메뉴 건너뛰기




Volumn 99, Issue 5, 2010, Pages 1397-1407

Cholesterol depletion mimics the effect of cytoskeletal destabilization on membrane dynamics of the serotonin1A receptor: A zFCS study

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956589441     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.06.031     Document Type: Article
Times cited : (71)

References (55)
  • 1
    • 0035575575 scopus 로고    scopus 로고
    • Shrinking patches and slippery rafts: Scales of domains in the plasma membrane
    • Edidin, M. 2001. Shrinking patches and slippery rafts: scales of domains in the plasma membrane. Trends Cell Biol. 11:492-496.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 492-496
    • Edidin, M.1
  • 3
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro, S. 2003. Lipid rafts: elusive or illusive? Cell. 115:377-388.
    • (2003) Cell. , vol.115 , pp. 377-388
    • Munro, S.1
  • 4
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • Jacobson, K., O. G. Mouritsen, and R. G. W. Anderson. 2007. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9:7-14.
    • (2007) Nat. Cell. Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 5
    • 33747591249 scopus 로고    scopus 로고
    • Dynamics in the plasma membrane: How to combine fluidity and order
    • Marguet, D., P.-F. Lenne, H. T. He. 2006. Dynamics in the plasma membrane: how to combine fluidity and order. EMBO J. 25:3446-3457.
    • (2006) EMBO J. , vol.25 , pp. 3446-3457
    • Marguet, D.1    Lenne, P.-F.2    He, H.T.3
  • 6
    • 33646019290 scopus 로고    scopus 로고
    • Membrane biophysics
    • Zimmerberg, J. 2006. Membrane biophysics. Curr. Biol. 16: R272-R276.
    • (2006) Curr. Biol. , vol.16
    • Zimmerberg, J.1
  • 8
    • 0024277783 scopus 로고
    • Lateral mobility of proteins and lipids in the red cell membrane and the activation of adenylate cyclase by β-adrenergic receptors
    • Peters, R. 1988. Lateral mobility of proteins and lipids in the red cell membrane and the activation of adenylate cyclase by β-adrenergic receptors. FEBS Lett. 234:1-7.
    • (1988) FEBS Lett. , vol.234 , pp. 1-7
    • Peters, R.1
  • 9
    • 20544464040 scopus 로고    scopus 로고
    • Single-molecule imaging of diffusion, recruitment, and activation of signaling molecules in living cells
    • Springer Series in Biophysics, S. Damjanovich, editor. Springer-Verlag, Berlin, Germany
    • Kusumi, A., H. Murakoshi, T. Fujiwara. 2005. Single-molecule imaging of diffusion, recruitment, and activation of signaling molecules in living cells. In Biophysical Aspects of Transmembrane Signaling, Springer Series in Biophysics. S. Damjanovich, editor. Springer-Verlag, Berlin, Germany.
    • (2005) Biophysical Aspects of Transmembrane Signaling
    • Kusumi, A.1    Murakoshi, H.2    Fujiwara, T.3
  • 10
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara, T., K. Ritchie, A. Kusumi. 2002. Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol. 157:1071-1081.
    • (2002) J. Cell. Biol. , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Kusumi, A.3
  • 11
  • 12
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: Novel variations of an established technique
    • Haustein, E., and P. Schwille. 2007. Fluorescence correlation spectroscopy: novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct. 36:151-169.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 13
    • 36448965981 scopus 로고    scopus 로고
    • Pharmacology under the microscope: The use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes
    • Briddon, S. J., and S. J. Hill. 2007. Pharmacology under the microscope: the use of fluorescence correlation spectroscopy to determine the properties of ligand-receptor complexes. Trends Pharmacol. Sci. 28:637-645.
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 637-645
    • Briddon, S.J.1    Hill, S.J.2
  • 14
    • 55849133025 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy for the study of membrane dynamics and protein/lipid interactions
    • García-Sáez, A. J., and P. Schwille. 2008. Fluorescence correlation spectroscopy for the study of membrane dynamics and protein/lipid interactions. Methods. 46:116-122.
    • (2008) Methods , vol.46 , pp. 116-122
    • García-Sáez, A.J.1    Schwille, P.2
  • 15
    • 0037154114 scopus 로고    scopus 로고
    • Biological and chemical applications of fluorescence correlation spectroscopy: A review
    • Hess, S. T., S. Huang, W. W. Webb. 2002. Biological and chemical applications of fluorescence correlation spectroscopy: a review. Biochemistry. 41:697-705.
    • (2002) Biochemistry , vol.41 , pp. 697-705
    • Hess, S.T.1    Huang, S.2    Webb, W.W.3
  • 16
    • 0038699021 scopus 로고    scopus 로고
    • How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy
    • Benda, A., M. Benes, M. Hof. 2003. How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy. Langmuir. 19:4120-4126.
    • (2003) Langmuir , vol.19 , pp. 4120-4126
    • Benda, A.1    Benes, M.2    Hof, M.3
  • 17
    • 33746711642 scopus 로고    scopus 로고
    • Probing diffusion laws within cellular membranes by Z-scan fluorescence correlation spectroscopy
    • Humpolícková, J., E. Gielen, Y. Engelborghs. 2006. Probing diffusion laws within cellular membranes by Z-scan fluorescence correlation spectroscopy. Biophys. J. 91: L23-L25.
    • (2006) Biophys. J. , vol.91
    • Humpolícková, J.1    Gielen, E.2    Engelborghs, Y.3
  • 18
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck, L., H. Rigneault, P. F. Lenne. 2005. Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys. J. 89:4029-4042.
    • (2005) Biophys. J. , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Lenne, P.F.3
  • 19
    • 33746581138 scopus 로고    scopus 로고
    • Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork
    • Lenne, P.-F., L. Wawrezinieck, D. Marguet. 2006. Dynamic molecular confinement in the plasma membrane by microdomains and the cytoskeleton meshwork. EMBO J. 25:3245-3256.
    • (2006) EMBO J. , vol.25 , pp. 3245-3256
    • Lenne, P.-F.1    Wawrezinieck, L.2    Marguet, D.3
  • 20
    • 0025992051 scopus 로고
    • Fluorescent membrane probes incorporating dipyrrometheneboron difluoride fluorophores
    • Johnson, I. D., H. C. Kang, and R. P. Haugland. 1991. Fluorescent membrane probes incorporating dipyrrometheneboron difluoride fluorophores. Anal. Biochem. 198:228-237.
    • (1991) Anal. Biochem. , vol.198 , pp. 228-237
    • Johnson, I.D.1    Kang, H.C.2    Haugland, R.P.3
  • 21
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., S. G. F. Rasmussen, and B. K. Kobilka. 2009. The structure and function of G-protein-coupled receptors. Nature. 459:356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.F.2    Kobilka, B.K.3
  • 22
    • 61649096359 scopus 로고    scopus 로고
    • G-protein-coupled receptor focused drug discovery using a target class platform approach
    • Heilker, R., M. Wolff, M. Bieler. 2009. G-protein-coupled receptor focused drug discovery using a target class platform approach. Drug Discov. Today. 14:231-240.
    • (2009) Drug Discov. Today , vol.14 , pp. 231-240
    • Heilker, R.1    Wolff, M.2    Bieler, M.3
  • 23
    • 18044362857 scopus 로고    scopus 로고
    • The serotonin1A receptor: A representative member of the serotonin receptor family
    • Pucadyil, T. J., S. Kalipatnapu, and A. Chattopadhyay. 2005. The serotonin1A receptor: a representative member of the serotonin receptor family. Cell. Mol. Neurobiol. 25:553-580.
    • (2005) Cell. Mol. Neurobiol. , vol.25 , pp. 553-580
    • Pucadyil, T.J.1    Kalipatnapu, S.2    Chattopadhyay, A.3
  • 25
    • 0016379116 scopus 로고
    • Fluorescence correlation spectroscopy. I. Conceptual basis and theory
    • Elson, E. L., and D. Magde. 1974. Fluorescence correlation spectroscopy. I. Conceptual basis and theory. Biopolymers. 13:1-27.
    • (1974) Biopolymers , vol.13 , pp. 1-27
    • Elson, E.L.1    Magde, D.2
  • 26
    • 0016651661 scopus 로고
    • Fluorescence correlation spectroscopy and Brownian rotational diffusion
    • Aragón, S. R., and R. Pecora. 1975. Fluorescence correlation spectroscopy and Brownian rotational diffusion. Biopolymers. 14:119-138.
    • (1975) Biopolymers , vol.14 , pp. 119-138
    • Aragón, S.R.1    Pecora, R.2
  • 27
    • 84975576954 scopus 로고
    • Optical spatial intensity profiles for high order autocorrelation in fluorescence spectroscopy
    • Palmer III, A. G., and N. L. Thompson. 1989. Optical spatial intensity profiles for high order autocorrelation in fluorescence spectroscopy. Appl. Opt. 28:1214-1220.
    • (1989) Appl. Opt. , vol.28 , pp. 1214-1220
    • Palmer III, A.G.1    Thompson, N.L.2
  • 28
    • 10844293498 scopus 로고    scopus 로고
    • G-proteindependent cell surface dynamics of the human serotonin1A receptor tagged to yellow fluorescent protein
    • Pucadyil, T. J., S. Kalipatnapu, A. Chattopadhyay. 2004. G-proteindependent cell surface dynamics of the human serotonin1A receptor tagged to yellow fluorescent protein. Biochemistry. 43:15852-15862.
    • (2004) Biochemistry , vol.43 , pp. 15852-15862
    • Pucadyil, T.J.1    Kalipatnapu, S.2    Chattopadhyay, A.3
  • 29
    • 33846815123 scopus 로고    scopus 로고
    • Diffusion analysis within single nanometric apertures reveals the ultrafine cell membrane organization
    • Wenger, J., F. Conchonaud, P. F. Lenne. 2007. Diffusion analysis within single nanometric apertures reveals the ultrafine cell membrane organization. Biophys. J. 92:913-919.
    • (2007) Biophys. J. , vol.92 , pp. 913-919
    • Wenger, J.1    Conchonaud, F.2    Lenne, P.F.3
  • 32
    • 17844389341 scopus 로고    scopus 로고
    • Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques
    • Suzuki, K., K. Ritchie, A. Kusumi. 2005. Rapid hop diffusion of a G-protein-coupled receptor in the plasma membrane as revealed by single-molecule techniques. Biophys. J. 88:3659-3680.
    • (2005) Biophys. J. , vol.88 , pp. 3659-3680
    • Suzuki, K.1    Ritchie, K.2    Kusumi, A.3
  • 33
    • 28644443374 scopus 로고    scopus 로고
    • Dynamics of receptor/G protein coupling in living cells
    • Hein, P., M. Frank, M. Bünemann. 2005. Dynamics of receptor/G protein coupling in living cells. EMBO J. 24:4106-4114.
    • (2005) EMBO J. , vol.24 , pp. 4106-4114
    • Hein, P.1    Frank, M.2    Bünemann, M.3
  • 34
    • 66649110614 scopus 로고    scopus 로고
    • GPCR and G proteins: Drug efficacy and activation in live cells
    • Vilardaga, J.-P., M. Bünemann, C. Hoffmann. 2009. GPCR and G proteins: drug efficacy and activation in live cells. Mol. Endocrinol. 23:590-599.
    • (2009) Mol. Endocrinol. , vol.23 , pp. 590-599
    • Vilardaga, J.-P.1    Bünemann, M.2    Hoffmann, C.3
  • 35
    • 0025731586 scopus 로고
    • Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments
    • Sampath, P., and T. D. Pollard. 1991. Effects of cytochalasin, phalloidin, and pH on the elongation of actin filaments. Biochemistry. 30:1973-1980.
    • (1991) Biochemistry , vol.30 , pp. 1973-1980
    • Sampath, P.1    Pollard, T.D.2
  • 36
    • 34249064912 scopus 로고    scopus 로고
    • Use of cyclodextrins to manipulate plasma membrane cholesterol content: Evidence, misconceptions and control strategies
    • Zidovetzki, R., and I. Levitan. 2007. Use of cyclodextrins to manipulate plasma membrane cholesterol content: evidence, misconceptions and control strategies. Biochim. Biophys. Acta. 1768:1311-1324.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1311-1324
    • Zidovetzki, R.1    Levitan, I.2
  • 37
    • 33744543610 scopus 로고    scopus 로고
    • Role of cholesterol in the function and organization of G-protein coupled receptors
    • Pucadyil, T. J., and A. Chattopadhyay. 2006. Role of cholesterol in the function and organization of G-protein coupled receptors. Prog. Lipid Res. 45:295-333.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 295-333
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 38
    • 59249094898 scopus 로고    scopus 로고
    • Are specific nonannular cholesterol binding sites present in G-protein coupled receptors?
    • Paila, Y. D., S. Tiwari, and A. Chattopadhyay. 2009. Are specific nonannular cholesterol binding sites present in G-protein coupled receptors? Biochim. Biophys. Acta. 1788:295-302.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 295-302
    • Paila, Y.D.1    Tiwari, S.2    Chattopadhyay, A.3
  • 40
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: Applications to membrane dynamics
    • Saxton, M. J., and K. Jacobson. 1997. Single-particle tracking: applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 26:373-399.
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 41
    • 38649085603 scopus 로고    scopus 로고
    • Lateral diffusion of proteins in the plasma membrane: Spatial tessellation and percolation theory
    • Sung, B. J., and A. Yethiraj. 2008. Lateral diffusion of proteins in the plasma membrane: spatial tessellation and percolation theory. J. Phys. Chem. B. 112:143-149.
    • (2008) J. Phys. Chem. B. , vol.112 , pp. 143-149
    • Sung, B.J.1    Yethiraj, A.2
  • 42
    • 0022625444 scopus 로고
    • Rates of membrane-associated reactions: Reduction of dimensionality revisited
    • McCloskey, M. A., and M.-M. Poo. 1986. Rates of membrane-associated reactions: reduction of dimensionality revisited. J. Cell Biol. 102:88-96.
    • (1986) J. Cell. Biol. , vol.102 , pp. 88-96
    • McCloskey, M.A.1    Poo, M.-M.2
  • 44
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin
    • Kwik, J., S. Boyle, M. Edidin. 2003. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4, 5-bisphosphate-dependent organization of cell actin. Proc. Natl. Acad. Sci. USA. 100:13964-13969.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Edidin, M.3
  • 45
    • 33746655717 scopus 로고    scopus 로고
    • Cholesterol deficiency perturbs actin signaling and glutamate homeostasis in hippocampal astrocytes
    • Tsai, H.-I., L.-H. Tsai, Y. C. Chou. 2006. Cholesterol deficiency perturbs actin signaling and glutamate homeostasis in hippocampal astrocytes. Brain Res. 1104:27-38.
    • (2006) Brain Res. , vol.1104 , pp. 27-38
    • Tsai, H.-I.1    Tsai, L.-H.2    Chou, Y.C.3
  • 46
    • 1142286431 scopus 로고    scopus 로고
    • Use of cyclodextrin for AFM monitoring of model raft formation
    • Giocondi, M.-C., P. E. Milhiet, C. Le Grimellec. 2004. Use of cyclodextrin for AFM monitoring of model raft formation. Biophys. J. 86:861-869.
    • (2004) Biophys. J. , vol.86 , pp. 861-869
    • Giocondi, M.-C.1    Milhiet, P.E.2    Le Grimellec, C.3
  • 47
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles
    • Rodal, S. K., G. Skretting, K. Sandvig. 1999. Extraction of cholesterol with methyl-β-cyclodextrin perturbs formation of clathrin-coated endocytic vesicles. Mol. Biol. Cell. 10:961-974.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Sandvig, K.3
  • 48
    • 0033535989 scopus 로고    scopus 로고
    • Acute cholesterol depletion inhibits clathrin-coated pit budding
    • Subtil, A., I. Gaidarov, T. E. McGraw. 1999. Acute cholesterol depletion inhibits clathrin-coated pit budding. Proc. Natl. Acad. Sci. USA. 96:6775-6780.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6775-6780
    • Subtil, A.1    Gaidarov, I.2    McGraw, T.E.3
  • 50
    • 2942655668 scopus 로고    scopus 로고
    • Dynamics of putative raft-associated proteins at the cell surface
    • Kenworthy, A. K., B. J. Nichols, J. Lippincott-Schwartz. 2004. Dynamics of putative raft-associated proteins at the cell surface. J. Cell Biol. 165:735-746.
    • (2004) J. Cell. Biol. , vol.165 , pp. 735-746
    • Kenworthy, A.K.1    Nichols, B.J.2    Lippincott-Schwartz, J.3
  • 51
    • 11244339619 scopus 로고    scopus 로고
    • Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane
    • Vrljic, M., S. Y. Nishimura, H. M. McConnell. 2005. Cholesterol depletion suppresses the translational diffusion of class II major histocompatibility complex proteins in the plasma membrane. Biophys. J. 88:334-347.
    • (2005) Biophys. J. , vol.88 , pp. 334-347
    • Vrljic, M.1    Nishimura, S.Y.2    McConnell, H.M.3
  • 52
    • 4143091360 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy relates rafts in model and native membranes
    • Bacia, K., D. Scherfeld, P. Schwille. 2004. Fluorescence correlation spectroscopy relates rafts in model and native membranes. Biophys. J. 87:1034-1043.
    • (2004) Biophys. J. , vol.87 , pp. 1034-1043
    • Bacia, K.1    Scherfeld, D.2    Schwille, P.3
  • 53
    • 34548662875 scopus 로고    scopus 로고
    • Membrane mobility and microdomain association of the dopamine transporter studied with fluorescence correlation spectroscopy and fluorescence recovery after photobleaching
    • Adkins, E. M., D. J. Samuvel, U. Gether. 2007. Membrane mobility and microdomain association of the dopamine transporter studied with fluorescence correlation spectroscopy and fluorescence recovery after photobleaching. Biochemistry. 46:10484-10497.
    • (2007) Biochemistry , vol.46 , pp. 10484-10497
    • Adkins, E.M.1    Samuvel, D.J.2    Gether, U.3
  • 54
    • 0034611005 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle, A., P. Keller, J. K. Hörber. 2000. Sphingolipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148:997-1008.
    • (2000) J. Cell. Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Hörber, J.K.3
  • 55
    • 0025924643 scopus 로고
    • 2-receptor mobile fraction and ligand-dependent adenylate cyclase activity are directly correlated in LLC-PK1 renal epithelial cells
    • 2-receptor mobile fraction and ligand-dependent adenylate cyclase activity are directly correlated in LLC-PK1 renal epithelial cells. J. Cell Biol. 114:53-60.
    • (1991) J. Cell. Biol. , vol.114 , pp. 53-60
    • Jans, D.A.1    Peters, R.2    Fahrenholz, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.