메뉴 건너뛰기




Volumn 191, Issue 4, 2010, Pages 771-781

Flotillin microdomains interact with the cortical cytoskeleton to control uropod formation and neutrophil recruitment

Author keywords

[No Author keywords available]

Indexed keywords

FLOTILLIN 1; FLOTILLIN 2; FORMYLMETHIONYLLEUCYLPHENYLALANINE; MYOSIN IIA; SPECTRIN;

EID: 78349264648     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201005140     Document Type: Article
Times cited : (98)

References (46)
  • 1
    • 34547726345 scopus 로고    scopus 로고
    • Dissecting the molecular function of reggie/flotillin proteins
    • doi:10.1016/ j.ejcb.2007.03.003
    • Babuke, T., and R. Tikkanen. 2007. Dissecting the molecular function of reggie/flotillin proteins. Eur. J. Cell Biol. 86:525-532. doi:10.1016/ j.ejcb.2007.03.003
    • (2007) Eur. J. Cell Biol. , vol.86 , pp. 525-532
    • Babuke, T.1    Tikkanen, R.2
  • 2
    • 67349189783 scopus 로고    scopus 로고
    • Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis
    • doi:10.1016/j.cellsig.2009.03.012
    • Babuke, T., M. Ruonala, M. Meister, M. Amaddii, C. Genzler, A. Esposito, and R. Tikkanen. 2009. Hetero-oligomerization of reggie-1/flotillin-2 and reggie-2/flotillin-1 is required for their endocytosis. Cell. Signal. 21:1287-1297. doi:10.1016/j.cellsig.2009.03.012
    • (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
  • 3
    • 0031010267 scopus 로고    scopus 로고
    • Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins
    • doi:10.1074/jbc.272.21.13793
    • Bickel, P.E., P.E. Scherer, J.E. Schnitzer, P. Oh, M.P. Lisanti, and H.F. Lodish. 1997. Flotillin and epidermal surface antigen define a new family of caveolae-associated integral membrane proteins. J. Biol. Chem. 272: 13793-13802. doi:10.1074/jbc.272.21.13793
    • (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
  • 4
    • 53549118575 scopus 로고    scopus 로고
    • Cripto recruits Furin and PACE4 and controls Nodal trafficking during proteolytic maturation
    • doi:10.1038/emboj.2008.174
    • Blanchet, M.H., J.A. Le Good, D. Mesnard, V. Oorschot, S. Baflast, G. Minchiotti, J. Klumperman, and D.B. Constam. 2008. Cripto recruits Furin and PACE4 and controls Nodal trafficking during proteolytic maturation. EMBO J. 27:2580-2591. doi:10.1038/emboj.2008.174
    • (2008) EMBO J. , vol.27 , pp. 2580-2591
    • Blanchet, M.H.1    Le Good, J.A.2    Mesnard, D.3    Oorschot, V.4    Baflast, S.5    Minchiotti, G.6    Klumperman, J.7    Constam, D.B.8
  • 5
    • 10344239445 scopus 로고    scopus 로고
    • Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct
    • doi:10.1074/jbc.M408565200
    • Chou, C.L., B.M. Christensen, S. Frische, H. Vorum, R.A. Desai, J.D. Hoffert, P. de Lanerolle, S. Nielsen, and M.A. Knepper. 2004. Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct. J. Biol. Chem. 279:49026-49035. doi:10.1074/jbc.M408565200
    • (2004) J. Biol. Chem. , vol.279 , pp. 49026-49035
    • Chou, C.L.1    Christensen, B.M.2    Frische, S.3    Vorum, H.4    Desai, R.A.5    Hoffert, J.D.6    De Lanerolle, P.7    Nielsen, S.8    Knepper, M.A.9
  • 6
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • doi:10.1242/jcs.007112
    • Conti, M.A., and R.S. Adelstein. 2008. Nonmuscle myosin II moves in new directions. J. Cell Sci. 121:11-18. doi:10.1242/jcs.007112
    • (2008) J. Cell Sci. , vol.121 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 7
    • 0027260841 scopus 로고
    • Neutrophils, differentiated macrophages, and monocyte/macrophage antigen presenting cells infiltrate murine epidermis after UV injury
    • doi:10.1111/1523-1747.ep12363639
    • Cooper, K.D., N. Duraiswamy, C. Hammerberg, E. Allen, C. Kimbrough-Green, W. Dillon, and D. Thomas. 1993. Neutrophils, differentiated macrophages, and monocyte/macrophage antigen presenting cells infiltrate murine epidermis after UV injury. J. Invest. Dermatol. 101:155-163. doi:10.1111/1523-1747.ep12363639
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 155-163
    • Cooper, K.D.1    Duraiswamy, N.2    Hammerberg, C.3    Allen, E.4    Kimbrough-Green, C.5    Dillon, W.6    Thomas, D.7
  • 8
    • 0141741538 scopus 로고    scopus 로고
    • MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils
    • doi:10.1016/S0898-6568(03)00074-3
    • Coxon, P.Y., M.J. Rane, S. Uriarte, D.W. Powell, S. Singh, W. Butt, Q. Chen, and K.R. McLeish. 2003. MAPK-activated protein kinase-2 participates in p38 MAPK-dependent and ERK-dependent functions in human neutrophils. Cell. Signal. 15:993-1001. doi:10.1016/S0898-6568(03)00074-3
    • (2003) Cell. Signal. , vol.15 , pp. 993-1001
    • Coxon, P.Y.1    Rane, M.J.2    Uriarte, S.3    Powell, D.W.4    Singh, S.5    Butt, W.6    Chen, Q.7    McLeish, K.R.8
  • 9
    • 0028863513 scopus 로고
    • Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of cAMP signaling pathway
    • doi:10.1083/jcb.131.2.495
    • del Pozo, M.A., P. Sánchez-Mateos, M. Nieto, and F. Sánchez-Madrid. 1995. Chemokines regulate cellular polarization and adhesion receptor redistribution during lymphocyte interaction with endothelium and extracellular matrix. Involvement of cAMP signaling pathway. J. Cell Biol. 131:495-508. doi:10.1083/jcb.131.2.495
    • (1995) J. Cell Biol. , vol.131 , pp. 495-508
    • Del Pozo, M.A.1    Sánchez-Mateos, P.2    Nieto, M.3    Sánchez-Madrid, F.4
  • 10
    • 61449181308 scopus 로고    scopus 로고
    • One-dimensional topography underlies three-dimensional fibrillar cell migration
    • doi:10.1083/jcb.200810041
    • Doyle, A.D., F.W. Wang, K. Matsumoto, and K.M. Yamada. 2009. One-dimensional topography underlies three-dimensional fibrillar cell migration. J. Cell Biol. 184:481-490. doi:10.1083/jcb.200810041
    • (2009) J. Cell Biol. , vol.184 , pp. 481-490
    • Doyle, A.D.1    Wang, F.W.2    Matsumoto, K.3    Yamada, K.M.4
  • 11
    • 0034107669 scopus 로고    scopus 로고
    • Ca2+-dependent myosin II activation is required for uropod retraction during neutrophil migration
    • Eddy, R.J., L.M. Pierini, F. Matsumura, and F.R. Maxfield. 2000. Ca2+-dependent myosin II activation is required for uropod retraction during neutrophil migration. J. Cell Sci. 113:1287-1298.
    • (2000) J. Cell Sci. , vol.113 , pp. 1287-1298
    • Eddy, R.J.1    Pierini, L.M.2    Matsumura, F.3    Maxfield, F.R.4
  • 12
    • 24644459023 scopus 로고    scopus 로고
    • Cell migration in 3D matrix
    • doi:10.1016/j.ceb.2005.08.015
    • Even-Ram, S., and K.M. Yamada. 2005. Cell migration in 3D matrix. Curr. Opin. Cell Biol. 17:524-532. doi:10.1016/j.ceb.2005.08.015
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 524-532
    • Even-Ram, S.1    Yamada, K.M.2
  • 13
    • 33846858648 scopus 로고    scopus 로고
    • Rho GTPase Rac1 is critical for neutrophil migration into the lung
    • doi:10.1182/blood-2006-04-017731
    • Filippi, M.D., K. Szczur, C.E. Harris, and P.Y. Berclaz. 2007. Rho GTPase Rac1 is critical for neutrophil migration into the lung. Blood. 109:1257-1264. doi:10.1182/blood-2006-04-017731
    • (2007) Blood , vol.109 , pp. 1257-1264
    • Filippi, M.D.1    Szczur, K.2    Harris, C.E.3    Berclaz, P.Y.4
  • 14
    • 34250851923 scopus 로고    scopus 로고
    • Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding
    • doi:10.1016/j.cub.2007.05.078
    • Frick, M., N.A. Bright, K. Riento, A. Bray, C. Merrified, and B.J. Nichols. 2007. Coassembly of flotillins induces formation of membrane microdomains, membrane curvature, and vesicle budding. Curr. Biol. 17:1151-1156. doi:10.1016/j.cub.2007.05.078
    • (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
  • 15
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrinindependent endocytic pathway in mammalian cells
    • doi:10.1038/ncb1342
    • Glebov, O.O., N.A. Bright, and B.J. Nichols. 2006. Flotillin-1 defines a clathrinindependent endocytic pathway in mammalian cells. Nat. Cell Biol. 8:46-54. doi:10.1038/ncb1342
    • (2006) Nat. Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 17
    • 0026773055 scopus 로고
    • Translocation of spectrin and protein kinase C to a cytoplasmic aggregate upon lymphocyte activation
    • doi:10.1073/ pnas.89.11.4947
    • Gregorio, C.C., R.T. Kubo, R.B. Bankert, and E.A. Repasky. 1992. Translocation of spectrin and protein kinase C to a cytoplasmic aggregate upon lymphocyte activation. Proc. Natl. Acad. Sci. USA. 89:4947-4951. doi:10.1073/ pnas.89.11.4947
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4947-4951
    • Gregorio, C.C.1    Kubo, R.T.2    Bankert, R.B.3    Repasky, E.A.4
  • 18
    • 69449096573 scopus 로고    scopus 로고
    • Molecular mechanisms of clathrin-independent endocytosis
    • doi:10.1242/jcs.033951
    • Hansen, C.G., and B.J. Nichols. 2009. Molecular mechanisms of clathrin-independent endocytosis. J. Cell Sci. 122:1713-1721. doi:10.1242/jcs.033951
    • (2009) J. Cell Sci. , vol.122 , pp. 1713-1721
    • Hansen, C.G.1    Nichols, B.J.2
  • 19
    • 26244449664 scopus 로고    scopus 로고
    • Lossand gain-of-function analysis of the lipid raft proteins Reggie/Flotillin in Drosophila: They are posttranslationally regulated, and misexpression interferes with wing and eye development
    • doi:10.1016/j.mcn.2005.07.007
    • Hoehne, M., H.G. de Couet, C.A. Stuermer, and K.F. Fischbach. 2005. Lossand gain-of-function analysis of the lipid raft proteins Reggie/Flotillin in Drosophila: they are posttranslationally regulated, and misexpression interferes with wing and eye development. Mol. Cell. Neurosci. 30:326-338. doi:10.1016/j.mcn.2005.07.007
    • (2005) Mol. Cell. Neurosci. , vol.30 , pp. 326-338
    • Hoehne, M.1    De Couet, H.G.2    Stuermer, C.A.3    Fischbach, K.F.4
  • 20
    • 61449225547 scopus 로고    scopus 로고
    • Myosin-IIA and ICAM-1 regulate the interchange between two distinct modes of T cell migration
    • doi:10 .4049/jimmunol.0803267
    • Jacobelli, J., F.C. Bennett, P. Pandurangi, A.J. Tooley, and M.F. Krummel. 2009. Myosin-IIA and ICAM-1 regulate the interchange between two distinct modes of T cell migration. J. Immunol. 182:2041-2050. doi:10 .4049/jimmunol.0803267
    • (2009) J. Immunol. , vol.182 , pp. 2041-2050
    • Jacobelli, J.1    Bennett, F.C.2    Pandurangi, P.3    Tooley, A.J.4    Krummel, M.F.5
  • 21
    • 66049157165 scopus 로고    scopus 로고
    • Induction of CCR2-dependent macrophage accumulation by oxidized phospholipids in the air-pouch model of inflammation
    • doi:10.1002/ art.24448
    • Kadl, A., E. Galkina, and N. Leitinger. 2009. Induction of CCR2-dependent macrophage accumulation by oxidized phospholipids in the air-pouch model of inflammation. Arthritis Rheum. 60:1362-1371. doi:10.1002/ art.24448
    • (2009) Arthritis Rheum. , vol.60 , pp. 1362-1371
    • Kadl, A.1    Galkina, E.2    Leitinger, N.3
  • 22
    • 33745308786 scopus 로고    scopus 로고
    • Flotillin-1 regulates IgE receptor-mediated signaling in rat basophilic leukemia (RBL-2H3) cells
    • Kato, N., M. Nakanishi, and N. Hirashima. 2006. Flotillin-1 regulates IgE receptor-mediated signaling in rat basophilic leukemia (RBL-2H3) cells. J. Immunol. 177:147-154.
    • (2006) J. Immunol. , vol.177 , pp. 147-154
    • Kato, N.1    Nakanishi, M.2    Hirashima, N.3
  • 23
    • 0020360978 scopus 로고
    • Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS sarcoma
    • doi:10.1021/bi00267a025
    • Kleinman, H.K., M.L. McGarvey, L.A. Liotta, P.G. Robey, K. Tryggvason, and G.R. Martin. 1982. Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS sarcoma. Biochemistry. 21:6188-6193. doi:10.1021/bi00267a025
    • (1982) Biochemistry , vol.21 , pp. 6188-6193
    • Kleinman, H.K.1    McGarvey, M.L.2    Liotta, L.A.3    Robey, P.G.4    Tryggvason, K.5    Martin, G.R.6
  • 24
    • 33748857158 scopus 로고    scopus 로고
    • Neutrophil infiltration and chemokines
    • Kobayashi, Y. 2006. Neutrophil infiltration and chemokines. Crit. Rev. Immunol. 26:307-316.
    • (2006) Crit. Rev. Immunol. , vol.26 , pp. 307-316
    • Kobayashi, Y.1
  • 25
    • 0031795591 scopus 로고    scopus 로고
    • Identification of reggie-1 and reggie-2 as plasmamembrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in non-caveolar micropatches in neurons
    • doi:10.1002/(SICI)1097-4695(199812)37:4〈502::AIDNEU2〉 3.0.CO;2-S
    • Lang, D.M., S. Lommel, M. Jung, R. Ankerhold, B. Petrausch, U. Laessing, M.F. Wiechers, H. Plattner, and C.A. Stuermer. 1998. Identification of reggie-1 and reggie-2 as plasmamembrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in non-caveolar micropatches in neurons. J. Neurobiol. 37:502-523. doi:10.1002/(SICI)1097-4695(199812)37: 4〈502::AIDNEU2〉 3.0.CO;2-S
    • (1998) J. Neurobiol. , vol.37 , pp. 502-523
    • Lang, D.M.1    Lommel, S.2    Jung, M.3    Ankerhold, R.4    Petrausch, B.5    Laessing, U.6    Wiechers, M.F.7    Plattner, H.8    Stuermer, C.A.9
  • 26
    • 34548664143 scopus 로고    scopus 로고
    • Linking membrane microdomains to the cytoskeleton: Regulation of the lateral mobility of reggie-1/flotillin-2 by interaction with actin
    • doi:10.1016/j.febslet.2007.08.074
    • Langhorst, M.F., G.P. Solis, S. Hannbeck, H. Plattner, and C.A. Stuermer. 2007. Linking membrane microdomains to the cytoskeleton: regulation of the lateral mobility of reggie-1/flotillin-2 by interaction with actin. FEBS Lett. 581:4697-4703. doi:10.1016/j.febslet.2007.08.074
    • (2007) FEBS Lett. , vol.581 , pp. 4697-4703
    • Langhorst, M.F.1    Solis, G.P.2    Hannbeck, S.3    Plattner, H.4    Stuermer, C.A.5
  • 28
    • 7244247060 scopus 로고    scopus 로고
    • Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation
    • doi:10.1083/jcb.200403091
    • Lee, J.H., T. Katakai, T. Hara, H. Gonda, M. Sugai, and A. Shimizu. 2004. Roles of p-ERM and Rho-ROCK signaling in lymphocyte polarity and uropod formation. J. Cell Biol. 167:327-337. doi:10.1083/jcb.200403091
    • (2004) J. Cell Biol. , vol.167 , pp. 327-337
    • Lee, J.H.1    Katakai, T.2    Hara, T.3    Gonda, H.4    Sugai, M.5    Shimizu, A.6
  • 29
    • 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
    • doi:10.1042/BJ20031100
    • Neumann-Giesen, C., B. Falkenbach, P. Beicht, S. Claasen, G. Lüers, C.A. Stuermer, V. Herzog, and R. Tikkanen. 2004. Membrane and raft association of reggie-1/flotillin-2: role of myristoylation, palmitoylation and oligomerization and induction of filopodia by overexpression. Biochem. J. 378:509-518. doi:10.1042/BJ20031100
    • (2004) Biochem. J. , vol.378 , pp. 509-518
    • Neumann-Giesen, C.1    Falkenbach, B.2    Beicht, P.3    Claasen, S.4    Lüers, G.5    Stuermer, C.A.6    Herzog, V.7    Tikkanen, R.8
  • 30
    • 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
    • doi:10.1242/jcs.03336
    • Neumann-Giesen, C., I. Fernow, M. Amaddii, and R. Tikkanen. 2007. Role of EGF-induced tyrosine phosphorylation of reggie-1/flotillin-2 in cell spreading and signaling to the actin cytoskeleton. J. Cell Sci. 120:395-406. doi:10.1242/jcs.03336
    • (2007) J. Cell Sci. , vol.120 , pp. 395-406
    • Neumann-Giesen, C.1    Fernow, I.2    Amaddii, M.3    Tikkanen, R.4
  • 31
    • 33947255616 scopus 로고    scopus 로고
    • Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands
    • doi:10.1111/j.1600-0854.2007.00540.x
    • Payne, C.K., S.A. Jones, C. Chen, and X. Zhuang. 2007. Internalization and trafficking of cell surface proteoglycans and proteoglycan-binding ligands. Traffic. 8:389-401. doi:10.1111/j.1600-0854.2007.00540.x
    • (2007) Traffic , vol.8 , pp. 389-401
    • Payne, C.K.1    Jones, S.A.2    Chen, C.3    Zhuang, X.4
  • 32
    • 77949504578 scopus 로고    scopus 로고
    • Flotillins are involved in the polarization of primitive and mature hematopoietic cells
    • doi:10.1371/journal.pone.0008290
    • Rajendran, L., J. Beckmann, A. Magenau, E.M. Boneberg, K. Gaus, A. Viola, B. Giebel, and H. Illges. 2009. Flotillins are involved in the polarization of primitive and mature hematopoietic cells. PLoS One. 4:e8290. doi:10.1371/journal.pone.0008290
    • (2009) PLoS One , vol.4
    • Rajendran, L.1    Beckmann, J.2    Magenau, A.3    Boneberg, E.M.4    Gaus, K.5    Viola, A.6    Giebel, B.7    Illges, H.8
  • 33
    • 66849106387 scopus 로고    scopus 로고
    • Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase
    • doi: 10.1242/jcs.039024
    • Riento, K., M. Frick, I. Schafer, and B.J. Nichols. 2009. Endocytosis of flotillin-1 and flotillin-2 is regulated by Fyn kinase. J. Cell Sci. 122:912-918. doi: 10.1242/jcs.039024
    • (2009) J. Cell Sci. , vol.122 , pp. 912-918
    • Riento, K.1    Frick, M.2    Schafer, I.3    Nichols, B.J.4
  • 34
    • 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
    • doi:10.1371/journal.pone.0005403
    • Rossy, J., D. Schlicht, B. Engelhardt, and V. Niggli. 2009. Flotillins interact with PSGL-1 in neutrophils and, upon stimulation, rapidly organize into membrane domains subsequently accumulating in the uropod. PLoS One. 4:e5403. doi:10.1371/journal.pone.0005403
    • (2009) PLoS One , vol.4
    • Rossy, J.1    Schlicht, D.2    Engelhardt, B.3    Niggli, V.4
  • 35
    • 0036826835 scopus 로고    scopus 로고
    • Endothelial Rho and Rho kinase regulate neutrophil migration via endothelial myosin light chain phosphorylation
    • Saito, H., Y. Minamiya, S. Saito, and J. Ogawa. 2002. Endothelial Rho and Rho kinase regulate neutrophil migration via endothelial myosin light chain phosphorylation. J. Leukoc. Biol. 72:829-836.
    • (2002) J. Leukoc. Biol. , vol.72 , pp. 829-836
    • Saito, H.1    Minamiya, Y.2    Saito, S.3    Ogawa, J.4
  • 36
    • 67349256860 scopus 로고    scopus 로고
    • Bringing up the rear: Defining the roles of the uropod
    • doi:10 .1038/nrm2680
    • Sánchez-Madrid, F., and J.M. Serrador. 2009. Bringing up the rear: defining the roles of the uropod. Nat. Rev. Mol. Cell Biol. 10:353-359. doi:10 .1038/nrm2680
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 353-359
    • Sánchez-Madrid, F.1    Serrador, J.M.2
  • 37
    • 40849097929 scopus 로고    scopus 로고
    • Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons
    • doi:10.1523/ JNEUROSCI.5345-07.2008
    • Schneider, A., L. Rajendran, M. Honsho, M. Gralle, G. Donnert, F. Wouters, S.W. Hell, and M. Simons. 2008. Flotillin-dependent clustering of the amyloid precursor protein regulates its endocytosis and amyloidogenic processing in neurons. J. Neurosci. 28:2874-2882. doi:10.1523/ JNEUROSCI.5345-07.2008
    • (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
  • 38
    • 0035200201 scopus 로고    scopus 로고
    • Cytoskeleton-dependent membrane domain segregation during neutrophil polarization
    • Seveau, S., R.J. Eddy, F.R. Maxfield, and L.M. Pierini. 2001. Cytoskeleton-dependent membrane domain segregation during neutrophil polarization. Mol. Biol. Cell. 12:3550-3562.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 3550-3562
    • Seveau, S.1    Eddy, R.J.2    Maxfield, F.R.3    Pierini, L.M.4
  • 40
    • 0037216850 scopus 로고    scopus 로고
    • Lowering the barriers to random walks on the cell surface
    • doi:10.1016/S0006-3495(03)74860-7
    • Tang, Q., and M. Edidin. 2003. Lowering the barriers to random walks on the cell surface. Biophys. J. 84:400-407. doi:10.1016/S0006-3495(03)74860-7
    • (2003) Biophys. J. , vol.84 , pp. 400-407
    • Tang, Q.1    Edidin, M.2
  • 41
    • 0036784639 scopus 로고    scopus 로고
    • The beta-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages
    • Taylor, P.R., G.D. Brown, D.M. Reid, J.A. Willment, L. Martinez-Pomares, S. Gordon, and S.Y. Wong. 2002. The beta-glucan receptor, dectin-1, is predominantly expressed on the surface of cells of the monocyte/macrophage and neutrophil lineages. J. Immunol. 169:3876-3882.
    • (2002) J. Immunol. , vol.169 , pp. 3876-3882
    • Taylor, P.R.1    Brown, G.D.2    Reid, D.M.3    Willment, J.A.4    Martinez-Pomares, L.5    Gordon, S.6    Wong, S.Y.7
  • 42
    • 0024576739 scopus 로고
    • Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay
    • Umemoto, S., A.R. Bengur, and J.R. Sellers. 1989. Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay. J. Biol. Chem. 264:1431-1436.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1431-1436
    • Umemoto, S.1    Bengur, A.R.2    Sellers, J.R.3
  • 43
    • 70350454867 scopus 로고    scopus 로고
    • Nonmuscle myosin II takes centre stage in cell adhesion and migration
    • doi:10.1038/nrm2786
    • Vicente-Manzanares, M., X. Ma, R.S. Adelstein, and A.R. Horwitz. 2009. Nonmuscle myosin II takes centre stage in cell adhesion and migration. Nat. Rev. Mol. Cell Biol. 10:778-790. doi:10.1038/nrm2786
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 778-790
    • Vicente-Manzanares, M.1    Ma, X.2    Adelstein, R.S.3    Horwitz, A.R.4
  • 44
    • 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
    • doi:10.1074/jbc.274.18.12702
    • Volonte, D., F. Galbiati, S. Li, K. Nishiyama, T. Okamoto, and M.P. Lisanti. 1999. 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. 274:12702-12709. doi:10.1074/jbc.274.18.12702
    • (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
  • 45
  • 46
    • 70350389560 scopus 로고    scopus 로고
    • Alternate raft pathways cooperate to mediate slow diffusion and efficient uptake of a sphingolipid tracer to degradative and recycling compartments
    • doi:10.1242/jcs.051557
    • Zhang, D., M. Manna, T. Wohland, and R. Kraut. 2009. Alternate raft pathways cooperate to mediate slow diffusion and efficient uptake of a sphingolipid tracer to degradative and recycling compartments. J. Cell Sci. 122:3715-3728. doi:10.1242/jcs.051557
    • (2009) J. Cell Sci. , vol.122 , pp. 3715-3728
    • Zhang, D.1    Manna, M.2    Wohland, T.3    Kraut, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.