 493-500
    • Strochlic, T.I.1
  • 41
    • 84875439550 scopus 로고    scopus 로고
    • Phosphatidic acid-dependent recruitment and function of the Rac activator DOCK1 during dorsal ruffle formation
    • Sanematsu F., et al. Phosphatidic acid-dependent recruitment and function of the Rac activator DOCK1 during dorsal ruffle formation. J. Biol. Chem. 2013, 288:8092-8100.
    • (2013) J. Biol. Chem. , vol.288 , pp. 8092-8100
    • Sanematsu, F.1
  • 42
    • 84859618951 scopus 로고    scopus 로고
    • Store-operated calcium channels: new perspectives on mechanism and function
    • Lewis R.S. Store-operated calcium channels: new perspectives on mechanism and function. Cold Spring Harb. Perspect. Biol. 2011, 3:a003970.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Lewis, R.S.1
  • 43
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-activated calcium channel Orai
    • Hou X., et al. Crystal structure of the calcium release-activated calcium channel Orai. Science 2012, 338:1308-1313.
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1
  • 44
    • 77950377028 scopus 로고    scopus 로고
    • Molecular basis of calcium signaling in lymphocytes: STIM and ORAI
    • Hogan P.G., et al. Molecular basis of calcium signaling in lymphocytes: STIM and ORAI. Annu. Rev. Immunol. 2010, 28:491-533.
    • (2010) Annu. Rev. Immunol. , vol.28 , pp. 491-533
    • Hogan, P.G.1
  • 45
    • 33646576875 scopus 로고    scopus 로고
    • A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function
    • Feske S., et al. A mutation in Orai1 causes immune deficiency by abrogating CRAC channel function. Nature 2006, 441:179-185.
    • (2006) Nature , vol.441 , pp. 179-185
    • Feske, S.1
  • 46
    • 61349137530 scopus 로고    scopus 로고
    • STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1
    • Park C.Y., et al. STIM1 clusters and activates CRAC channels via direct binding of a cytosolic domain to Orai1. Cell 2009, 136:876-890.
    • (2009) Cell , vol.136 , pp. 876-890
    • Park, C.Y.1
  • 47
    • 72449150765 scopus 로고    scopus 로고
    • Role of phosphoinositides in STIM1 dynamics and store-operated calcium entry
    • Walsh C.M., et al. Role of phosphoinositides in STIM1 dynamics and store-operated calcium entry. Biochem. J. 2010, 425:159-168.
    • (2010) Biochem. J. , vol.425 , pp. 159-168
    • Walsh, C.M.1
  • 48
    • 70649107057 scopus 로고    scopus 로고
    • A conserved, lipid-mediated sorting mechanism of yeast Ist2 and mammalian STIM proteins to the peripheral ER
    • Ercan E., et al. A conserved, lipid-mediated sorting mechanism of yeast Ist2 and mammalian STIM proteins to the peripheral ER. Traffic 2009, 10:1802-1818.
    • (2009) Traffic , vol.10 , pp. 1802-1818
    • Ercan, E.1
  • 49
    • 84881447865 scopus 로고    scopus 로고
    • Initial activation of STIM1, the regulator of store-operated calcium entry
    • Zhou Y., et al. Initial activation of STIM1, the regulator of store-operated calcium entry. Nat. Struct. Mol. Biol. 2013, 20:973-981.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 973-981
    • Zhou, Y.1
  • 50
    • 84880509648 scopus 로고    scopus 로고
    • 2+ entry
    • 2+ entry. Nature 2013, 499:238-242.
    • (2013) Nature , vol.499 , pp. 238-242
    • Sharma, S.1
  • 51
    • 74049157769 scopus 로고    scopus 로고
    • TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation
    • Lillemeier B.F., et al. TCR and Lat are expressed on separate protein islands on T cell membranes and concatenate during activation. Nat. Immunol. 2010, 11:90-96.
    • (2010) Nat. Immunol. , vol.11 , pp. 90-96
    • Lillemeier, B.F.1
  • 52
    • 81955164142 scopus 로고    scopus 로고
    • Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor
    • Sherman E., et al. Functional nanoscale organization of signaling molecules downstream of the T cell antigen receptor. Immunity 2011, 35:705-720.
    • (2011) Immunity , vol.35 , pp. 705-720
    • Sherman, E.1
  • 53
    • 48249119533 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
    • James D.J., et al. Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion. J. Cell Biol. 2008, 182:355-366.
    • (2008) J. Cell Biol. , vol.182 , pp. 355-366
    • James, D.J.1
  • 54
    • 39449106371 scopus 로고    scopus 로고
    • SNARE-catalyzed fusion events are regulated by syntaxin1A-lipid interactions
    • Lam A.D., et al. SNARE-catalyzed fusion events are regulated by syntaxin1A-lipid interactions. Mol. Biol. Cell 2008, 19:485-497.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 485-497
    • Lam, A.D.1
  • 55
    • 66349122907 scopus 로고    scopus 로고
    • Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol
    • Murray D.H., Tamm L.K. Clustering of syntaxin-1A in model membranes is modulated by phosphatidylinositol 4,5-bisphosphate and cholesterol. Biochemistry 2009, 48:4617-4625.
    • (2009) Biochemistry , vol.48 , pp. 4617-4625
    • Murray, D.H.1    Tamm, L.K.2
  • 56
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition
    • Aivazian D., Stern L.J. Phosphorylation of T cell receptor zeta is regulated by a lipid dependent folding transition. Nat. Struct. Biol. 2000, 7:1023-1026.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 57
    • 70249122432 scopus 로고    scopus 로고
    • The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions
    • Deford-Watts L.M., et al. The cytoplasmic tail of the T cell receptor CD3 epsilon subunit contains a phospholipid-binding motif that regulates T cell functions. J. Immunol. 2009, 183:1055-1064.
    • (2009) J. Immunol. , vol.183 , pp. 1055-1064
    • Deford-Watts, L.M.1
  • 58
    • 82755165363 scopus 로고    scopus 로고
    • Basic residues in the T-cell receptor zeta cytoplasmic domain mediate membrane association and modulate signaling
    • Zhang H., et al. Basic residues in the T-cell receptor zeta cytoplasmic domain mediate membrane association and modulate signaling. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:19323-19328.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 19323-19328
    • Zhang, H.1
  • 59
    • 79959542722 scopus 로고    scopus 로고
    • The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse
    • DeFord-Watts L.M., et al. The CD3 zeta subunit contains a phosphoinositide-binding motif that is required for the stable accumulation of TCR-CD3 complex at the immunological synapse. J. Immunol. 2011, 186:6839-6847.
    • (2011) J. Immunol. , vol.186 , pp. 6839-6847
    • DeFord-Watts, L.M.1
  • 60
    • 84871736291 scopus 로고    scopus 로고
    • 2+ regulates T-cell receptor activation by modulating the charge property of lipids
    • 2+ regulates T-cell receptor activation by modulating the charge property of lipids. Nature 2013, 493:111-115.
    • (2013) Nature , vol.493 , pp. 111-115
    • Shi, X.1
  • 61
    • 84871909015 scopus 로고    scopus 로고
    • Local changes in lipid environment of TCR microclusters regulate membrane binding by the CD3epsilon cytoplasmic domain
    • Gagnon E., et al. Local changes in lipid environment of TCR microclusters regulate membrane binding by the CD3epsilon cytoplasmic domain. J. Exp. Med. 2012, 209:2423-2439.
    • (2012) J. Exp. Med. , vol.209 , pp. 2423-2439
    • Gagnon, E.1
  • 62
    • 77953658109 scopus 로고    scopus 로고
    • TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers
    • Sumioka A., et al. TARP phosphorylation regulates synaptic AMPA receptors through lipid bilayers. Neuron 2010, 66:755-767.
    • (2010) Neuron , vol.66 , pp. 755-767
    • Sumioka, A.1
  • 63
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • Cao E., et al. TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 2013, 77:667-679.
    • (2013) Neuron , vol.77 , pp. 667-679
    • Cao, E.1
  • 65
    • 84881428576 scopus 로고    scopus 로고
    • Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening
    • Zaydman M.A., et al. Kv7.1 ion channels require a lipid to couple voltage sensing to pore opening. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:13180-13185.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 13180-13185
    • Zaydman, M.A.1
  • 66
    • 84866336468 scopus 로고    scopus 로고
    • 2 controls voltage-sensor movement and pore opening of Kv channels through the S4-S5 linker
    • 2 controls voltage-sensor movement and pore opening of Kv channels through the S4-S5 linker. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:E2399-E2408.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109
    • Rodriguez-Menchaca, A.A.1
  • 68
    • 77955488732 scopus 로고    scopus 로고
    • 2+ channels by membrane phosphatidylinositol 4,5-bisphosphate
    • 2+ channels by membrane phosphatidylinositol 4,5-bisphosphate. Neuron 2010, 67:224-238.
    • (2010) Neuron , vol.67 , pp. 224-238
    • Suh, B.C.1
  • 69
    • 42949125051 scopus 로고    scopus 로고
    • Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1
    • Kim A.Y., et al. Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1. Cell 2008, 133:475-485.
    • (2008) Cell , vol.133 , pp. 475-485
    • Kim, A.Y.1
  • 70
    • 72949091450 scopus 로고    scopus 로고
    • + channel Kir2.2 at 3.1Å resolution
    • + channel Kir2.2 at 3.1Å resolution. Science 2009, 326:1668-1674.
    • (2009) Science , vol.326 , pp. 1668-1674
    • Tao, X.1
  • 71
    • 84859651420 scopus 로고    scopus 로고
    • Mechanism of voltage gating in potassium channels
    • Jensen M.O., et al. Mechanism of voltage gating in potassium channels. Science 2012, 336:229-233.
    • (2012) Science , vol.336 , pp. 229-233
    • Jensen, M.O.1
  • 72
    • 47249152762 scopus 로고    scopus 로고
    • 2+ channels: impact on cell function
    • 2+ channels: impact on cell function. J. Physiol. 2008, 586:3043-3054.
    • (2008) J. Physiol. , vol.586 , pp. 3043-3054
    • Parekh, A.B.1
  • 73
    • 34248532811 scopus 로고    scopus 로고
    • Phospholipid scramblases: an overview
    • Sahu S.K., et al. Phospholipid scramblases: an overview. Arch. Biochem. Biophys. 2007, 462:103-114.
    • (2007) Arch. Biochem. Biophys. , vol.462 , pp. 103-114
    • Sahu, S.K.1
  • 74
    • 84877709762 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members
    • Suzuki J., et al. Calcium-dependent phospholipid scramblase activity of TMEM16 protein family members. J. Biol. Chem. 2013, 288:13305-13316.
    • (2013) J. Biol. Chem. , vol.288 , pp. 13305-13316
    • Suzuki, J.1
  • 75
    • 84876516813 scopus 로고    scopus 로고
    • Both TMEM16F-dependent and TMEM16F-independent pathways contribute to phosphatidylserine exposure in platelet apoptosis and platelet activation
    • van Kruchten R., et al. Both TMEM16F-dependent and TMEM16F-independent pathways contribute to phosphatidylserine exposure in platelet apoptosis and platelet activation. Blood 2013, 121:1850-1857.
    • (2013) Blood , vol.121 , pp. 1850-1857
    • van Kruchten, R.1
  • 76
    • 84871860558 scopus 로고    scopus 로고
    • 2+-activated cation channel required for lipid scrambling in platelets during blood coagulation
    • 2+-activated cation channel required for lipid scrambling in platelets during blood coagulation. Cell 2012, 151:111-122.
    • (2012) Cell , vol.151 , pp. 111-122
    • Yang, H.1
  • 77
    • 78650172970 scopus 로고    scopus 로고
    • Calcium-dependent phospholipid scrambling by TMEM16F
    • Suzuki J., et al. Calcium-dependent phospholipid scrambling by TMEM16F. Nature 2010, 468:834-838.
    • (2010) Nature , vol.468 , pp. 834-838
    • Suzuki, J.1
  • 78
    • 84874204802 scopus 로고    scopus 로고
    • Phospholipid scramblase-1-induced lipid reorganization regulates compensatory endocytosis in neuroendocrine cells
    • Ory S., et al. Phospholipid scramblase-1-induced lipid reorganization regulates compensatory endocytosis in neuroendocrine cells. J. Neurosci. 2013, 33:3545-3556.
    • (2013) J. Neurosci. , vol.33 , pp. 3545-3556
    • Ory, S.1
  • 79
    • 0037172775 scopus 로고    scopus 로고
    • Transbilayer asymmetry of phospholipids in the plasma membrane regulates exocytotic release in mast cells
    • Kato N., et al. Transbilayer asymmetry of phospholipids in the plasma membrane regulates exocytotic release in mast cells. Biochemistry 2002, 41:8068-8074.
    • (2002) Biochemistry , vol.41 , pp. 8068-8074
    • Kato, N.1
  • 80
    • 84872471468 scopus 로고    scopus 로고
    • Inactivation of anoctamin-6/Tmem16f, a regulator of phosphatidylserine scrambling in osteoblasts, leads to decreased mineral deposition in skeletal tissues
    • Ehlen H.W.A., et al. Inactivation of anoctamin-6/Tmem16f, a regulator of phosphatidylserine scrambling in osteoblasts, leads to decreased mineral deposition in skeletal tissues. J. Bone Miner. Res. 2013, 28:246-259.
    • (2013) J. Bone Miner. Res. , vol.28 , pp. 246-259
    • Ehlen, H.W.A.1
  • 82
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador W.E., et al. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 1993, 262:1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1
  • 84
    • 0033571223 scopus 로고    scopus 로고
    • 2+ bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • 2+ bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 1999, 18:6329-6338.
    • (1999) EMBO J. , vol.18 , pp. 6329-6338
    • Verdaguer, N.1
  • 85
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • Eggeling C., et al. Direct observation of the nanoscale dynamics of membrane lipids in a living cell. Nature 2009, 457:1159-1162.
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1
  • 86
    • 77951082775 scopus 로고    scopus 로고
    • Fast molecular tracking maps nanoscale dynamics of plasma membrane lipids
    • Sahl S.J., et al. Fast molecular tracking maps nanoscale dynamics of plasma membrane lipids. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:6829-6834.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 6829-6834
    • Sahl, S.J.1
  • 87
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson K.M., et al. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 1995, 83:1037-1046.
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1
  • 88
    • 79952922725 scopus 로고    scopus 로고
    • Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers
    • Boettcher J.M., et al. Atomic view of calcium-induced clustering of phosphatidylserine in mixed lipid bilayers. Biochemistry 2011, 50:2264-2273.
    • (2011) Biochemistry , vol.50 , pp. 2264-2273
    • Boettcher, J.M.1
  • 89
    • 69249120489 scopus 로고    scopus 로고
    • 2)- and cholesterol-containing monolayers
    • 2)- and cholesterol-containing monolayers. Biochemistry 2009, 48:8241-8248.
    • (2009) Biochemistry , vol.48 , pp. 8241-8248
    • Levental, I.1
  • 90
    • 84863145014 scopus 로고    scopus 로고
    • Divalent cation-induced cluster formation by polyphosphoinositides in model membranes
    • Wang Y.H., et al. Divalent cation-induced cluster formation by polyphosphoinositides in model membranes. J. Am. Chem. Soc. 2012, 134:3387-3395.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3387-3395
    • Wang, Y.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.