메뉴 건너뛰기




Volumn 16, Issue 10, 2006, Pages 493-498

Bar domain proteins: a role in tubulation, scission and actin assembly in clathrin-mediated endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AMPHIPHYSIN; BIN PROTEIN; CLATHRIN; DYNAMIN; ENDOPHILIN; GUANOSINE TRIPHOSPHATASE; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PROTEIN; RVS PROTEIN; SCAFFOLD PROTEIN; SYNAPTOJANIN; UNCLASSIFIED DRUG;

EID: 33748964289     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2006.08.004     Document Type: Review
Times cited : (197)

References (68)
  • 2
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy C., and Wrana J.L. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell Biol. 6 (2005) 112-126
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 3
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M., et al. Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 7 (2006) 404-414
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1
  • 4
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A., et al. GTP-dependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 441 (2006) 528-531
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1
  • 5
    • 12844265252 scopus 로고    scopus 로고
    • A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • Yarar D., et al. A dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis. Mol. Biol. Cell 16 (2005) 964-975
    • (2005) Mol. Biol. Cell , vol.16 , pp. 964-975
    • Yarar, D.1
  • 6
    • 26844517614 scopus 로고    scopus 로고
    • A modular design for the clathrin- and actin-mediated endocytosis machinery
    • Kaksonen M., et al. A modular design for the clathrin- and actin-mediated endocytosis machinery. Cell 123 (2005) 305-320
    • (2005) Cell , vol.123 , pp. 305-320
    • Kaksonen, M.1
  • 7
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield C.J., et al. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat. Cell Biol. 4 (2002) 691-698
    • (2002) Nat. Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1
  • 8
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • Merrifield C.J., et al. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121 (2005) 593-606
    • (2005) Cell , vol.121 , pp. 593-606
    • Merrifield, C.J.1
  • 9
    • 1842419430 scopus 로고    scopus 로고
    • Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts
    • Merrifield C.J., et al. Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts. Eur. J. Cell Biol. 83 (2004) 13-18
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 13-18
    • Merrifield, C.J.1
  • 10
    • 33644873004 scopus 로고    scopus 로고
    • Actin dynamics at the Golgi complex in mammalian cells
    • Egea G., et al. Actin dynamics at the Golgi complex in mammalian cells. Curr. Opin. Cell Biol. 18 (2006) 168-178
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 168-178
    • Egea, G.1
  • 11
    • 33646864565 scopus 로고    scopus 로고
    • Staying in shape with formins
    • Faix J., and Grosse R. Staying in shape with formins. Dev. Cell 10 (2006) 693-706
    • (2006) Dev. Cell , vol.10 , pp. 693-706
    • Faix, J.1    Grosse, R.2
  • 12
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar D.R., et al. Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124 (2006) 423-435
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1
  • 13
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 14
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T., et al. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev. Cell 9 (2005) 791-804
    • (2005) Dev. Cell , vol.9 , pp. 791-804
    • Itoh, T.1
  • 15
    • 33745523031 scopus 로고    scopus 로고
    • Mechanism of endophilin N-BAR domain-mediated membrane curvature
    • Gallop J.L., et al. Mechanism of endophilin N-BAR domain-mediated membrane curvature. EMBO J. 25 (2006) 2898-2910
    • (2006) EMBO J. , vol.25 , pp. 2898-2910
    • Gallop, J.L.1
  • 16
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • Masuda M., et al. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO J. 25 (2006) 2889-2897
    • (2006) EMBO J. , vol.25 , pp. 2889-2897
    • Masuda, M.1
  • 17
    • 22544482948 scopus 로고    scopus 로고
    • Crystal structure of the endophilin-A1 BAR domain
    • Weissenhorn W. Crystal structure of the endophilin-A1 BAR domain. J. Mol. Biol. 351 (2005) 653-661
    • (2005) J. Mol. Biol. , vol.351 , pp. 653-661
    • Weissenhorn, W.1
  • 18
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
    • Peter B.J., et al. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303 (2004) 495-499
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1
  • 19
    • 1542677037 scopus 로고    scopus 로고
    • Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton
    • Salazar M.A., et al. Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. J. Biol. Chem. 278 (2003) 49031-49043
    • (2003) J. Biol. Chem. , vol.278 , pp. 49031-49043
    • Salazar, M.A.1
  • 20
    • 33746863655 scopus 로고    scopus 로고
    • Tuba stimulates intracellular N-WASP-dependent actin assembly
    • Kovacs E.M., et al. Tuba stimulates intracellular N-WASP-dependent actin assembly. J. Cell Sci. 119 (2006) 2715-2726
    • (2006) J. Cell Sci. , vol.119 , pp. 2715-2726
    • Kovacs, E.M.1
  • 21
    • 12744281102 scopus 로고    scopus 로고
    • Sorting nexins-unifying trends and new perspectives
    • Carlton J., et al. Sorting nexins-unifying trends and new perspectives. Traffic 6 (2005) 75-82
    • (2005) Traffic , vol.6 , pp. 75-82
    • Carlton, J.1
  • 22
    • 27644512056 scopus 로고    scopus 로고
    • Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport
    • Carlton J.G., et al. Sorting nexin-2 is associated with tubular elements of the early endosome, but is not essential for retromer-mediated endosome-to-TGN transport. J. Cell Sci. 118 (2005) 4527-4539
    • (2005) J. Cell Sci. , vol.118 , pp. 4527-4539
    • Carlton, J.G.1
  • 23
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides
    • Carlton J., et al. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high- curvature membranes and 3-phosphoinositides. Curr. Biol. 14 (2004) 1791-1800
    • (2004) Curr. Biol. , vol.14 , pp. 1791-1800
    • Carlton, J.1
  • 24
    • 16344382928 scopus 로고    scopus 로고
    • SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis
    • Soulet F., et al. SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis. Mol. Biol. Cell 16 (2005) 2058-2067
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2058-2067
    • Soulet, F.1
  • 25
    • 24144444058 scopus 로고    scopus 로고
    • SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1
    • Yeow-Fong L., et al. SNX9 as an adaptor for linking synaptojanin-1 to the Cdc42 effector ACK1. FEBS Lett. 579 (2005) 5040-5048
    • (2005) FEBS Lett. , vol.579 , pp. 5040-5048
    • Yeow-Fong, L.1
  • 26
    • 0345731934 scopus 로고    scopus 로고
    • The sorting nexin, DSH3PX1, connects the axonal guidance receptor, Dscam, to the actin cytoskeleton
    • Worby C.A., et al. The sorting nexin, DSH3PX1, connects the axonal guidance receptor, Dscam, to the actin cytoskeleton. J. Biol. Chem. 276 (2001) 41782-41789
    • (2001) J. Biol. Chem. , vol.276 , pp. 41782-41789
    • Worby, C.A.1
  • 27
    • 33745862046 scopus 로고    scopus 로고
    • Membrane topology of helix 0 of the Epsin N-terminal homology domain
    • Kweon D.H., et al. Membrane topology of helix 0 of the Epsin N-terminal homology domain. Mol. Cells 21 (2006) 428-435
    • (2006) Mol. Cells , vol.21 , pp. 428-435
    • Kweon, D.H.1
  • 28
    • 0042707772 scopus 로고    scopus 로고
    • Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains
    • Stahelin R.V., et al. Contrasting membrane interaction mechanisms of AP180 N-terminal homology (ANTH) and epsin N-terminal homology (ENTH) domains. J. Biol. Chem. 278 (2003) 28993-28999
    • (2003) J. Biol. Chem. , vol.278 , pp. 28993-28999
    • Stahelin, R.V.1
  • 29
    • 26044447158 scopus 로고    scopus 로고
    • Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase
    • Kaneko T., et al. Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase. Genes Cells 10 (2005) 973-987
    • (2005) Genes Cells , vol.10 , pp. 973-987
    • Kaneko, T.1
  • 30
    • 27544489397 scopus 로고    scopus 로고
    • A slowed classical pathway rather than kiss-and-run mediates endocytosis at synapses lacking synaptojanin and endophilin
    • Dickman D.K., et al. A slowed classical pathway rather than kiss-and-run mediates endocytosis at synapses lacking synaptojanin and endophilin. Cell 123 (2005) 521-533
    • (2005) Cell , vol.123 , pp. 521-533
    • Dickman, D.K.1
  • 31
    • 0037458578 scopus 로고    scopus 로고
    • Neural Wiskott-Aldrich syndrome protein is recruited to rafts and associates with endophilin A in response to epidermal growth factor
    • Otsuki M., et al. Neural Wiskott-Aldrich syndrome protein is recruited to rafts and associates with endophilin A in response to epidermal growth factor. J. Biol. Chem. 278 (2003) 6461-6469
    • (2003) J. Biol. Chem. , vol.278 , pp. 6461-6469
    • Otsuki, M.1
  • 32
    • 4644280545 scopus 로고    scopus 로고
    • The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature
    • Yoshida Y., et al. The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. EMBO J. 23 (2004) 3483-3491
    • (2004) EMBO J. , vol.23 , pp. 3483-3491
    • Yoshida, Y.1
  • 33
    • 0034625338 scopus 로고    scopus 로고
    • Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites
    • Slepnev V.I., et al. Tandem arrangement of the clathrin and AP-2 binding domains in amphiphysin 1 and disruption of clathrin coat function by amphiphysin fragments comprising these sites. J. Biol. Chem. 275 (2000) 17583-17589
    • (2000) J. Biol. Chem. , vol.275 , pp. 17583-17589
    • Slepnev, V.I.1
  • 34
    • 0031746484 scopus 로고    scopus 로고
    • Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites
    • Ramjaun A.R., and McPherson P.S. Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. J. Neurochem. 70 (1998) 2369-2376
    • (1998) J. Neurochem. , vol.70 , pp. 2369-2376
    • Ramjaun, A.R.1    McPherson, P.S.2
  • 35
    • 0030060326 scopus 로고    scopus 로고
    • A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals
    • David C., et al. A role of amphiphysin in synaptic vesicle endocytosis suggested by its binding to dynamin in nerve terminals. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 331-335
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 331-335
    • David, C.1
  • 36
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita K., et al. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172 (2006) 269-279
    • (2006) J. Cell Biol. , vol.172 , pp. 269-279
    • Tsujita, K.1
  • 37
    • 0036273766 scopus 로고    scopus 로고
    • Closing in on the biological functions of Fps/Fes and Fer
    • Greer P. Closing in on the biological functions of Fps/Fes and Fer. Nat. Rev. Mol. Cell Biol. 3 (2002) 278-289
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 278-289
    • Greer, P.1
  • 38
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • Kamioka Y., et al. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J. Biol. Chem. 279 (2004) 40091-40099
    • (2004) J. Biol. Chem. , vol.279 , pp. 40091-40099
    • Kamioka, Y.1
  • 39
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho H.Y., et al. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118 (2004) 203-216
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1
  • 40
    • 0034677932 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules
    • Tian L., et al. Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J. Biol. Chem. 275 (2000) 7854-7861
    • (2000) J. Biol. Chem. , vol.275 , pp. 7854-7861
    • Tian, L.1
  • 41
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: linking membrane trafficking with the cytoskeleton
    • Kessels M.M., and Qualmann B. The syndapin protein family: linking membrane trafficking with the cytoskeleton. J. Cell Sci. 117 (2004) 3077-3086
    • (2004) J. Cell Sci. , vol.117 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 42
    • 0034503124 scopus 로고    scopus 로고
    • All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger J., et al. All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J. Cell Sci. 113 (2000) 4511-4521
    • (2000) J. Cell Sci. , vol.113 , pp. 4511-4521
    • Modregger, J.1
  • 43
    • 33745726868 scopus 로고    scopus 로고
    • Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis
    • Anggono V., et al. Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis. Nat. Neurosci. 9 (2006) 752-760
    • (2006) Nat. Neurosci. , vol.9 , pp. 752-760
    • Anggono, V.1
  • 44
    • 33646710836 scopus 로고    scopus 로고
    • Complexes of syndapin II with dynamin II promote vesicle formation at the trans-Golgi network
    • Kessels M.M., et al. Complexes of syndapin II with dynamin II promote vesicle formation at the trans-Golgi network. J. Cell Sci. 119 (2006) 1504-1516
    • (2006) J. Cell Sci. , vol.119 , pp. 1504-1516
    • Kessels, M.M.1
  • 45
    • 33745000739 scopus 로고    scopus 로고
    • Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization
    • Kessels M.M., and Qualmann B. Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization. J. Biol. Chem. 281 (2006) 13285-13299
    • (2006) J. Biol. Chem. , vol.281 , pp. 13285-13299
    • Kessels, M.M.1    Qualmann, B.2
  • 46
    • 23144467137 scopus 로고    scopus 로고
    • EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling
    • Braun A., et al. EHD proteins associate with syndapin I and II and such interactions play a crucial role in endosomal recycling. Mol. Biol. Cell 16 (2005) 3642-3658
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3642-3658
    • Braun, A.1
  • 47
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels M.M., and Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J. 21 (2002) 6083-6094
    • (2002) EMBO J. , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 48
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann B., and Kelly R.B. Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J. Cell Biol. 148 (2000) 1047-1062
    • (2000) J. Cell Biol. , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 49
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • Gasman S., et al. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat. Cell Biol. 5 (2003) 195-204
    • (2003) Nat. Cell Biol. , vol.5 , pp. 195-204
    • Gasman, S.1
  • 50
    • 21644478501 scopus 로고    scopus 로고
    • RhoB regulates endosome transport by promoting actin assembly on endosomal membranes through Dia1
    • Fernandez-Borja M., et al. RhoB regulates endosome transport by promoting actin assembly on endosomal membranes through Dia1. J. Cell Sci. 118 (2005) 2661-2670
    • (2005) J. Cell Sci. , vol.118 , pp. 2661-2670
    • Fernandez-Borja, M.1
  • 51
    • 33746622160 scopus 로고    scopus 로고
    • Moving matters: signals and mechanisms in directed cell migration
    • Insall R.H., and Jones G.E. Moving matters: signals and mechanisms in directed cell migration. Nat. Cell Biol. 8 (2006) 776-779
    • (2006) Nat. Cell Biol. , vol.8 , pp. 776-779
    • Insall, R.H.1    Jones, G.E.2
  • 52
    • 1342312355 scopus 로고    scopus 로고
    • Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila
    • Coyle I.P., et al. Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in Drosophila. Neuron 41 (2004) 521-534
    • (2004) Neuron , vol.41 , pp. 521-534
    • Coyle, I.P.1
  • 53
    • 33644994992 scopus 로고    scopus 로고
    • Altered synaptic development and active zone spacing in endocytosis mutants
    • Dickman D.K., et al. Altered synaptic development and active zone spacing in endocytosis mutants. Curr. Biol. 16 (2006) 591-598
    • (2006) Curr. Biol. , vol.16 , pp. 591-598
    • Dickman, D.K.1
  • 54
    • 22944438407 scopus 로고    scopus 로고
    • FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation
    • Wu X., et al. FAK-mediated src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation. Dev. Cell 9 (2005) 185-196
    • (2005) Dev. Cell , vol.9 , pp. 185-196
    • Wu, X.1
  • 55
    • 0035902604 scopus 로고    scopus 로고
    • The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia
    • Fuchs U., et al. The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 8756-8761
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8756-8761
    • Fuchs, U.1
  • 56
    • 13444291116 scopus 로고    scopus 로고
    • Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53
    • Millard T.H., et al. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. EMBO J. 24 (2005) 240-250
    • (2005) EMBO J. , vol.24 , pp. 240-250
    • Millard, T.H.1
  • 57
    • 29244441978 scopus 로고    scopus 로고
    • Involvement of Rac in actin cytoskeleton rearrangements induced by MIM-B
    • Bompard G., et al. Involvement of Rac in actin cytoskeleton rearrangements induced by MIM-B. J. Cell Sci. 118 (2005) 5393-5403
    • (2005) J. Cell Sci. , vol.118 , pp. 5393-5403
    • Bompard, G.1
  • 58
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac
    • Suetsugu S., et al. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. J. Cell Biol. 173 (2006) 571-585
    • (2006) J. Cell Biol. , vol.173 , pp. 571-585
    • Suetsugu, S.1
  • 59
    • 20444455430 scopus 로고    scopus 로고
    • Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment
    • Rangone H., et al. Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. J. Biol. Chem. 280 (2005) 22021-22028
    • (2005) J. Biol. Chem. , vol.280 , pp. 22021-22028
    • Rangone, H.1
  • 60
    • 0043162110 scopus 로고    scopus 로고
    • The RhoGAP activity of OPHN1, a new F-actin-binding protein, is negatively controlled by its amino-terminal domain
    • Fauchereau F., et al. The RhoGAP activity of OPHN1, a new F-actin-binding protein, is negatively controlled by its amino-terminal domain. Mol. Cell. Neurosci. 23 (2003) 574-586
    • (2003) Mol. Cell. Neurosci. , vol.23 , pp. 574-586
    • Fauchereau, F.1
  • 62
    • 0037830319 scopus 로고    scopus 로고
    • Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells
    • Spitzenberger F., et al. Islet cell autoantigen of 69 kDa is an arfaptin-related protein associated with the Golgi complex of insulinoma INS-1 cells. J. Biol. Chem. 278 (2003) 26166-26173
    • (2003) J. Biol. Chem. , vol.278 , pp. 26166-26173
    • Spitzenberger, F.1
  • 63
    • 33644872978 scopus 로고    scopus 로고
    • Targeted in vivo mutations of the AMPA receptor subunit GluR2 and its interacting protein PICK1 eliminate cerebellar long-term depression
    • Steinberg J.P., et al. Targeted in vivo mutations of the AMPA receptor subunit GluR2 and its interacting protein PICK1 eliminate cerebellar long-term depression. Neuron 49 (2006) 845-860
    • (2006) Neuron , vol.49 , pp. 845-860
    • Steinberg, J.P.1
  • 64
    • 33644854568 scopus 로고    scopus 로고
    • Lipid binding regulates synaptic targeting of PICK1, AMPA receptor trafficking, and synaptic plasticity
    • Jin W., et al. Lipid binding regulates synaptic targeting of PICK1, AMPA receptor trafficking, and synaptic plasticity. J. Neurosci. 26 (2006) 2380-2390
    • (2006) J. Neurosci. , vol.26 , pp. 2380-2390
    • Jin, W.1
  • 65
    • 0038493639 scopus 로고    scopus 로고
    • Characterization of several leukemia-associated antigens inducing humoral immune responses in acute and chronic myeloid leukemia
    • Greiner J., et al. Characterization of several leukemia-associated antigens inducing humoral immune responses in acute and chronic myeloid leukemia. Int. J. Cancer 106 (2003) 224-231
    • (2003) Int. J. Cancer , vol.106 , pp. 224-231
    • Greiner, J.1
  • 66
    • 3042717086 scopus 로고    scopus 로고
    • RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes
    • Richnau N., et al. RICH-1 has a BIN/Amphiphysin/Rvsp domain responsible for binding to membrane lipids and tubulation of liposomes. Biochem. Biophys. Res. Commun. 320 (2004) 1034-1042
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 1034-1042
    • Richnau, N.1
  • 67
    • 27944450775 scopus 로고    scopus 로고
    • NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS
    • Icking A., et al. NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS. J. Cell Sci. 118 (2005) 5059-5069
    • (2005) J. Cell Sci. , vol.118 , pp. 5059-5069
    • Icking, A.1
  • 68
    • 29344467993 scopus 로고    scopus 로고
    • FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
    • Icking A., et al. FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN. FEBS Lett. 580 (2006) 223-228
    • (2006) FEBS Lett. , vol.580 , pp. 223-228
    • Icking, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.