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Volumn 4, Issue 3, 2014, Pages 356-371

Endocytic trafficking of membrane-bound cargo: A flotillin point of view

Author keywords

Clathrin independent endocytosis; Dynamin; Endocytosis; Endosomal sorting; Exosomes; Flotillin; Lipid microdomains; Recycling

Indexed keywords

AMINO ACIDS; CELL ADHESION; MOLECULES; RECYCLING; SIGNAL TRANSDUCTION;

EID: 84904277977     PISSN: None     EISSN: 20770375     Source Type: Journal    
DOI: 10.3390/membranes4030356     Document Type: Review
Times cited : (85)

References (95)
  • 1
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A.; Rose, J.K. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 1992, 68, 533-544
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 2
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K.; Ikonen, E. Functional rafts in cell membranes. Nature 1997, 387, 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 3
    • 84860448210 scopus 로고    scopus 로고
    • Membrane organization and lipid rafts
    • doi:10.1101/cshperspect.a004697
    • Simons, K.; Sampaio, J.L. Membrane organization and lipid rafts. Cold Spring Harb. Perspect. Biol. 2011, 3, doi:10.1101/cshperspect.a004697
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Simons, K.1    Sampaio, J.L.2
  • 4
    • 0026937122 scopus 로고
    • Glycosyl-phosphatidylinositol-anchored membrane proteins
    • Brown, D.; Waneck, G.L. Glycosyl-phosphatidylinositol-anchored membrane proteins. J. Am. Soc. Nephrol. 1992, 3, 895-906
    • (1992) J. Am. Soc. Nephrol , vol.3 , pp. 895-906
    • Brown, D.1    Waneck, G.L.2
  • 5
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra, A.M.; Williamson, E.; Simons, K.; Parton, R.G. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 1994, 269, 30745-30748
    • (1994) J. Biol. Chem , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 6
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M.; Sudol, M.; Tang, Z.; Lisanti, M.P. Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 1993, 122, 789-807
    • (1993) J. Cell Biol , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 7
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh, M.D. Myristylation and palmitylation of Src family members: The fats of the matter. Cell 1994, 76, 411-413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 8
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey, P.J. Protein lipidation in cell signaling. Science 1995, 268, 221-225
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 9
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: Lipid modifications determine protein association with membrane rafts
    • Levental, I.; Grzybek, M.; Simons, K. Greasing their way: Lipid modifications determine protein association with membrane rafts. Biochemistry 2010, 49, 6305-6316
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 10
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • Dietrich, C.; Volovyk, Z.N.; Levi, M.; Thompson, N.L.; Jacobson, K. Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc. Natl. Acad. Sci. USA 2001, 98, 10642-10647
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 11
    • 1642271441 scopus 로고    scopus 로고
    • Membrane and raft association of reggie-1/flotillin-2: Role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression
    • Neumann-Giesen, C.; Falkenbach, B.; Beicht, P.; Claasen, S.; Luers, G.; Stuermer, C.A.; Herzog, V.; Tikkanen, R. Membrane and raft association of reggie-1/flotillin-2: Role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochem. J. 2004, 378, 509-518
    • (2004) Biochem. J , vol.378 , pp. 509-518
    • Neumann-Giesen, C.1    Falkenbach, B.2    Beicht, P.3    Claasen, S.4    Luers, G.5    Stuermer, C.A.6    Herzog, V.7    Tikkanen, R.8
  • 12
    • 67349189783 scopus 로고    scopus 로고
    • Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis
    • Babuke, T.; Ruonala, M.; Meister, M.; Amaddii, M.; Genzler, C.; Esposito, A.; Tikkanen, R. Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis. Cell Signal. 2009, 21, 1287-1297
    • (2009) Cell Signal , vol.21 , pp. 1287-1297
    • Babuke, T.1    Ruonala, M.2    Meister, M.3    Amaddii, M.4    Genzler, C.5    Esposito, A.6    Tikkanen, R.7
  • 13
    • 56949091061 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: A unique platform for cell signaling and PM remodeling
    • Donaldson, J.G.; Porat-Shliom, N.; Cohen, L.A. Clathrin-independent endocytosis: A unique platform for cell signaling and PM remodeling. Cell Signal. 2009, 21, 1-6
    • (2009) Cell Signal , vol.21 , pp. 1-6
    • Donaldson, J.G.1    Porat-Shliom, N.2    Cohen, L.A.3
  • 15
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon, H.T.; Boucrot, E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 2011, 12, 517-533
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 17
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton, R.G.; del Pozo, M.A. Caveolae as plasma membrane sensors, protectors and organizers. Nat. Rev. Mol. Cell Biol. 2013, 14, 98-112
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 98-112
    • Parton, R.G.1    del Pozo, M.A.2
  • 19
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P.; McIntosh, D.P.; Schnitzer, J.E. Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol. 1998, 141, 101-114
    • (1998) J. Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 20
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov, O.O.; Bright, N.A.; Nichols, B.J. Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat. Cell Biol. 2006, 8, 46-54
    • (2006) Nat. Cell Biol , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 21
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding
    • Frick, M.; Bright, N.A.; Riento, K.; Bray, A.; Merrified, C.; Nichols, B.J. Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding. Curr. Biol. 2007, 17, 1151-1156
    • (2007) Curr. Biol , vol.17 , pp. 1151-1156
    • Frick, M.1    Bright, N.A.2    Riento, K.3    Bray, A.4    Merrified, C.5    Nichols, B.J.6
  • 22
    • 84903778711 scopus 로고    scopus 로고
    • Role of dynamin and clathrin in the cellular trafficking of flotillins
    • Meister, M.; Zuk, A.; Tikkanen, R. Role of dynamin and clathrin in the cellular trafficking of flotillins. FEBS J. 2014, 281, 2956-2976
    • (2014) FEBS J , vol.281 , pp. 2956-2976
    • Meister, M.1    Zuk, A.2    Tikkanen, R.3
  • 23
    • 84856866968 scopus 로고    scopus 로고
    • The roles of flotillin microdomains-Endocytosis and beyond
    • Otto, G.P.; Nichols, B.J. The roles of flotillin microdomains-Endocytosis and beyond. J. Cell Sci. 2012, 124, 3933-3940
    • (2012) J. Cell Sci , vol.124 , pp. 3933-3940
    • Otto, G.P.1    Nichols, B.J.2
  • 24
    • 0037073697 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation
    • Morrow, I.C.; Rea, S.; Martin, S.; Prior, I.A.; Prohaska, R.; Hancock, J.F.; James, D.E.; Parton, R.G. Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. J. Biol. Chem. 2002, 277, 48834-48841
    • (2002) J. Biol. Chem , vol.277 , pp. 48834-48841
    • Morrow, I.C.1    Rea, S.2    Martin, S.3    Prior, I.A.4    Prohaska, R.5    Hancock, J.F.6    James, D.E.7    Parton, R.G.8
  • 25
    • 84855253929 scopus 로고    scopus 로고
    • DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
    • Li, Y.; Martin, B.R.; Cravatt, B.F.; Hofmann, S.L. DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells. J. Biol. Chem. 2012, 287, 523-530
    • (2012) J. Biol. Chem , vol.287 , pp. 523-530
    • Li, Y.1    Martin, B.R.2    Cravatt, B.F.3    Hofmann, S.L.4
  • 27
  • 28
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • Bickel, P.E.; Scherer, P.E.; Schnitzer, J.E.; Oh, P.; Lisanti, M.P.; Lodish, H.F. Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J. Biol. Chem. 1997, 272, 13793-13802
    • (1997) J. Biol. Chem , vol.272 , pp. 13793-13802
    • Bickel, P.E.1    Scherer, P.E.2    Schnitzer, J.E.3    Oh, P.4    Lisanti, M.P.5    Lodish, H.F.6
  • 29
    • 0033617415 scopus 로고    scopus 로고
    • Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
    • Volonte, D.; Galbiati, F.; Li, S.; Nishiyama, K.; Okamoto, T.; Lisanti, M.P. Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe. J. Biol. Chem. 1999, 274, 12702-12709
    • (1999) J. Biol. Chem , vol.274 , pp. 12702-12709
    • Volonte, D.1    Galbiati, F.2    Li, S.3    Nishiyama, K.4    Okamoto, T.5    Lisanti, M.P.6
  • 30
    • 34249701297 scopus 로고    scopus 로고
    • Reggie-1 and reggie-2 localize in non-caveolar rafts in epithelial cells: Cellular localization is not dependent on the expression of caveolin proteins
    • Fernow, I.; Icking, A.; Tikkanen, R. Reggie-1 and reggie-2 localize in non-caveolar rafts in epithelial cells: Cellular localization is not dependent on the expression of caveolin proteins. Eur. J. Cell Biol. 2007, 86, 345-352
    • (2007) Eur. J. Cell Biol , vol.86 , pp. 345-352
    • Fernow, I.1    Icking, A.2    Tikkanen, R.3
  • 31
    • 18144396107 scopus 로고    scopus 로고
    • The stomatin/prohibitin/ flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes
    • Liu, J.; Deyoung, S.M.; Zhang, M.; Dold, L.H.; Saltiel, A.R. The stomatin/prohibitin/ flotillin/HflK/C domain of flotillin-1 contains distinct sequences that direct plasma membrane localization and protein interactions in 3T3-L1 adipocytes. J. Biol. Chem. 2005, 280, 16125-16134
    • (2005) J. Biol. Chem , vol.280 , pp. 16125-16134
    • Liu, J.1    Deyoung, S.M.2    Zhang, M.3    Dold, L.H.4    Saltiel, A.R.5
  • 32
    • 33847387596 scopus 로고    scopus 로고
    • Role of EGF-induced tyrosine phosphorylation of reggie-1/flotillin-2 in cell spreading and signaling to the actin cytoskeleton
    • Neumann-Giesen, C.; Fernow, I.; Amaddii, M.; Tikkanen, R. Role of EGF-induced tyrosine phosphorylation of reggie-1/flotillin-2 in cell spreading and signaling to the actin cytoskeleton. J. Cell Sci. 2007, 120, 395-406
    • (2007) J. Cell Sci , vol.120 , pp. 395-406
    • Neumann-Giesen, C.1    Fernow, I.2    Amaddii, M.3    Tikkanen, R.4
  • 33
    • 66849106387 scopus 로고    scopus 로고
    • Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase
    • Riento, K.; Frick, M.; Schafer, I.; Nichols, B.J. Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase. J. Cell Sci. 2009, 122, 912-918
    • (2009) J. Cell Sci , vol.122 , pp. 912-918
    • Riento, K.1    Frick, M.2    Schafer, I.3    Nichols, B.J.4
  • 34
    • 84890129115 scopus 로고    scopus 로고
    • Function of Flotillins in Receptor Tyrosine Kinase Signaling and Endocytosis: Role of Tyrosine Phosphorylation and Oligomerization
    • Huang, C., Ed.; InTech Publisher: Rijeka, Croatia
    • Kurrle, N.; John, B.; Meister, M.; Tikkanen, R. Function of Flotillins in Receptor Tyrosine Kinase Signaling and Endocytosis: Role of Tyrosine Phosphorylation and Oligomerization. In Protein Phosphorylation in Human Health; Huang, C., Ed.; InTech Publisher: Rijeka, Croatia, 2012
    • (2012) Protein Phosphorylation In Human Health
    • Kurrle, N.1    John, B.2    Meister, M.3    Tikkanen, R.4
  • 35
    • 0035122581 scopus 로고    scopus 로고
    • Flotillin-1: Gene structure: CDNA cloning from human lung and the identification of alternative polyadenylation signals
    • Edgar, A.J.; Polak, J.M. Flotillin-1: Gene structure: CDNA cloning from human lung and the identification of alternative polyadenylation signals. Int. J. BioChem. Cell Biol. 2001, 33, 53-64
    • (2001) Int. J. BioChem. Cell Biol , vol.33 , pp. 53-64
    • Edgar, A.J.1    Polak, J.M.2
  • 36
    • 32044464800 scopus 로고    scopus 로고
    • Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: Convergent evolution of the SPFH domain
    • Rivera-Milla, E.; Stuermer, C.A.; Malaga-Trillo, E. Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: Convergent evolution of the SPFH domain. Cell Mol. Life Sci. 2006, 63, 343-357
    • (2006) Cell Mol. Life Sci , vol.63 , pp. 343-357
    • Rivera-Milla, E.1    Stuermer, C.A.2    Malaga-Trillo, E.3
  • 37
    • 84857746692 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 protein plays dual role in activation of receptor-tyrosine kinase/mitogenactivated protein kinase signaling
    • Amaddii, M.; Meister, M.; Banning, A.; Tomasovic, A.; Mooz, J.; Rajalingam, K.; Tikkanen, R. Flotillin-1/reggie-2 protein plays dual role in activation of receptor-tyrosine kinase/mitogenactivated protein kinase signaling. J. Biol. Chem. 2012, 287, 7265-7278
    • (2012) J. Biol. Chem , vol.287 , pp. 7265-7278
    • Amaddii, M.1    Meister, M.2    Banning, A.3    Tomasovic, A.4    Mooz, J.5    Rajalingam, K.6    Tikkanen, R.7
  • 38
    • 84888417935 scopus 로고    scopus 로고
    • Increased activity of mitogen activated protein kinase pathway in flotillin-2 knockout mouse model
    • Banning, A.; Regenbrecht, C.R.; Tikkanen, R. Increased activity of mitogen activated protein kinase pathway in flotillin-2 knockout mouse model. Cell Signal. 2014, 26, 198-207
    • (2014) Cell Signal , vol.26 , pp. 198-207
    • Banning, A.1    Regenbrecht, C.R.2    Tikkanen, R.3
  • 39
    • 84903789654 scopus 로고    scopus 로고
    • Flotillins in receptor tyrosine kinase signaling and cancer
    • Banning, A.; Kurrle, N.; Meister, M.; Tikkanen, R. Flotillins in receptor tyrosine kinase signaling and cancer. Cells 2014, 3, 129-149
    • (2014) Cells , vol.3 , pp. 129-149
    • Banning, A.1    Kurrle, N.2    Meister, M.3    Tikkanen, R.4
  • 40
    • 84875078622 scopus 로고    scopus 로고
    • Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount
    • Meister, M.; Tomasovic, A.; Banning, A.; Tikkanen, R. Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount. Int. J. Mol. Sci. 2013, 14, 4854-4884
    • (2013) Int. J. Mol. Sci , vol.14 , pp. 4854-4884
    • Meister, M.1    Tomasovic, A.2    Banning, A.3    Tikkanen, R.4
  • 41
    • 0035171631 scopus 로고    scopus 로고
    • Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2
    • Stuermer, C.A.; Lang, D.M.; Kirsch, F.; Wiechers, M.; Deininger, S.O.; Plattner, H. Glycosylphosphatidyl inositol-anchored proteins and fyn kinase assemble in noncaveolar plasma membrane microdomains defined by reggie-1 and -2. Mol. Biol. Cell 2001, 12, 3031-3045
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3031-3045
    • Stuermer, C.A.1    Lang, D.M.2    Kirsch, F.3    Wiechers, M.4    Deininger, S.O.5    Plattner, H.6
  • 42
    • 84883332951 scopus 로고    scopus 로고
    • Reggies/flotillins interact with Rab11a and SNX4 at the tubulovesicular recycling compartment and function in transferrin receptor and E-cadherin trafficking
    • Solis, G.P.; Hulsbusch, N.; Radon, Y.; Katanaev, V.L.; Plattner, H.; Stuermer, C.A. Reggies/flotillins interact with Rab11a and SNX4 at the tubulovesicular recycling compartment and function in transferrin receptor and E-cadherin trafficking. Mol. Biol. Cell 2013, 24, 2689-2702
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2689-2702
    • Solis, G.P.1    Hulsbusch, N.2    Radon, Y.3    Katanaev, V.L.4    Plattner, H.5    Stuermer, C.A.6
  • 43
    • 0033836520 scopus 로고    scopus 로고
    • The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components
    • Gagescu, R.; Demaurex, N.; Parton, R.G.; Hunziker, W.; Huber, L.A.; Gruenberg, J. The recycling endosome of Madin-Darby canine kidney cells is a mildly acidic compartment rich in raft components. Mol. Biol. Cell 2000, 11, 2775-2791
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2775-2791
    • Gagescu, R.1    Demaurex, N.2    Parton, R.G.3    Hunziker, W.4    Huber, L.A.5    Gruenberg, J.6
  • 46
    • 84899948104 scopus 로고    scopus 로고
    • Regulation of exosome release by glycosphingolipids and flotillins
    • Phuyal, S.; Hessvik, N.P.; Skotland, T.; Sandvig, K.; Llorente, A. Regulation of exosome release by glycosphingolipids and flotillins. FEBS J. 2014, 281, 2214-2227
    • (2014) FEBS J , vol.281 , pp. 2214-2227
    • Phuyal, S.1    Hessvik, N.P.2    Skotland, T.3    Sandvig, K.4    Llorente, A.5
  • 47
    • 84855335580 scopus 로고    scopus 로고
    • Molecular networks in FGF signaling: Flotillin-1 and cbl-associated protein compete for the binding to fibroblast growth factor receptor substrate 2
    • Tomasovic, A.; Traub, S.; Tikkanen, R. Molecular networks in FGF signaling: Flotillin-1 and cbl-associated protein compete for the binding to fibroblast growth factor receptor substrate 2. PLoS ONE 2012, 7, e29739
    • (2012) PLoS ONE , vol.7
    • Tomasovic, A.1    Traub, S.2    Tikkanen, R.3
  • 48
    • 79951579332 scopus 로고    scopus 로고
    • Flotillin-dependent endocytosis and a phagocytosis-like mechanism for cellular internalization of disulfide-based poly(amido amine)/DNA polyplexes
    • Vercauteren, D.; Piest, M.; van der Aa, L.J.; Al Soraj, M.; Jones, A.T.; Engbersen, J.F.; de Smedt, S.C.; Braeckmans, K. Flotillin-dependent endocytosis and a phagocytosis-like mechanism for cellular internalization of disulfide-based poly(amido amine)/DNA polyplexes. Biomaterials 2011, 32, 3072-3084
    • (2011) Biomaterials , vol.32 , pp. 3072-3084
    • Vercauteren, D.1    Piest, M.2    van der Aa, L.J.3    Al Soraj, M.4    Jones, A.T.5    Engbersen, J.F.6    de Smedt, S.C.7    Braeckmans, K.8
  • 49
    • 33947255616 scopus 로고    scopus 로고
    • Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands
    • Payne, C.K.; Jones, S.A.; Chen, C.; Zhuang, X. Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands. Traffic 2007, 8, 389-401
    • (2007) Traffic , vol.8 , pp. 389-401
    • Payne, C.K.1    Jones, S.A.2    Chen, C.3    Zhuang, X.4
  • 50
    • 79952265242 scopus 로고    scopus 로고
    • Flotillins play an essential role in Niemann-Pick C1-like 1-mediated cholesterol uptake
    • Ge, L.; Qi, W.; Wang, L.J.; Miao, H.H.; Qu, Y.X.; Li, B.L.; Song, B.L. Flotillins play an essential role in Niemann-Pick C1-like 1-mediated cholesterol uptake. Proc. Natl. Acad. Sci. USA 2011, 108, 551-556
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 551-556
    • Ge, L.1    Qi, W.2    Wang, L.J.3    Miao, H.H.4    Qu, Y.X.5    Li, B.L.6    Song, B.L.7
  • 52
    • 84862618219 scopus 로고    scopus 로고
    • siRNA and pharmacological inhibition of endocytic pathways to characterize the differential role of macropinocytosis and the actin cytoskeleton on cellular uptake of dextran and cationic cell penetrating peptides octaarginine (R8) and HIV-Tat
    • Al Soraj, M.; He, L.; Peynshaert, K.; Cousaert, J.; Vercauteren, D.; Braeckmans, K.; de Smedt, S.C.; Jones, A.T. siRNA and pharmacological inhibition of endocytic pathways to characterize the differential role of macropinocytosis and the actin cytoskeleton on cellular uptake of dextran and cationic cell penetrating peptides octaarginine (R8) and HIV-Tat. J. Control. Release 2012, 161, 132-141
    • (2012) J. Control. Release , vol.161 , pp. 132-141
    • Al Soraj, M.1    He, L.2    Peynshaert, K.3    Cousaert, J.4    Vercauteren, D.5    Braeckmans, K.6    de Smedt, S.C.7    Jones, A.T.8
  • 54
    • 0037446837 scopus 로고    scopus 로고
    • GM1-containing lipid rafts are depleted within clathrin-coated pits
    • Nichols, B.J. GM1-containing lipid rafts are depleted within clathrin-coated pits. Curr. Biol. 2003, 13, 686-690
    • (2003) Curr. Biol , vol.13 , pp. 686-690
    • Nichols, B.J.1
  • 55
    • 1842432088 scopus 로고    scopus 로고
    • Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts
    • Kusumi, A.; Koyama-Honda, I.; Suzuki, K. Molecular dynamics and interactions for creation of stimulation-induced stabilized rafts from small unstable steady-state rafts. Traffic 2004, 5, 213-230
    • (2004) Traffic , vol.5 , pp. 213-230
    • Kusumi, A.1    Koyama-Honda, I.2    Suzuki, K.3
  • 57
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • Schneider, A.; Rajendran, L.; Honsho, M.; Gralle, M.; Donnert, G.; Wouters, F.; Hell, S.W.; Simons, M. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J. NeuroSci. 2008, 28, 2874-2882
    • (2008) J. NeuroSci , vol.28 , pp. 2874-2882
    • Schneider, A.1    Rajendran, L.2    Honsho, M.3    Gralle, M.4    Donnert, G.5    Wouters, F.6    Hell, S.W.7    Simons, M.8
  • 59
    • 84861228341 scopus 로고    scopus 로고
    • Lipid raft redistribution and morphological cell polarization are separable processes providing a basis for hematopoietic stem and progenitor cell migration
    • Gorgens, A.; Beckmann, J.; Ludwig, A.K.; Mollmann, M.; Durig, J.; Horn, P.A.; Rajendran, L.; Giebel, B. Lipid raft redistribution and morphological cell polarization are separable processes providing a basis for hematopoietic stem and progenitor cell migration. Int. J. BioChem. Cell Biol. 2012, 44, 1121-1132
    • (2012) Int. J. BioChem. Cell Biol , vol.44 , pp. 1121-1132
    • Gorgens, A.1    Beckmann, J.2    Ludwig, A.K.3    Mollmann, M.4    Durig, J.5    Horn, P.A.6    Rajendran, L.7    Giebel, B.8
  • 63
    • 79959332509 scopus 로고    scopus 로고
    • Dynamic reorganization of flotillins in chemokine-stimulated human T-lymphocytes
    • Affentranger, S.; Martinelli, S.; Hahn, J.; Rossy, J.; Niggli, V. Dynamic reorganization of flotillins in chemokine-stimulated human T-lymphocytes. BMC Cell Biol. 2011, 12, 28
    • (2011) BMC Cell Biol , vol.12 , pp. 28
    • Affentranger, S.1    Martinelli, S.2    Hahn, J.3    Rossy, J.4    Niggli, V.5
  • 64
    • 65549095347 scopus 로고    scopus 로고
    • Flotillins interact with PSGL-1 in neutrophils and, upon stimulation, rapidly organize into membrane domains subsequently accumulating in the uropod
    • Rossy, J.; Schlicht, D.; Engelhardt, B.; Niggli, V. Flotillins interact with PSGL-1 in neutrophils and, upon stimulation, rapidly organize into membrane domains subsequently accumulating in the uropod. PLoS ONE 2009, 4, e5403
    • (2009) PLoS ONE , vol.4
    • Rossy, J.1    Schlicht, D.2    Engelhardt, B.3    Niggli, V.4
  • 65
    • 78349264648 scopus 로고    scopus 로고
    • Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment
    • Ludwig, A.; Otto, G.P.; Riento, K.; Hams, E.; Fallon, P.G.; Nichols, B.J. Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment. J. Cell Biol. 2010, 191, 771-781
    • (2010) J. Cell Biol , vol.191 , pp. 771-781
    • Ludwig, A.1    Otto, G.P.2    Riento, K.3    Hams, E.4    Fallon, P.G.5    Nichols, B.J.6
  • 66
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan, S.; Simpson, R.J. ExoCarta: A compendium of exosomal proteins and RNA. Proteomics 2009, 9, 4997-5000
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 69
    • 84899411384 scopus 로고    scopus 로고
    • Flotillins bind to the dileucine sorting motif of beta-site amyloid precursor protein-cleaving enzyme 1 and influence its endosomal sorting
    • John, B.A.; Meister, M.; Banning, A.; Tikkanen, R. Flotillins bind to the dileucine sorting motif of beta-site amyloid precursor protein-cleaving enzyme 1 and influence its endosomal sorting. FEBS J. 2014, 281, 2074-2087
    • (2014) FEBS J , vol.281 , pp. 2074-2087
    • John, B.A.1    Meister, M.2    Banning, A.3    Tikkanen, R.4
  • 70
    • 84874377202 scopus 로고    scopus 로고
    • Extracellular vesicles: Exosomes, microvesicles, and friends
    • Raposo, G.; Stoorvogel, W. Extracellular vesicles: Exosomes, microvesicles, and friends. J. Cell Biol. 2013, 200, 373-383
    • (2013) J. Cell Biol , vol.200 , pp. 373-383
    • Raposo, G.1    Stoorvogel, W.2
  • 72
    • 66449086207 scopus 로고    scopus 로고
    • Proteomics of MUC1-containing lipid rafts from plasma membranes and exosomes of human breast carcinoma cells MCF-7
    • Staubach, S.; Razawi, H.; Hanisch, F.G. Proteomics of MUC1-containing lipid rafts from plasma membranes and exosomes of human breast carcinoma cells MCF-7. Proteomics 2009, 9, 2820-2835
    • (2009) Proteomics , vol.9 , pp. 2820-2835
    • Staubach, S.1    Razawi, H.2    Hanisch, F.G.3
  • 74
    • 0037205737 scopus 로고    scopus 로고
    • Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: Implications on the endocytosis mechanism of memapsin 2
    • He, X.; Chang, W.P.; Koelsch, G.; Tang, J. Memapsin 2 (beta-secretase) cytosolic domain binds to the VHS domains of GGA1 and GGA2: Implications on the endocytosis mechanism of memapsin 2. FEBS Lett. 2002, 524, 183-187
    • (2002) FEBS Lett , vol.524 , pp. 183-187
    • He, X.1    Chang, W.P.2    Koelsch, G.3    Tang, J.4
  • 75
    • 0036200884 scopus 로고    scopus 로고
    • The carboxyl-terminus of BACE contains a sorting signal that regulates BACE trafficking but not the formation of total A(beta)
    • Pastorino, L.; Ikin, A.F.; Nairn, A.C.; Pursnani, A.; Buxbaum, J.D. The carboxyl-terminus of BACE contains a sorting signal that regulates BACE trafficking but not the formation of total A(beta). Mol. Cell NeuroSci. 2002, 19, 175-185
    • (2002) Mol. Cell NeuroSci , vol.19 , pp. 175-185
    • Pastorino, L.1    Ikin, A.F.2    Nairn, A.C.3    Pursnani, A.4    Buxbaum, J.D.5
  • 79
    • 84861123391 scopus 로고    scopus 로고
    • Reggies/flotillins regulate E-cadherin-mediated cell contact formation by affecting EGFR trafficking
    • Solis, G.P.; Schrock, Y.; Hulsbusch, N.; Wiechers, M.; Plattner, H.; Stuermer, C.A. Reggies/flotillins regulate E-cadherin-mediated cell contact formation by affecting EGFR trafficking. Mol. Biol. Cell 2012, 23, 1812-1825
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1812-1825
    • Solis, G.P.1    Schrock, Y.2    Hulsbusch, N.3    Wiechers, M.4    Plattner, H.5    Stuermer, C.A.6
  • 80
    • 84878159356 scopus 로고    scopus 로고
    • Flotillins regulate membrane mobility of the dopamine transporter but are not required for its protein kinase C dependent endocytosis
    • Sorkina, T.; Caltagarone, J.; Sorkin, A. Flotillins regulate membrane mobility of the dopamine transporter but are not required for its protein kinase C dependent endocytosis. Traffic 2013, 14, 709-724
    • (2013) Traffic , vol.14 , pp. 709-724
    • Sorkina, T.1    Caltagarone, J.2    Sorkin, A.3
  • 81
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo, E.H.; Squazzo, S.L. Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 1994, 269, 17386-17389
    • (1994) J. Biol. Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 82
    • 0029950149 scopus 로고    scopus 로고
    • Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody
    • Koo, E.H.; Squazzo, S.L.; Selkoe, D.J.; Koo, C.H. Trafficking of cell-surface amyloid beta-protein precursor. I. Secretion, endocytosis and recycling as detected by labeled monoclonal antibody. J. Cell Sci. 1996, 109, 991-998
    • (1996) J. Cell Sci , vol.109 , pp. 991-998
    • Koo, E.H.1    Squazzo, S.L.2    Selkoe, D.J.3    Koo, C.H.4
  • 83
    • 0033516554 scopus 로고    scopus 로고
    • Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42
    • Perez, R.G.; Soriano, S.; Hayes, J.D.; Ostaszewski, B.; Xia, W.; Selkoe, D.J.; Chen, X.; Stokin, G.B.; Koo, E.H. Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42. J. Biol. Chem. 1999, 274, 18851-18856
    • (1999) J. Biol. Chem , vol.274 , pp. 18851-18856
    • Perez, R.G.1    Soriano, S.2    Hayes, J.D.3    Ostaszewski, B.4    Xia, W.5    Selkoe, D.J.6    Chen, X.7    Stokin, G.B.8    Koo, E.H.9
  • 84
    • 12744281091 scopus 로고    scopus 로고
    • Constitutive and protein kinase C-induced internalization of the dopamine transporter is mediated by a clathrin-dependent mechanism
    • Sorkina, T.; Hoover, B.R.; Zahniser, N.R.; Sorkin, A. Constitutive and protein kinase C-induced internalization of the dopamine transporter is mediated by a clathrin-dependent mechanism. Traffic 2005, 6, 157-170
    • (2005) Traffic , vol.6 , pp. 157-170
    • Sorkina, T.1    Hoover, B.R.2    Zahniser, N.R.3    Sorkin, A.4
  • 85
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund, S.; Argenzio, E.; Tosoni, D.; Cavallaro, E.; Polo, S.; di Fiore, P.P. Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell 2008, 15, 209-219
    • (2008) Dev. Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5    di Fiore, P.P.6
  • 89
    • 44349126634 scopus 로고    scopus 로고
    • The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1
    • Ge, L.; Wang, J.; Qi, W.; Miao, H.H.; Cao, J.; Qu, Y.X.; Li, B.L.; Song, B.L. The cholesterol absorption inhibitor ezetimibe acts by blocking the sterol-induced internalization of NPC1L1. Cell Metab. 2008, 7, 508-519
    • (2008) Cell Metab , vol.7 , pp. 508-519
    • Ge, L.1    Wang, J.2    Qi, W.3    Miao, H.H.4    Cao, J.5    Qu, Y.X.6    Li, B.L.7    Song, B.L.8
  • 90
    • 77950407292 scopus 로고    scopus 로고
    • Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors
    • Abrami, L.; Bischofberger, M.; Kunz, B.; Groux, R.; van der Goot, F.G. Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathog. 2010, 6, e1000792
    • (2010) PLoS Pathog , vol.6
    • Abrami, L.1    Bischofberger, M.2    Kunz, B.3    Groux, R.4    van der Goot, F.G.5
  • 91
    • 76549104967 scopus 로고    scopus 로고
    • Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake
    • Abrami, L.; Kunz, B.; van der Goot, F.G. Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake. Proc. Natl. Acad. Sci. USA 2010, 107, 1420-1424
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 1420-1424
    • Abrami, L.1    Kunz, B.2    van der Goot, F.G.3
  • 92
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami, L.; Liu, S.; Cosson, P.; Leppla, S.H.; van der Goot, F.G. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 2003, 160, 321-328
    • (2003) J. Cell Biol , vol.160 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    van der Goot, F.G.5
  • 93
    • 33746618384 scopus 로고    scopus 로고
    • Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1
    • Deinhardt, K.; Berninghausen, O.; Willison, H.J.; Hopkins, C.R.; Schiavo, G. Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1. J. Cell Biol. 2006, 174, 459-471
    • (2006) J. Cell Biol , vol.174 , pp. 459-471
    • Deinhardt, K.1    Berninghausen, O.2    Willison, H.J.3    Hopkins, C.R.4    Schiavo, G.5
  • 94
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles
    • Van Dam, E.M.; Stoorvogel, W. Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol. Biol. Cell 2002, 13, 169-182
    • (2002) Mol. Biol. Cell , vol.13 , pp. 169-182
    • van Dam, E.M.1    Stoorvogel, W.2
  • 95
    • 0037073739 scopus 로고    scopus 로고
    • Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways
    • Van Dam, E.M.; Ten Broeke, T.; Jansen, K.; Spijkers, P.; Stoorvogel, W. Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways. J. Biol. Chem. 2002, 277, 48876-48883.
    • (2002) J. Biol. Chem , vol.277 , pp. 48876-48883
    • van Dam, E.M.1    Ten Broeke, T.2    Jansen, K.3    Spijkers, P.4    Stoorvogel, W.5


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