메뉴 건너뛰기




Volumn 15, Issue 15, 2016, Pages 1977-1985

Linking up at the BAR: Oligomerization and F-BAR protein function

Author keywords

actin cytoskeleton; cell motility; cytokinesis; endocytosis; F BAR domain; membrane bending; membrane binding; oligomerization; scaffolding; signaling; tubulation

Indexed keywords

ACTIN FILAMENT; CELL MOTILITY; CYTOKINESIS; ENDOCYTOSIS; MEMBRANE BINDING; OLIGOMERIZATION; PROTEIN FUNCTION; ANIMAL; BIOLOGICAL MODEL; CELL MEMBRANE; CHEMISTRY; HUMAN; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN TERTIARY STRUCTURE; SIGNAL TRANSDUCTION;

EID: 84976262111     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.1080/15384101.2016.1190893     Document Type: Note
Times cited : (26)

References (109)
  • 1
    • 84949552712 scopus 로고    scopus 로고
    • Cytoskeletal dynamics: A view from the membrane
    • 25963816
    • M.Bezanilla, A.S.Gladfelter, D.R.Kovar, W.L.Lee. Cytoskeletal dynamics: A view from the membrane. J Cell Biol 2015; 209:329-37; PMID:25963816; http://dx.doi.org/10.1083/jcb.201502062
    • (2015) J Cell Biol , vol.209 , pp. 329-337
    • Bezanilla, M.1    Gladfelter, A.S.2    Kovar, D.R.3    Lee, W.L.4
  • 2
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
    • 14645856
    • B.J.Peter, H.M.Kent, I.G.Mills, Y.Vallis, P.J.Butler, P.R.Evans, H.T.McMahon. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 2004; 303:495-9; PMID:14645856; http://dx.doi.org/10.1126/science.1092586
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.5    Evans, P.R.6    McMahon, H.T.7
  • 3
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature
    • 17540576
    • W.M.Henne, H.M.Kent, M.G.Ford, B.G.Hegde, O.Daumke, P.J.G.Butler, R.Mittal, R.Langen, P.R.Evans, H.T.McMahon. Structure and analysis of FCHo2 F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 2007; 15:839-52; PMID:17540576; http://dx.doi.org/10.1016/j.str.2007.05.002
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.3    Hegde, B.G.4    Daumke, O.5    Butler, P.J.G.6    Mittal, R.7    Langen, R.8    Evans, P.R.9    McMahon, H.T.10
  • 4
    • 13444291116 scopus 로고    scopus 로고
    • Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53
    • T.H.Millard, G.Bompard, M.Y.Heung, T.R.Dafforn, D.J.Scott, L.M.Machesky, K.Fütterer. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. EMBO 2005; 24:240-50; http://dx.doi.org/10.1038/sj.emboj.7600535
    • (2005) EMBO , vol.24 , pp. 240-250
    • Millard, T.H.1    Bompard, G.2    Heung, M.Y.3    Dafforn, T.R.4    Scott, D.J.5    Machesky, L.M.6    Fütterer, K.7
  • 5
    • 77953244134 scopus 로고    scopus 로고
    • FCHo proteins are nucleators of clathrin-mediated endocytosis
    • 20448150
    • W.M.Henne, E.Boucrot, M.Meinecke, E.Evergren, Y.Vallis, R.Mittal, H.T.McMahon. FCHo proteins are nucleators of clathrin-mediated endocytosis. Science 2010; 328:1281-4; PMID:20448150; http://dx.doi.org/10.1126/science.1188462
    • (2010) Science , vol.328 , pp. 1281-1284
    • Henne, W.M.1    Boucrot, E.2    Meinecke, M.3    Evergren, E.4    Vallis, Y.5    Mittal, R.6    McMahon, H.T.7
  • 6
    • 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
    • 16418535
    • K.Tsujita, S.Suetsugu, N.Sasaki, M.Furutani, T.Oikawa, T.Takenawa. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol 2006; 172:269-79; PMID:16418535; http://dx.doi.org/10.1083/jcb.200508091
    • (2006) J Cell Biol , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5    Takenawa, T.6
  • 8
    • 84954271853 scopus 로고    scopus 로고
    • The tubulation activity of a fission yeast F-BAR protein is dispensable for its function in cytokinesis
    • 26776521
    • N.A.McDonald, Y.Takizawa, A.Feoktistova, P.Xu, M.D.Ohi, C.W.Vander Kooi, K.L.Gould. The tubulation activity of a fission yeast F-BAR protein is dispensable for its function in cytokinesis. Cell Rep 2016; 14:534-46; PMID:26776521; http://dx.doi.org/10.1016/j.celrep.2015.12.062
    • (2016) Cell Rep , vol.14 , pp. 534-546
    • McDonald, N.A.1    Takizawa, Y.2    Feoktistova, A.3    Xu, P.4    Ohi, M.D.5    Vander Kooi, C.W.6    Gould, K.L.7
  • 9
    • 84955241226 scopus 로고    scopus 로고
    • Oligomerization but not membrane bending underlies the function of certain f-bar proteins in cell motility and cytokinesis
    • 26702831
    • N.A.McDonald, C.W.Vander Kooi, M.D.Ohi, K.L.Gould. Oligomerization but not membrane bending underlies the function of certain f-bar proteins in cell motility and cytokinesis. Dev Cell 2015; 35:725-36; PMID:26702831; http://dx.doi.org/10.1016/j.devcel.2015.11.023
    • (2015) Dev Cell , vol.35 , pp. 725-736
    • McDonald, N.A.1    Vander Kooi, C.W.2    Ohi, M.D.3    Gould, K.L.4
  • 10
    • 69449100707 scopus 로고    scopus 로고
    • The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis
    • 19737524
    • S.Guerrier, J.Coutinho-Budd, T.Sassa, A.Gresset, N.V.Jordan, K.Chen, W.L.Jin, A.Frost, F.Polleux. The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis. Cell 2009; 138:990-1004; PMID:19737524; http://dx.doi.org/10.1016/j.cell.2009.06.047
    • (2009) Cell , vol.138 , pp. 990-1004
    • Guerrier, S.1    Coutinho-Budd, J.2    Sassa, T.3    Gresset, A.4    Jordan, N.V.5    Chen, K.6    Jin, W.L.7    Frost, A.8    Polleux, F.9
  • 11
    • 70350348378 scopus 로고    scopus 로고
    • F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis
    • 19846719
    • E.Dharmalingam, A.Haeckel, R.Pinyol, L.Schwintzer, D.Koch, M.M.Kessels, B.Qualmann. F-BAR proteins of the syndapin family shape the plasma membrane and are crucial for neuromorphogenesis. J Neurosci 2009; 29:13315-27; PMID:19846719; http://dx.doi.org/10.1523/JNEUROSCI.3973-09.2009
    • (2009) J Neurosci , vol.29 , pp. 13315-13327
    • Dharmalingam, E.1    Haeckel, A.2    Pinyol, R.3    Schwintzer, L.4    Koch, D.5    Kessels, M.M.6    Qualmann, B.7
  • 12
    • 79955368638 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of the F-BAR protein Hof1 during cytokinesis
    • 21498574
    • F.Meitinger, M.E.Boehm, A.Hofmann, B.Hub, H.Zentgraf, W.D.Lehmann, G.Pereira. Phosphorylation-dependent regulation of the F-BAR protein Hof1 during cytokinesis. Genes Dev 2011; 25:875-88; PMID:21498574; http://dx.doi.org/10.1101/gad.622411
    • (2011) Genes Dev , vol.25 , pp. 875-888
    • Meitinger, F.1    Boehm, M.E.2    Hofmann, A.3    Hub, B.4    Zentgraf, H.5    Lehmann, W.D.6    Pereira, G.7
  • 13
    • 84877111824 scopus 로고    scopus 로고
    • Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycle
    • 23468521
    • Y.Oh, J.Schreiter, R.Nishihama, C.Wloka, E.Bi. Targeting and functional mechanisms of the cytokinesis-related F-BAR protein Hof1 during the cell cycle. Mol Biol Cell 2013; 24:1305-20; PMID:23468521; http://dx.doi.org/10.1091/mbc.E12-11-0804
    • (2013) Mol Biol Cell , vol.24 , pp. 1305-1320
    • Oh, Y.1    Schreiter, J.2    Nishihama, R.3    Wloka, C.4    Bi, E.5
  • 14
    • 70350336434 scopus 로고    scopus 로고
    • Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation
    • 19713939
    • A.Reider, S.L.Barker, S.K.Mishra, Y.J.Im, L.Maldonado-Báez, J.H.Hurley, L.M.Traub, B.Wendland. Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. EMBO J 2009; 28:3103-16; PMID:19713939; http://dx.doi.org/10.1038/emboj.2009.248
    • (2009) EMBO J , vol.28 , pp. 3103-3116
    • Reider, A.1    Barker, S.L.2    Mishra, S.K.3    Im, Y.J.4    Maldonado-Báez, L.5    Hurley, J.H.6    Traub, L.M.7    Wendland, B.8
  • 16
    • 69149089020 scopus 로고    scopus 로고
    • Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin
    • 19549836
    • Q.Wang, M.V.Navarro, G.Peng, E.Molinelli, S.L.Goh, B.L.Judson, K.R.Rajashankar, H.Sondermann. Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin. PNAS 2009; 106:12700-5; PMID:19549836; http://dx.doi.org/10.1073/pnas.0902974106
    • (2009) PNAS , vol.106 , pp. 12700-12705
    • Wang, Q.1    Navarro, M.V.2    Peng, G.3    Molinelli, E.4    Goh, S.L.5    Judson, B.L.6    Rajashankar, K.R.7    Sondermann, H.8
  • 18
    • 79951823003 scopus 로고    scopus 로고
    • WRP/srGAP3 facilitates the initiation of spine development by an inverse F-BAR domain, and its loss impairs long-term memory
    • 21325512
    • B.R.Carlson, K.E.Lloyd, A.Kruszewski, I.H.Kim, R.M.Rodriguiz, C.Heindel, M.Faytell, S.M.Dudek, W.C.Wetsel, S.H.Soderling. WRP/srGAP3 facilitates the initiation of spine development by an inverse F-BAR domain, and its loss impairs long-term memory. J Neurosci 2011; 31:2447-60; PMID:21325512; http://dx.doi.org/10.1523/JNEUROSCI.4433-10.2011
    • (2011) J Neurosci , vol.31 , pp. 2447-2460
    • Carlson, B.R.1    Lloyd, K.E.2    Kruszewski, A.3    Kim, I.H.4    Rodriguiz, R.M.5    Heindel, C.6    Faytell, M.7    Dudek, S.M.8    Wetsel, W.C.9    Soderling, S.H.10
  • 19
    • 84869136260 scopus 로고    scopus 로고
    • The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently
    • 22467852
    • J.Coutinho-Budd, V.Ghukasyan, M.J.Zylka, F.Polleux. The F-BAR domains from srGAP1, srGAP2 and srGAP3 regulate membrane deformation differently. J Cell Sci 2012; 125:3390-401; PMID:22467852; http://dx.doi.org/10.1242/jcs.098962
    • (2012) J Cell Sci , vol.125 , pp. 3390-3401
    • Coutinho-Budd, J.1    Ghukasyan, V.2    Zylka, M.J.3    Polleux, F.4
  • 20
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • 18216767
    • M.A.Lemmon. Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 2008; 9:99-111; PMID:18216767; http://dx.doi.org/10.1038/nrm2328
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 21
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • 16326391
    • T.Itoh, K.S.Erdmann, A.Roux, B.Habermann, H.Werner, P.De Camilli. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 2005; 9:791-804; PMID:16326391; http://dx.doi.org/10.1016/j.devcel.2005.11.005
    • (2005) Dev Cell , vol.9 , pp. 791-804
    • Itoh, T.1    Erdmann, K.S.2    Roux, A.3    Habermann, B.4    Werner, H.5    De Camilli, P.6
  • 22
    • 77449095272 scopus 로고    scopus 로고
    • The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration
    • 19738202
    • T.Itoh, J.Hasegawa, K.Tsujita, Y.Kanaho, T.Takenawa. The tyrosine kinase Fer is a downstream target of the PLD-PA pathway that regulates cell migration. Sci Signal 2009; 2:ra52; PMID:19738202; http://dx.doi.org/10.1126/scisignal.2000393
    • (2009) Sci Signal , vol.2 , pp. ra52
    • Itoh, T.1    Hasegawa, J.2    Tsujita, K.3    Kanaho, Y.4    Takenawa, T.5
  • 23
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • 17035995
    • G.Di Paolo, P.De Camilli. Phosphoinositides in cell regulation and membrane dynamics. Nature 2006; 443:651-7; PMID:17035995; http://dx.doi.org/10.1038/nature05185
    • (2006) Nature , vol.443 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 24
    • 84884546644 scopus 로고    scopus 로고
    • Membrane-sculpting BAR domains generate stable lipid microdomains
    • 24055060
    • H.Zhao, A.Michelot, E.V.Koskela, V.Tkach, D.Stamou, D.G.Drubin, P.Lappalainen. Membrane-sculpting BAR domains generate stable lipid microdomains. Cell Rep 2013; 4:1213-23; PMID:24055060; http://dx.doi.org/10.1016/j.celrep.2013.08.024
    • (2013) Cell Rep , vol.4 , pp. 1213-1223
    • Zhao, H.1    Michelot, A.2    Koskela, E.V.3    Tkach, V.4    Stamou, D.5    Drubin, D.G.6    Lappalainen, P.7
  • 25
    • 84925600167 scopus 로고    scopus 로고
    • Phosphoinositides in endocytosis
    • 25264171
    • Y.Posor, M.Eichhorn-Grunig, V.Haucke. Phosphoinositides in endocytosis. Biochim Biophys Acta 2015; 1851:794-804; PMID:25264171; http://dx.doi.org/10.1016/j.bbalip.2014.09.014
    • (2015) Biochim Biophys Acta , vol.1851 , pp. 794-804
    • Posor, Y.1    Eichhorn-Grunig, M.2    Haucke, V.3
  • 26
    • 79961145704 scopus 로고    scopus 로고
    • Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis
    • 21807942
    • C.G.Hansen, G.Howard, B.J.Nichols. Pacsin 2 is recruited to caveolae and functions in caveolar biogenesis. J Cell Sci 2011; 124:2777-85; PMID:21807942; http://dx.doi.org/10.1242/jcs.084319
    • (2011) J Cell Sci , vol.124 , pp. 2777-2785
    • Hansen, C.G.1    Howard, G.2    Nichols, B.J.3
  • 28
    • 4544251239 scopus 로고    scopus 로고
    • A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis
    • 15252009
    • Y.Kamioka, S.Fukuhara, H.Sawa, K.Nagashima, M.Masuda, M.Matsuda, N.Mochizuki. A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem 2004; 279:40091-9; PMID:15252009; http://dx.doi.org/10.1074/jbc.M404899200
    • (2004) J Biol Chem , vol.279 , pp. 40091-40099
    • Kamioka, Y.1    Fukuhara, S.2    Sawa, H.3    Nagashima, K.4    Masuda, M.5    Matsuda, M.6    Mochizuki, N.7
  • 29
    • 34249316521 scopus 로고    scopus 로고
    • Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis
    • 17512409
    • A.Shimada, H.Niwa, K.Tsujita, S.Suetsugu, K.Nitta, K.Hanawa-Suetsugu, R.Akasaka, Y.Nishino, M.Toyama, L.Chen, et al. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell 2007; 129:761-72; PMID:17512409; http://dx.doi.org/10.1016/j.cell.2007.03.040
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1    Niwa, H.2    Tsujita, K.3    Suetsugu, S.4    Nitta, K.5    Hanawa-Suetsugu, K.6    Akasaka, R.7    Nishino, Y.8    Toyama, M.9    Chen, L.10
  • 30
    • 84873517639 scopus 로고    scopus 로고
    • Membrane sculpting by F-BAR domains studied by molecular dynamics simulations
    • 23382665
    • H.Yu, K.Schulten. Membrane sculpting by F-BAR domains studied by molecular dynamics simulations. PLoS Comput Biol 2013; 9:e1002892; PMID:23382665; http://dx.doi.org/10.1371/journal.pcbi.1002892
    • (2013) PLoS Comput Biol , vol.9 , pp. 1002892
    • Yu, H.1    Schulten, K.2
  • 31
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • 19379681
    • A.Frost, V.M.Unger, P.De Camilli. The BAR domain superfamily: membrane-molding macromolecules. Cell 2009; 137:191-6; PMID:19379681; http://dx.doi.org/10.1016/j.cell.2009.04.010
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 32
    • 84870055317 scopus 로고    scopus 로고
    • Membrane curvature and its generation by BAR proteins
    • 23058040
    • C.Mim, V.M.Unger. Membrane curvature and its generation by BAR proteins. Trends Biochem Sci 2012; 37:526-33; PMID:23058040; http://dx.doi.org/10.1016/j.tibs.2012.09.001
    • (2012) Trends Biochem Sci , vol.37 , pp. 526-533
    • Mim, C.1    Unger, V.M.2
  • 33
    • 80052194357 scopus 로고    scopus 로고
    • Let's go bananas: revisiting the endocytic BAR code
    • B.Qualmann, D.Koch, M.M.Kessels. Let's go bananas: revisiting the endocytic BAR code. EMBO 2011; 30:3501-15; http://dx.doi.org/10.1038/emboj.2011.266
    • (2011) EMBO , vol.30 , pp. 3501-3515
    • Qualmann, B.1    Koch, D.2    Kessels, M.M.3
  • 34
    • 77950594242 scopus 로고    scopus 로고
    • Subcellular membrane curvature mediated by the BAR domain superfamily proteins
    • 19963073
    • S.Suetsugu, K.Toyooka, Y.Senju. Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Semin Cell Dev Biol 2010; 21:340-9; PMID:19963073; http://dx.doi.org/10.1016/j.semcdb.2009.12.002
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 340-349
    • Suetsugu, S.1    Toyooka, K.2    Senju, Y.3
  • 36
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: where they are and how they behave
    • 18216768
    • G.van Meer, D.R.Voelker, G.W.Feigenson. Membrane lipids: where they are and how they behave. Nat Rev Mol Cell Biol 2008; 9:112-24; PMID:18216768; http://dx.doi.org/10.1038/nrm2330
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 112-124
    • van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 38
    • 0033506708 scopus 로고    scopus 로고
    • Regulation of c-Fes tyrosine kinase and biological activities by N-terminal coiled-coil oligomerization domains
    • 10567558
    • H.Cheng, J.A.Rogers, N.A.Dunham, T.E.Smithgall. Regulation of c-Fes tyrosine kinase and biological activities by N-terminal coiled-coil oligomerization domains. Mol Cell Biol 1999; 19:8335-43; PMID:10567558; http://dx.doi.org/10.1128/MCB.19.12.8335
    • (1999) Mol Cell Biol , vol.19 , pp. 8335-8343
    • Cheng, H.1    Rogers, J.A.2    Dunham, N.A.3    Smithgall, T.E.4
  • 39
    • 0033538551 scopus 로고    scopus 로고
    • Disruption of coiled-coil domains in Fer protein-tyrosine kinase abolishes trimerization but not kinase activation
    • 10391941
    • A.W.Craig, R.Zirngibl, P.Greer. Disruption of coiled-coil domains in Fer protein-tyrosine kinase abolishes trimerization but not kinase activation. J Biol Chem 1999; 274:19934-42; PMID:10391941; http://dx.doi.org/10.1074/jbc.274.28.19934
    • (1999) J Biol Chem , vol.274 , pp. 19934-19942
    • Craig, A.W.1    Zirngibl, R.2    Greer, P.3
  • 40
    • 77954261508 scopus 로고    scopus 로고
    • Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site
    • 20603077
    • R.H.Roberts-Galbraith, M.D.Ohi, B.A.Ballif, J.S.Chen, I.McLeod, W.H.McDonald, S.P.Gygi, J.R.Yates, K.L.Gould. Dephosphorylation of F-BAR protein Cdc15 modulates its conformation and stimulates its scaffolding activity at the cell division site. Mol Cell 2010; 39:86-99; PMID:20603077; http://dx.doi.org/10.1016/j.molcel.2010.06.012
    • (2010) Mol Cell , vol.39 , pp. 86-99
    • Roberts-Galbraith, R.H.1    Ohi, M.D.2    Ballif, B.A.3    Chen, J.S.4    McLeod, I.5    McDonald, W.H.6    Gygi, S.P.7    Yates, J.R.8    Gould, K.L.9
  • 41
    • 59849084607 scopus 로고    scopus 로고
    • The SH3 domains of two PCH family members cooperate in assembly of the schizosaccharomyces pombe contractile ring
    • 19139265
    • R.H.Roberts-Galbraith, J.S.Chen, J.Wang, K.L.Gould. The SH3 domains of two PCH family members cooperate in assembly of the schizosaccharomyces pombe contractile ring. J Cell Biol 2009; 184:113-27; PMID:19139265; http://dx.doi.org/10.1083/jcb.200806044
    • (2009) J Cell Biol , vol.184 , pp. 113-127
    • Roberts-Galbraith, R.H.1    Chen, J.S.2    Wang, J.3    Gould, K.L.4
  • 42
    • 84920973213 scopus 로고    scopus 로고
    • The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast
    • 25428987
    • L.Ren, A.H.Willet, R.H.Roberts-Galbraith, N.A.McDonald, A.Feoktistova, J.S.Chen, H.Huang, R.Guillen, C.Boone, S.S.Sidhu, et al. The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast. Mol Biol Cell 2015; 26:256-69; PMID:25428987; http://dx.doi.org/10.1091/mbc.E14-10-1451
    • (2015) Mol Biol Cell , vol.26 , pp. 256-269
    • Ren, L.1    Willet, A.H.2    Roberts-Galbraith, R.H.3    McDonald, N.A.4    Feoktistova, A.5    Chen, J.S.6    Huang, H.7    Guillen, R.8    Boone, C.9    Sidhu, S.S.10
  • 43
    • 85017309190 scopus 로고    scopus 로고
    • A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing
    • P.K.Umasankar, L.Ma, J.R.Thieman, A.Jha, B.Doray, S.C.Watkins, L.M.Traub. A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing. Elife 2014; 3:1-33; http://dx.doi.org/10.7554/eLife.04137
    • (2014) Elife , vol.3 , pp. 1-33
    • Umasankar, P.K.1    Ma, L.2    Thieman, J.R.3    Jha, A.4    Doray, B.5    Watkins, S.C.6    Traub, L.M.7
  • 45
    • 73949119447 scopus 로고    scopus 로고
    • Early-Arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast
    • 19776351
    • H.E.M.Stimpson, C.P.Toret, A.T.Cheng, B.S.Pauly, D.G.Drubin. Early-Arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol Biol Cell 2009; 20:4640-51; PMID:19776351; http://dx.doi.org/10.1091/mbc.E09-05-0429
    • (2009) Mol Biol Cell , vol.20 , pp. 4640-4651
    • Stimpson, H.E.M.1    Toret, C.P.2    Cheng, A.T.3    Pauly, B.S.4    Drubin, D.G.5
  • 46
    • 84864634144 scopus 로고    scopus 로고
    • The first five seconds in the life of a clathrin-coated pit
    • 22863004
    • E.Cocucci, F.Aguet, S.Boulant, T.Kirchhausen. The first five seconds in the life of a clathrin-coated pit. Cell 2012; 150:495-507; PMID:22863004; http://dx.doi.org/10.1016/j.cell.2012.05.047
    • (2012) Cell , vol.150 , pp. 495-507
    • Cocucci, E.1    Aguet, F.2    Boulant, S.3    Kirchhausen, T.4
  • 48
    • 84883672372 scopus 로고    scopus 로고
    • A cost–benefit analysis of the physical mechanisms of membrane curvature
    • 23999615
    • J.C.Stachowiak, F.M.Brodsky, E.A.Miller. A cost–benefit analysis of the physical mechanisms of membrane curvature. Nat Cell Biol 2013; 15:1019-27; PMID:23999615; http://dx.doi.org/10.1038/ncb2832
    • (2013) Nat Cell Biol , vol.15 , pp. 1019-1027
    • Stachowiak, J.C.1    Brodsky, F.M.2    Miller, E.A.3
  • 49
    • 34547969807 scopus 로고    scopus 로고
    • Endocytosis: clathrin-mediated membrane budding
    • 17631994
    • E.J.Ungewickell, L.Hinrichsen. Endocytosis: clathrin-mediated membrane budding. Curr Opin Cell Biol 2007; 19:417-25; PMID:17631994; http://dx.doi.org/10.1016/j.ceb.2007.05.003
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 417-425
    • Ungewickell, E.J.1    Hinrichsen, L.2
  • 50
    • 79953718772 scopus 로고    scopus 로고
    • A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis
    • 21445324
    • M.J.Taylor, D.Perrais, C.J.Merrifield. A high precision survey of the molecular dynamics of mammalian clathrin-mediated endocytosis. PLoS Biol 2011; 9:e1000604; PMID:21445324; http://dx.doi.org/10.1371/journal.pbio.1000604
    • (2011) PLoS Biol , vol.9 , pp. 1000604
    • Taylor, M.J.1    Perrais, D.2    Merrifield, C.J.3
  • 51
    • 55249104474 scopus 로고    scopus 로고
    • Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-Cadherin endocytosis
    • 18976911
    • A.Leibfried, R.Fricke, M.J.Morgan, S.Bogdan, Y.Bellaiche. Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-Cadherin endocytosis. Curr Biol 2008; 18:1639-48; PMID:18976911; http://dx.doi.org/10.1016/j.cub.2008.09.063
    • (2008) Curr Biol , vol.18 , pp. 1639-1648
    • Leibfried, A.1    Fricke, R.2    Morgan, M.J.3    Bogdan, S.4    Bellaiche, Y.5
  • 53
    • 69949116356 scopus 로고    scopus 로고
    • Drosophila Cip4/Toca-1 integrates membrane trafficking and actin dynamics through WASP and SCAR/WAVE7
    • 19716703
    • R.Fricke, C.Gohl, E.Dharmalingam, A.Grevelhörster, B.Zahedi, N.Harden, M.Kessels, B.Qualmann, S.Bogdan. Drosophila Cip4/Toca-1 integrates membrane trafficking and actin dynamics through WASP and SCAR/WAVE7. Curr Biol 2009; 19:1429-37; PMID:19716703; http://dx.doi.org/10.1016/j.cub.2009.07.058
    • (2009) Curr Biol , vol.19 , pp. 1429-1437
    • Fricke, R.1    Gohl, C.2    Dharmalingam, E.3    Grevelhörster, A.4    Zahedi, B.5    Harden, N.6    Kessels, M.7    Qualmann, B.8    Bogdan, S.9
  • 54
    • 84856111189 scopus 로고    scopus 로고
    • Dynamin, a membrane-remodelling GTPase
    • 22233676
    • S.M.Ferguson, P.De Camilli. Dynamin, a membrane-remodelling GTPase. Nat Rev Mol Cell Biol 2012; 13:75-88; PMID:22233676
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 75-88
    • Ferguson, S.M.1    De Camilli, P.2
  • 55
    • 84871568885 scopus 로고    scopus 로고
    • The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization
    • 23129763
    • B.-J.de Kreuk, E.C.Anthony, D.Geertss, P.L.Hordijk. The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization. J Biol Chem 2012; 287:43438-53; PMID:23129763; http://dx.doi.org/10.1074/jbc.M112.391078
    • (2012) J Biol Chem , vol.287 , pp. 43438-43453
    • de Kreuk, B.-J.1    Anthony, E.C.2    Geertss, D.3    Hordijk, P.L.4
  • 56
    • 79958105143 scopus 로고    scopus 로고
    • Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting
    • 21610094
    • Y.Senju, Y.Itoh, K.Takano, S.Hamada, S.Suetsugu. Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting. J Cell Sci 2011; 124:2032-40; PMID:21610094; http://dx.doi.org/10.1242/jcs.086264
    • (2011) J Cell Sci , vol.124 , pp. 2032-2040
    • Senju, Y.1    Itoh, Y.2    Takano, K.3    Hamada, S.4    Suetsugu, S.5
  • 57
    • 27944450775 scopus 로고    scopus 로고
    • NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS
    • 16234328
    • A.Icking, S.Matt, N.Opitz, A.Wiesenthal, W.Müller-Esterl, K.Schilling. NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS. J Cell Sci 2005; 118:5059-69; PMID:16234328; http://dx.doi.org/10.1242/jcs.02620
    • (2005) J Cell Sci , vol.118 , pp. 5059-5069
    • Icking, A.1    Matt, S.2    Opitz, N.3    Wiesenthal, A.4    Müller-Esterl, W.5    Schilling, K.6
  • 58
    • 0037168547 scopus 로고    scopus 로고
    • NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase
    • 12446846
    • K.Zimmermann, N.Opitz, J.Dedio, C.Renne, W.Muller-Esterl, S.Oess. NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase. PNAS 2002; 99:17167-72; PMID:12446846; http://dx.doi.org/10.1073/pnas.252345399
    • (2002) PNAS , vol.99 , pp. 17167-17172
    • Zimmermann, K.1    Opitz, N.2    Dedio, J.3    Renne, C.4    Muller-Esterl, W.5    Oess, S.6
  • 59
    • 1342312355 scopus 로고    scopus 로고
    • Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in drosophila
    • 14980202
    • I.P.Coyle, Y.H.Koh, W.C.Lee, J.Slind, T.Fergestad, J.T.Littleton, B.Ganetzky. Nervous wreck, an SH3 adaptor protein that interacts with Wsp, regulates synaptic growth in drosophila. Neuron 2004; 41:521-34; PMID:14980202; http://dx.doi.org/10.1016/S0896-6273(04)00016-9
    • (2004) Neuron , vol.41 , pp. 521-534
    • Coyle, I.P.1    Koh, Y.H.2    Lee, W.C.3    Slind, J.4    Fergestad, T.5    Littleton, J.T.6    Ganetzky, B.7
  • 60
    • 51149107857 scopus 로고    scopus 로고
    • Nervous wreck and Cdc42 cooperate to regulate endocytic actin assembly during synaptic growth
    • 18701694
    • A.A.Rodal, R.N.Motola-Barnes, J.T.Littleton. Nervous wreck and Cdc42 cooperate to regulate endocytic actin assembly during synaptic growth. J Neurosci 2008; 28:8316-25; PMID:18701694; http://dx.doi.org/10.1523/JNEUROSCI.2304-08.2008
    • (2008) J Neurosci , vol.28 , pp. 8316-8325
    • Rodal, A.A.1    Motola-Barnes, R.N.2    Littleton, J.T.3
  • 61
    • 79955501404 scopus 로고    scopus 로고
    • A presynaptic endosomal trafficking pathway controls synaptic growth signaling
    • 21464232
    • A.A.Rodal, A.D.Blunk, Y.Akbergenova, R.A.Jorquera, L.K.Buhl, J.T.Littleton. A presynaptic endosomal trafficking pathway controls synaptic growth signaling. J Cell Biol 2011; 193:201-17; PMID:21464232; http://dx.doi.org/10.1083/jcb.201009052
    • (2011) J Cell Biol , vol.193 , pp. 201-217
    • Rodal, A.A.1    Blunk, A.D.2    Akbergenova, Y.3    Jorquera, R.A.4    Buhl, L.K.5    Littleton, J.T.6
  • 62
    • 43449130032 scopus 로고    scopus 로고
    • Nervous Wreck Interacts with Thickveins and the endocytic machinery to attenuate retrograde BMP signaling during synaptic growth
    • K.M.O'Connor-Giles, L.L.Ho, B.Ganetzky. Nervous Wreck Interacts with Thickveins and the endocytic machinery to attenuate retrograde BMP signaling during synaptic growth. Neuron 2008; 58:507-18; http://dx.doi.org/10.1016/j.neuron.2008.03.007
    • (2008) Neuron , vol.58 , pp. 507-518
    • O'Connor-Giles, K.M.1    Ho, L.L.2    Ganetzky, B.3
  • 63
    • 84858698819 scopus 로고    scopus 로고
    • The F-BAR protein CIP4 inhibits neurite formation by producing lamellipodial protrusions
    • 22361215
    • W.Saengsawang, K.Mitok, C.Viesselmann, L.Pietila, D.C.Lumbard, S.J.Corey, E.W.Dent. The F-BAR protein CIP4 inhibits neurite formation by producing lamellipodial protrusions. Curr Biol 2012; 22:494-501; PMID:22361215; http://dx.doi.org/10.1016/j.cub.2012.01.038
    • (2012) Curr Biol , vol.22 , pp. 494-501
    • Saengsawang, W.1    Mitok, K.2    Viesselmann, C.3    Pietila, L.4    Lumbard, D.C.5    Corey, S.J.6    Dent, E.W.7
  • 64
    • 84880001242 scopus 로고    scopus 로고
    • CIP4 coordinates with phospholipids and actin-associated proteins to localize to the protruding edge and produce actin ribs and veils
    • 23572514
    • W.Saengsawang, K.L.Taylor, D.C.Lumbard, K.Mitok, A.Price, L.Pietila, T.M.Gomez, E.W.Dent. CIP4 coordinates with phospholipids and actin-associated proteins to localize to the protruding edge and produce actin ribs and veils. J Cell Sci 2013; 126:2411-23; PMID:23572514; http://dx.doi.org/10.1242/jcs.117473
    • (2013) J Cell Sci , vol.126 , pp. 2411-2423
    • Saengsawang, W.1    Taylor, K.L.2    Lumbard, D.C.3    Mitok, K.4    Price, A.5    Pietila, L.6    Gomez, T.M.7    Dent, E.W.8
  • 65
    • 78449267306 scopus 로고    scopus 로고
    • Cdc42-interacting protein 4 promotes breast cancer cell invasion and formation of invadopodia through activation of N-WASp
    • 20940394
    • C.S.Pichot, C.Arvanitis, S.M.Hartig, S.A.Jensen, J.Bechill, S.Marzouk, J.Yu, J.A.Frost, S.J.Corey. Cdc42-interacting protein 4 promotes breast cancer cell invasion and formation of invadopodia through activation of N-WASp. Cancer Res 2010; 70:8347-56; PMID:20940394; http://dx.doi.org/10.1158/0008-5472.CAN-09-4149
    • (2010) Cancer Res , vol.70 , pp. 8347-8356
    • Pichot, C.S.1    Arvanitis, C.2    Hartig, S.M.3    Jensen, S.A.4    Bechill, J.5    Marzouk, S.6    Yu, J.7    Frost, J.A.8    Corey, S.J.9
  • 66
    • 0032489515 scopus 로고    scopus 로고
    • Tyrosine Phosphorylation Regulates the SH3-mediated binding of the wiskott-aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein
    • 9488710
    • Y.Wu, S.D.Spencer, L.A.Lasky. Tyrosine Phosphorylation Regulates the SH3-mediated binding of the wiskott-aldrich syndrome protein to PSTPIP, a cytoskeletal-associated protein. J Biol Chem 1998; 273:5765-70; PMID:9488710; http://dx.doi.org/10.1074/jbc.273.10.5765
    • (1998) J Biol Chem , vol.273 , pp. 5765-5770
    • Wu, Y.1    Spencer, S.D.2    Lasky, L.A.3
  • 67
    • 0037169501 scopus 로고    scopus 로고
    • PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-PEST toward a specific dephosphorylation of WASP
    • J.F.Côté, P.L.Chung, J.F.Théberge, M.Hallé, S.Spencer, L.A.Lasky, M.L.Tremblay. PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding PTP-PEST toward a specific dephosphorylation of WASP. J Biol Chem 2002; 277:2973-86; http://dx.doi.org/10.1074/jbc.M106428200
    • (2002) J Biol Chem , vol.277 , pp. 2973-2986
    • Côté, J.F.1    Chung, P.L.2    Théberge, J.F.3    Hallé, M.4    Spencer, S.5    Lasky, L.A.6    Tremblay, M.L.7
  • 68
    • 0034510155 scopus 로고    scopus 로고
    • Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation
    • 11163214
    • F.Cong, S.Spencer, J.F.Côté, Y.Wu, M.L.Tremblay, L.A.Lasky, S.P.Goff. Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Mol Cell 2000; 6:1413-23; PMID:11163214; http://dx.doi.org/10.1016/S1097-2765(00)00138-6
    • (2000) Mol Cell , vol.6 , pp. 1413-1423
    • Cong, F.1    Spencer, S.2    Côté, J.F.3    Wu, Y.4    Tremblay, M.L.5    Lasky, L.A.6    Goff, S.P.7
  • 69
    • 0032547838 scopus 로고    scopus 로고
    • imp2, a new component of the actin ring in the fission yeast
    • 9786952
    • J.Demeter, S.Sazer. imp2, a new component of the actin ring in the fission yeast. J Cell Biol 1998; 143:415-27; PMID:9786952; http://dx.doi.org/10.1083/jcb.143.2.415
    • (1998) J Cell Biol , vol.143 , pp. 415-427
    • Demeter, J.1    Sazer, S.2
  • 70
    • 0029112482 scopus 로고
    • The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis
    • 7634333
    • C.Fankhauser, A.Reymond, L.Cerutti, S.Utzig, K.Hofmann, V.Simanis. The S. pombe cdc15 gene is a key element in the reorganization of F-actin at mitosis. Cell 1995; 82:435-44; PMID:7634333; http://dx.doi.org/10.1016/0092-8674(95)90432-8
    • (1995) Cell , vol.82 , pp. 435-444
    • Fankhauser, C.1    Reymond, A.2    Cerutti, L.3    Utzig, S.4    Hofmann, K.5    Simanis, V.6
  • 72
    • 0032561342 scopus 로고    scopus 로고
    • Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p: Implication in cytokinesis in Saccharomyces cerevisiae
    • 9774458
    • T.Kamei, K.Tanaka, T.Hihara, M.Umikawa, H.Imamura, M.Kikyo, K.Ozaki, Y.Takai. Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p: Implication in cytokinesis in Saccharomyces cerevisiae. J Biol Chem 1998; 273:28341-5; PMID:9774458; http://dx.doi.org/10.1074/jbc.273.43.28341
    • (1998) J Biol Chem , vol.273 , pp. 28341-28345
    • Kamei, T.1    Tanaka, K.2    Hihara, T.3    Umikawa, M.4    Imamura, H.5    Kikyo, M.6    Ozaki, K.7    Takai, Y.8
  • 74
    • 0041885217 scopus 로고    scopus 로고
    • The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomycespombe
    • 12939254
    • R.H.Carnahan, K.L.Gould. The PCH family protein, Cdc15p, recruits two F-actin nucleation pathways to coordinate cytokinetic actin ring formation in Schizosaccharomycespombe. J Cell Biol 2003; 162:851-62; PMID:12939254; http://dx.doi.org/10.1083/jcb.200305012
    • (2003) J Cell Biol , vol.162 , pp. 851-862
    • Carnahan, R.H.1    Gould, K.L.2
  • 75
    • 84924692147 scopus 로고    scopus 로고
    • The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12
    • 25688133
    • A.H.Willet, N.A.Mcdonald, K.A.Bohnert, M.A.Baird, J.R.Allen, M.W.Davidson, K.L.Gould. The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12. J Cell Biol 2015; 208:391-9; PMID:25688133; http://dx.doi.org/10.1083/jcb.201411097
    • (2015) J Cell Biol , vol.208 , pp. 391-399
    • Willet, A.H.1    Mcdonald, N.A.2    Bohnert, K.A.3    Baird, M.A.4    Allen, J.R.5    Davidson, M.W.6    Gould, K.L.7
  • 76
    • 0030958087 scopus 로고    scopus 로고
    • Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • 9105045
    • F.Chang, D.Drubin, P.Nurse. Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J Cell Biol 1997; 137:169-82; PMID:9105045; http://dx.doi.org/10.1083/jcb.137.1.169
    • (1997) J Cell Biol , vol.137 , pp. 169-182
    • Chang, F.1    Drubin, D.2    Nurse, P.3
  • 77
    • 0344823965 scopus 로고    scopus 로고
    • Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway
    • 14595024
    • N.G.Shoham, M.Centola, E.Mansfield, K.M.Hull, G.Wood, C.A.Wise, D.L.Kastner. Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway. PNAS 2003; 100:13501-6; PMID:14595024; http://dx.doi.org/10.1073/pnas.2135380100
    • (2003) PNAS , vol.100 , pp. 13501-13506
    • Shoham, N.G.1    Centola, M.2    Mansfield, E.3    Hull, K.M.4    Wood, G.5    Wise, C.A.6    Kastner, D.L.7
  • 78
    • 35348934890 scopus 로고    scopus 로고
    • Pyrin Activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants
    • 17964261
    • J.W.Yu, T.Fernandes-Alnemri, P.Datta, J.Wu, C.Juliana, L.Solorzano, M.McCormick, Z.Zhang, E.S.Alnemri. Pyrin Activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants. Mol Cell 2007; 28:214-27; PMID:17964261; http://dx.doi.org/10.1016/j.molcel.2007.08.029
    • (2007) Mol Cell , vol.28 , pp. 214-227
    • Yu, J.W.1    Fernandes-Alnemri, T.2    Datta, P.3    Wu, J.4    Juliana, C.5    Solorzano, L.6    McCormick, M.7    Zhang, Z.8    Alnemri, E.S.9
  • 80
    • 24044540256 scopus 로고    scopus 로고
    • Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction
    • 16134966
    • S.S.Li. Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. Biochem J 2005; 390:641-53; PMID:16134966; http://dx.doi.org/10.1042/BJ20050411
    • (2005) Biochem J , vol.390 , pp. 641-653
    • Li, S.S.1
  • 81
    • 38049019805 scopus 로고    scopus 로고
    • Spatial recruitment and activation of the Fes kinase by ezrin promotes HGF-induced cell scattering
    • 18046454
    • A.Naba, C.Reverdy, D.Louvard, M.Arpin. Spatial recruitment and activation of the Fes kinase by ezrin promotes HGF-induced cell scattering. EMBO J 2008; 27:38-50; PMID:18046454; http://dx.doi.org/10.1038/sj.emboj.7601943
    • (2008) EMBO J , vol.27 , pp. 38-50
    • Naba, A.1    Reverdy, C.2    Louvard, D.3    Arpin, M.4
  • 82
    • 67349177014 scopus 로고    scopus 로고
    • Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes
    • 19339212
    • M.A.Oh, S.Choi, M.J.Lee, M.C.Choi, S.A.Lee, W.Ko, W.G.Cance, E.S.Oh, L.Buday, S.H.Kim, et al. Specific tyrosine phosphorylation of focal adhesion kinase mediated by Fer tyrosine kinase in suspended hepatocytes. Biochim Biophys Acta 2009; 1793:781-91; PMID:19339212; http://dx.doi.org/10.1016/j.bbamcr.2009.01.015
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 781-791
    • Oh, M.A.1    Choi, S.2    Lee, M.J.3    Choi, M.C.4    Lee, S.A.5    Ko, W.6    Cance, W.G.7    Oh, E.S.8    Buday, L.9    Kim, S.H.10
  • 83
    • 0029003669 scopus 로고
    • The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors
    • 7623846
    • L.Kim, T.W.Wong. The cytoplasmic tyrosine kinase FER is associated with the catenin-like substrate pp120 and is activated by growth factors. Mol Cell Biol 1995; 15:4553-61; PMID:7623846; http://dx.doi.org/10.1128/MCB.15.8.4553
    • (1995) Mol Cell Biol , vol.15 , pp. 4553-4561
    • Kim, L.1    Wong, T.W.2
  • 84
    • 0032483517 scopus 로고    scopus 로고
    • Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER
    • 9722593
    • L.Kim, T.W.Wong. Growth factor-dependent phosphorylation of the actin-binding protein cortactin is mediated by the cytoplasmic tyrosine kinase FER. J Biol Chem 1998; 273:23542-8; PMID:9722593; http://dx.doi.org/10.1074/jbc.273.36.23542
    • (1998) J Biol Chem , vol.273 , pp. 23542-23548
    • Kim, L.1    Wong, T.W.2
  • 85
    • 0036273766 scopus 로고    scopus 로고
    • Closing in on the biological functions of Fps/Fes and Fer
    • 11994747
    • P.Greer. Closing in on the biological functions of Fps/Fes and Fer. Nat Rev Mol Cell Biol 2002; 3:278-89; PMID:11994747; http://dx.doi.org/10.1038/nrm783
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 278-289
    • Greer, P.1
  • 86
    • 17944380009 scopus 로고    scopus 로고
    • Signal transduction in neuronal migration: Roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway
    • 11672528
    • K.Wong, X.R.Ren, Y.Z.Huang, Y.Xie, G.Liu, H.Saito, H.Tang, L.Wen, S.M.Brady-Kalnay, L.Mei, et al. Signal transduction in neuronal migration: Roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway. Cell 2001; 107:209-21; PMID:11672528; http://dx.doi.org/10.1016/S0092-8674(01)00530-X
    • (2001) Cell , vol.107 , pp. 209-221
    • Wong, K.1    Ren, X.R.2    Huang, Y.Z.3    Xie, Y.4    Liu, G.5    Saito, H.6    Tang, H.7    Wen, L.8    Brady-Kalnay, S.M.9    Mei, L.10
  • 88
    • 84945244485 scopus 로고    scopus 로고
    • SrGAP2-Dependent integration of membrane geometry and Slit-Robo-Repulsive cues regulates fibroblast contact inhibition of locomotion
    • 26439400
    • R.D.Fritz, D.Menshykau, K.Martin, A.Reimann, V.Pontelli, O.Pertz. SrGAP2-Dependent integration of membrane geometry and Slit-Robo-Repulsive cues regulates fibroblast contact inhibition of locomotion. Dev Cell 2015; 35:78-92; PMID:26439400; http://dx.doi.org/10.1016/j.devcel.2015.09.002
    • (2015) Dev Cell , vol.35 , pp. 78-92
    • Fritz, R.D.1    Menshykau, D.2    Martin, K.3    Reimann, A.4    Pontelli, V.5    Pertz, O.6
  • 90
    • 0030763619 scopus 로고    scopus 로고
    • A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1
    • 9305890
    • J.Saras, P.Franzén, P.Aspenström, U.Hellman, L.J.Gonez, C.H.Heldin. A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. J Biol Chem 1997; 272:24333-8; PMID:9305890; http://dx.doi.org/10.1074/jbc.272.39.24333
    • (1997) J Biol Chem , vol.272 , pp. 24333-24338
    • Saras, J.1    Franzén, P.2    Aspenström, P.3    Hellman, U.4    Gonez, L.J.5    Heldin, C.H.6
  • 91
    • 0036799215 scopus 로고    scopus 로고
    • A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases
    • 12093360
    • S.Aresta, M.-F.de Tand-Heim, F.Beranger, J.de Gunzburg. A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases. Biochem J 2002; 367:57-65; PMID:12093360; http://dx.doi.org/10.1042/bj20020829
    • (2002) Biochem J , vol.367 , pp. 57-65
    • Aresta, S.1    de Tand-Heim, M.-F.2    Beranger, F.3    de Gunzburg, J.4
  • 92
    • 35448938873 scopus 로고    scopus 로고
    • ARHGAP4 is a novel RhoGAP that mediates inhibition of cell motility and axon outgrowth
    • 17804252
    • D.L.Vogt, C.D.Gray, W.S.Young, S.A.Orellana, A.T.Malouf. ARHGAP4 is a novel RhoGAP that mediates inhibition of cell motility and axon outgrowth. Mol Cell Neurosci 2007; 36:332-42; PMID:17804252; http://dx.doi.org/10.1016/j.mcn.2007.07.004
    • (2007) Mol Cell Neurosci , vol.36 , pp. 332-342
    • Vogt, D.L.1    Gray, C.D.2    Young, W.S.3    Orellana, S.A.4    Malouf, A.T.5
  • 93
    • 77958473954 scopus 로고    scopus 로고
    • Setting the F-BAR: Functions and regulation of the F-BAR protein family
    • 20948299
    • R.H.Roberts-Galbraith, K.L.Gould. Setting the F-BAR: Functions and regulation of the F-BAR protein family. Cell Cycle 2010; 9:4091-7; PMID:20948299; http://dx.doi.org/10.4161/cc.9.20.13587
    • (2010) Cell Cycle , vol.9 , pp. 4091-4097
    • Roberts-Galbraith, R.H.1    Gould, K.L.2
  • 94
    • 84959260343 scopus 로고    scopus 로고
    • The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles
    • 26553932
    • P.Ullal, N.A.McDonald, J.S.Chen, L.Lo Presti, R.H.Roberts-Galbraith, K.L.Gould, S.G.Martin. The DYRK-family kinase Pom1 phosphorylates the F-BAR protein Cdc15 to prevent division at cell poles. J Cell Biol 2015; 211:653-68; PMID:26553932; http://dx.doi.org/10.1083/jcb.201504073
    • (2015) J Cell Biol , vol.211 , pp. 653-668
    • Ullal, P.1    McDonald, N.A.2    Chen, J.S.3    Lo Presti, L.4    Roberts-Galbraith, R.H.5    Gould, K.L.6    Martin, S.G.7
  • 95
    • 84877104017 scopus 로고    scopus 로고
    • Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis
    • 23447700
    • F.Meitinger, S.Palani, B.Hub, G.Pereira. Dual function of the NDR-kinase Dbf2 in the regulation of the F-BAR protein Hof1 during cytokinesis. Mol Biol Cell 2013; 24:1290-304; PMID:23447700; http://dx.doi.org/10.1091/mbc.E12-08-0608
    • (2013) Mol Biol Cell , vol.24 , pp. 1290-1304
    • Meitinger, F.1    Palani, S.2    Hub, B.3    Pereira, G.4
  • 98
    • 84913594397 scopus 로고    scopus 로고
    • The new frontier of genome engineering with CRISPR-Cas9
    • 25430774
    • J.A.Doudna, E.Charpentier. The new frontier of genome engineering with CRISPR-Cas9. Science 2014; 346:1258096-1-9; PMID:25430774; http://dx.doi.org/10.1126/science.1258096
    • (2014) Science , vol.346
    • Doudna, J.A.1    Charpentier, E.2
  • 99
    • 0031194076 scopus 로고    scopus 로고
    • A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton
    • 9210375
    • P.Aspenström. A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol 1997; 7:479-87; PMID:9210375; http://dx.doi.org/10.1016/S0960-9822(06)00219-3
    • (1997) Curr Biol , vol.7 , pp. 479-487
    • Aspenström, P.1
  • 100
    • 0032919866 scopus 로고    scopus 로고
    • Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein
    • 9950691
    • B.Qualmann, J.Roos, P.J.DiGregorio, R.B.Kelly. Syndapin I, a synaptic dynamin-binding protein that associates with the neural Wiskott-Aldrich syndrome protein. Mol Biol Cell 1999; 10:501-13; PMID:9950691; http://dx.doi.org/10.1091/mbc.10.2.501
    • (1999) Mol Biol Cell , vol.10 , pp. 501-513
    • Qualmann, B.1    Roos, J.2    DiGregorio, P.J.3    Kelly, R.B.4
  • 101
    • 54249122300 scopus 로고    scopus 로고
    • The PCH family member Proline-Serine-Threonine Phosphatase–interacting Protein 1 Targets to the leukocyte uropod and regulates directed cell migration
    • 18480402
    • K.M.Cooper, D.A.Bennin, A.Huttenlocher. The PCH family member Proline-Serine-Threonine Phosphatase–interacting Protein 1 Targets to the leukocyte uropod and regulates directed cell migration. Mol Biol Cell 2008; 19:3180-91; PMID:18480402; http://dx.doi.org/10.1091/mbc.E08-02-0225
    • (2008) Mol Biol Cell , vol.19 , pp. 3180-3191
    • Cooper, K.M.1    Bennin, D.A.2    Huttenlocher, A.3
  • 102
  • 103
    • 0031964702 scopus 로고    scopus 로고
    • Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein
    • 9422760
    • D.Dowbenko, S.Spencer, C.Quan, L.A.Lasky. Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein. J Biol Chem 1998; 273:989-96; PMID:9422760; http://dx.doi.org/10.1074/jbc.273.2.989
    • (1998) J Biol Chem , vol.273 , pp. 989-996
    • Dowbenko, D.1    Spencer, S.2    Quan, C.3    Lasky, L.A.4
  • 104
    • 0036840975 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro
    • 12391157
    • A.Soulard, T.Lechler, V.Spiridonov, A.Shevchenko, A.Shevchenko, R.Li, B.Winsor. Saccharomyces cerevisiae Bzz1p is implicated with type I myosins in actin patch polarization and is able to recruit actin-polymerizing machinery in vitro. Mol Cell Biol 2002; 22:7889-906; PMID:12391157; http://dx.doi.org/10.1128/MCB.22.22.7889-7906.2002
    • (2002) Mol Cell Biol , vol.22 , pp. 7889-7906
    • Soulard, A.1    Lechler, T.2    Spiridonov, V.3    Shevchenko, A.4    Shevchenko, A.5    Li, R.6    Winsor, B.7
  • 107
    • 1542571932 scopus 로고    scopus 로고
    • The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomycespombe
    • 14506270
    • P.Yang, Y.Qyang, G.Bartholomeusz, X.Zhou, S.Marcus. The novel Rho GTPase-activating protein family protein, Rga8, provides a potential link between Cdc42/p21-activated kinase and Rho signaling pathways in the fission yeast, Schizosaccharomycespombe. J Biol Chem 2003; 278:48821-30; PMID:14506270; http://dx.doi.org/10.1074/jbc.M306819200
    • (2003) J Biol Chem , vol.278 , pp. 48821-48830
    • Yang, P.1    Qyang, Y.2    Bartholomeusz, G.3    Zhou, X.4    Marcus, S.5
  • 108
    • 0032880908 scopus 로고    scopus 로고
    • The yeast Rgd1p is a GTPase activating protein of the Rho3 and Rho4 proteins
    • 10526184
    • F.Doignon, C.Weinachter, O.Roumanie, M.Crouzet. The yeast Rgd1p is a GTPase activating protein of the Rho3 and Rho4 proteins. FEBS Lett 1999; 459:458-62; PMID:10526184; http://dx.doi.org/10.1016/S0014-5793(99)01293-4
    • (1999) FEBS Lett , vol.459 , pp. 458-462
    • Doignon, F.1    Weinachter, C.2    Roumanie, O.3    Crouzet, M.4
  • 109
    • 0035812886 scopus 로고    scopus 로고
    • Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from saccharomyces cerevisiae
    • 11591390
    • O.Roumanie, C.Weinachter, I.Larrieu, M.Crouzet, F.Doignon. Functional characterization of the Bag7, Lrg1 and Rgd2 RhoGAP proteins from saccharomyces cerevisiae. FEBS Lett 2001; 506:149-56; PMID:11591390; http://dx.doi.org/10.1016/S0014-5793(01)02906-4
    • (2001) FEBS Lett , vol.506 , pp. 149-156
    • Roumanie, O.1    Weinachter, C.2    Larrieu, I.3    Crouzet, M.4    Doignon, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.