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Volumn 23, Issue 1, 2011, Pages 14-21

I-BAR domain proteins: Linking actin and plasma membrane dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITIDE; PROTEIN ABBA; PROTEIN I BAR; PROTEIN IRSP53; PROTEIN IRTKS; PROTEIN MIM; PROTEIN SRGAP2; UNCLASSIFIED DRUG;

EID: 79951558392     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceb.2010.10.005     Document Type: Review
Times cited : (162)

References (64)
  • 1
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard T.D., Cooper J.A. Actin, a central player in cell shape and movement. Science 2009, 326:1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 2
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman S.J., Ridley A.J. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat Rev Mol Cell Biol 2008, 9:690-701.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 3
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas J., Zhao H., Lappalainen P. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol Rev 2010, 90:259-289.
    • (2010) Physiol Rev , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 4
    • 77955052751 scopus 로고    scopus 로고
    • Interplay of proteins and lipids in generating membrane curvature
    • Graham T.R., Kozlov M.M. Interplay of proteins and lipids in generating membrane curvature. Curr Opin Cell Biol 2010, 22:430-436.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 430-436
    • Graham, T.R.1    Kozlov, M.M.2
  • 5
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen M., Toret C.P., Drubin D.G. Harnessing actin dynamics for clathrin-mediated endocytosis. Nat Rev Mol Cell Biol 2006, 7:404-414.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 7
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: membrane-molding macromolecules
    • Frost A., Unger V.M., De Camilli P. The BAR domain superfamily: membrane-molding macromolecules. Cell 2009, 137:191-196.
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 8
    • 0029741917 scopus 로고    scopus 로고
    • BIN1 is a novel MYC-interacting protein with features of a tumour suppressor
    • Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C. BIN1 is a novel MYC-interacting protein with features of a tumour suppressor. Nat Genet 1996, 14:8-10.
    • (1996) Nat Genet , vol.14 , pp. 8-10
    • Sakamuro, D.1    Elliott, K.J.2    Wechsler-Reya, R.3    Prendergast, G.C.4
  • 9
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat Cell Biol 1999, 1:33-39.
    • (1999) Nat Cell Biol , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 10
    • 0035890136 scopus 로고    scopus 로고
    • Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila
    • Razzaq A., Robinson I.M., McMahon H.T., Skepper J.N., Su Y., Zelhof A.C., Jackson A.P., Gay N.J., O'KaneF C.J. Amphiphysin is necessary for organization of the excitation-contraction coupling machinery of muscles, but not for synaptic vesicle endocytosis in Drosophila. Genes Dev 2001, 15:2967-2979.
    • (2001) Genes Dev , vol.15 , pp. 2967-2979
    • Razzaq, A.1    Robinson, I.M.2    McMahon, H.T.3    Skepper, J.N.4    Su, Y.5    Zelhof, A.C.6    Jackson, A.P.7    Gay, N.J.8    O'KaneF, C.J.9
  • 12
    • 28444452974 scopus 로고    scopus 로고
    • Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins
    • Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P. Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell 2005, 9:791-804.
    • (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
  • 13
    • 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., Suetsugu S., Sasaki N., Furutani M., Oikawa T., Takenawa T. 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, 172:269-279.
    • (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
  • 14
    • 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
    • Aspenström P. 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, 7:479-487.
    • (1997) Curr Biol , vol.7 , pp. 479-487
    • Aspenström, P.1
  • 17
    • 73949119447 scopus 로고    scopus 로고
    • Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast
    • Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G. Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast. Mol Biol Cell 2009, 20:4640-4651.
    • (2009) Mol Biol Cell , vol.20 , pp. 4640-4651
    • Stimpson, H.E.1    Toret, C.P.2    Cheng, A.T.3    Pauly, B.S.4    Drubin, D.G.5
  • 21
    • 2442458996 scopus 로고    scopus 로고
    • A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein
    • Yamagishi A., Masuda M., Ohki T., Onishi H., Mochizuki N. A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein. J Biol Chem 2004, 279:14929-14936.
    • (2004) J Biol Chem , vol.279 , pp. 14929-14936
    • Yamagishi, A.1    Masuda, M.2    Ohki, T.3    Onishi, H.4    Mochizuki, N.5
  • 23
  • 24
    • 33846817369 scopus 로고    scopus 로고
    • Structural basis for the actin-binding function of missing-in-metastasis
    • Lee S.H., Kerff F., Chereau D., Ferron F., Klug A., Dominguez R. Structural basis for the actin-binding function of missing-in-metastasis. Structure 2007, 15:145-155.
    • (2007) Structure , vol.15 , pp. 145-155
    • Lee, S.H.1    Kerff, F.2    Chereau, D.3    Ferron, F.4    Klug, A.5    Dominguez, R.6
  • 27
    • 77952676240 scopus 로고    scopus 로고
    • ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor
    • Zhao H., Hakala M., Lappalainen P. ADF/cofilin binds phosphoinositides in a multivalent manner to act as a PIP(2)-density sensor. Biophys J 2010, 98:2327-2336.
    • (2010) Biophys J , vol.98 , pp. 2327-2336
    • Zhao, H.1    Hakala, M.2    Lappalainen, P.3
  • 29
    • 39149109271 scopus 로고    scopus 로고
    • IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions
    • Scita G., Confalonieri S., Lappalainen P., Suetsugu S. IRSp53: crossing the road of membrane and actin dynamics in the formation of membrane protrusions. Trends Cell Biol 2008, 18:52-60.
    • (2008) Trends Cell Biol , vol.18 , pp. 52-60
    • Scita, G.1    Confalonieri, S.2    Lappalainen, P.3    Suetsugu, S.4
  • 30
    • 0034619847 scopus 로고    scopus 로고
    • IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling
    • Miki H., Yamaguchi H., Suetsugu S., Takenawa T. IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling. Nature 2000, 408:732-735.
    • (2000) Nature , vol.408 , pp. 732-735
    • Miki, H.1    Yamaguchi, H.2    Suetsugu, S.3    Takenawa, T.4
  • 32
    • 3442898762 scopus 로고    scopus 로고
    • IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness
    • Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H. IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness. Cancer Res 2004, 64:5237-5244.
    • (2004) Cancer Res , vol.64 , pp. 5237-5244
    • Funato, Y.1    Terabayashi, T.2    Suenaga, N.3    Seiki, M.4    Takenawa, T.5    Miki, H.6
  • 33
    • 0035809181 scopus 로고    scopus 로고
    • Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin
    • Govind S., Kozma R., Monfries C., Lim L., Ahmed S. Cdc42Hs facilitates cytoskeletal reorganization and neurite outgrowth by localizing the 58-kD insulin receptor substrate to filamentous actin. J Cell Biol 2001, 152:579-594.
    • (2001) J Cell Biol , vol.152 , pp. 579-594
    • Govind, S.1    Kozma, R.2    Monfries, C.3    Lim, L.4    Ahmed, S.5
  • 34
    • 16444374271 scopus 로고    scopus 로고
    • Differential regulation of cortactin and N-WASP-mediated actin polymerization by missing in metastasis (MIM) protein
    • Lin J., Liu J., Wang Y., Zhu J., Zhou K., Smith N., Zhan X. Differential regulation of cortactin and N-WASP-mediated actin polymerization by missing in metastasis (MIM) protein. Oncogene 2005, 24:2059-2066.
    • (2005) Oncogene , vol.24 , pp. 2059-2066
    • Lin, J.1    Liu, J.2    Wang, Y.3    Zhu, J.4    Zhou, K.5    Smith, N.6    Zhan, X.7
  • 35
    • 0030020789 scopus 로고    scopus 로고
    • Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase
    • Yeh T.C., Ogawa W., Danielsen A.G., Roth R.A. Characterization and cloning of a 58/53-kDa substrate of the insulin receptor tyrosine kinase. J Biol Chem 1996, 271:2921-3278.
    • (1996) J Biol Chem , vol.271 , pp. 2921-3278
    • Yeh, T.C.1    Ogawa, W.2    Danielsen, A.G.3    Roth, R.A.4
  • 37
    • 33646763140 scopus 로고    scopus 로고
    • Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac
    • Suetsugu S., Kurisu S., Oikawa T., Yamazaki D., Oda A., Takenawa T. Optimization of WAVE2 complex-induced actin polymerization by membrane-bound IRSp53, PIP(3), and Rac. J Cell Biol 2006, 173:571-585.
    • (2006) J Cell Biol , vol.173 , pp. 571-585
    • Suetsugu, S.1    Kurisu, S.2    Oikawa, T.3    Yamazaki, D.4    Oda, A.5    Takenawa, T.6
  • 38
    • 50649084583 scopus 로고    scopus 로고
    • The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics
    • Lim K.B., Bu W., Goh W.I., Koh E., Ong S.H., Pawson T., Sudhaharan T., Ahmed S. The Cdc42 effector IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics. J Biol Chem 2008, 283:20454-20472.
    • (2008) J Biol Chem , vol.283 , pp. 20454-20472
    • Lim, K.B.1    Bu, W.2    Goh, W.I.3    Koh, E.4    Ong, S.H.5    Pawson, T.6    Sudhaharan, T.7    Ahmed, S.8
  • 40
    • 18944389626 scopus 로고    scopus 로고
    • Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation
    • Connolly B.A., Rice J., Feig L.A., Buchsbaum R.J. Tiam1-IRSp53 complex formation directs specificity of rac-mediated actin cytoskeleton regulation. Mol Cell Biol 2005, 25:4602-4614.
    • (2005) Mol Cell Biol , vol.25 , pp. 4602-4614
    • Connolly, B.A.1    Rice, J.2    Feig, L.A.3    Buchsbaum, R.J.4
  • 41
    • 75149189018 scopus 로고    scopus 로고
    • Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization
    • Robens J.M., Yeow-Fong L., Ng E., Hall C., Manser E. Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization. Mol Cell Biol 2010, 30:829-844.
    • (2010) Mol Cell Biol , vol.30 , pp. 829-844
    • Robens, J.M.1    Yeow-Fong, L.2    Ng, E.3    Hall, C.4    Manser, E.5
  • 42
    • 59649118111 scopus 로고    scopus 로고
    • Enhanced NMDA receptor-mediated synaptic transmission, enhanced long-term potentiation, and impaired learning and memory in mice lacking IRSp53
    • Kim M.H., Choi J., Yang J., Chung W., Kim J.H., Paik S.K., Kim K., Han S., Won H., Bae Y.S., et al. Enhanced NMDA receptor-mediated synaptic transmission, enhanced long-term potentiation, and impaired learning and memory in mice lacking IRSp53. J Neurosci 2009, 29:1586-1595.
    • (2009) J Neurosci , vol.29 , pp. 1586-1595
    • Kim, M.H.1    Choi, J.2    Yang, J.3    Chung, W.4    Kim, J.H.5    Paik, S.K.6    Kim, K.7    Han, S.8    Won, H.9    Bae, Y.S.10
  • 45
    • 19944433966 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphogenesis by insulin receptor substrate 53, a downstream effector of Rac1 and Cdc42 small GTPases
    • Choi J., Ko J., Racz B., Burette A., Lee J.R., Kim S., Na M., Lee H.W., Kim K., Weinberg R.J., Kim E. Regulation of dendritic spine morphogenesis by insulin receptor substrate 53, a downstream effector of Rac1 and Cdc42 small GTPases. J Neurosci 2005, 25:869-879.
    • (2005) J Neurosci , vol.25 , pp. 869-879
    • Choi, J.1    Ko, J.2    Racz, B.3    Burette, A.4    Lee, J.R.5    Kim, S.6    Na, M.7    Lee, H.W.8    Kim, K.9    Weinberg, R.J.10    Kim, E.11
  • 46
    • 70350179623 scopus 로고    scopus 로고
    • Cdc42- and IRSp53-dependent contractile filopodia tether presumptive lens and retina to coordinate epithelial invagination
    • Chauhan B.K., Disanza A., Choi S.Y., Faber S.C., Lou M., Beggs H.E., Scita G., Zheng Y., Lang R.A. Cdc42- and IRSp53-dependent contractile filopodia tether presumptive lens and retina to coordinate epithelial invagination. Development 2009, 136:3657-3667.
    • (2009) Development , vol.136 , pp. 3657-3667
    • Chauhan, B.K.1    Disanza, A.2    Choi, S.Y.3    Faber, S.C.4    Lou, M.5    Beggs, H.E.6    Scita, G.7    Zheng, Y.8    Lang, R.A.9
  • 47
    • 34249722773 scopus 로고    scopus 로고
    • Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties
    • Millard T.H., Dawson J., Machesky L.M. Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties. J Cell Sci 2007, 120:1663-1672.
    • (2007) J Cell Sci , vol.120 , pp. 1663-1672
    • Millard, T.H.1    Dawson, J.2    Machesky, L.M.3
  • 50
    • 0036020201 scopus 로고    scopus 로고
    • MIM, a potential metastasis suppressor gene in bladder cancer
    • Lee Y.G., Macoska J.A., Korenchuk S., Pienta K.J. MIM, a potential metastasis suppressor gene in bladder cancer. Neoplasia 2002, 4:291-294.
    • (2002) Neoplasia , vol.4 , pp. 291-294
    • Lee, Y.G.1    Macoska, J.A.2    Korenchuk, S.3    Pienta, K.J.4
  • 51
    • 34249886299 scopus 로고    scopus 로고
    • MIM: a multifunctional scaffold protein
    • Machesky L.M., Johnston S.A. MIM: a multifunctional scaffold protein. J Mol Med 2007, 85:569-576.
    • (2007) J Mol Med , vol.85 , pp. 569-576
    • Machesky, L.M.1    Johnston, S.A.2
  • 52
    • 0037424488 scopus 로고    scopus 로고
    • Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain
    • Mattila P.K., Salminen M., Yamashiro T., Lappalainen P. Mouse MIM, a tissue-specific regulator of cytoskeletal dynamics, interacts with ATP-actin monomers through its C-terminal WH2 domain. J Biol Chem 2003, 278:8452-8459.
    • (2003) J Biol Chem , vol.278 , pp. 8452-8459
    • Mattila, P.K.1    Salminen, M.2    Yamashiro, T.3    Lappalainen, P.4
  • 53
    • 0038641656 scopus 로고    scopus 로고
    • MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta
    • Woodings J.A., Sharp S.J., Machesky L.M. MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta. Biochem J 2003, 371:463-471.
    • (2003) Biochem J , vol.371 , pp. 463-471
    • Woodings, J.A.1    Sharp, S.J.2    Machesky, L.M.3
  • 54
    • 34147108621 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of missing in metastasis protein is implicated in platelet-derived growth factor-mediated cell shape changes
    • Wang Y., Zhou K., Zeng X., Lin J., Zhan X. Tyrosine phosphorylation of missing in metastasis protein is implicated in platelet-derived growth factor-mediated cell shape changes. J Biol Chem 2007, 282:7624-7631.
    • (2007) J Biol Chem , vol.282 , pp. 7624-7631
    • Wang, Y.1    Zhou, K.2    Zeng, X.3    Lin, J.4    Zhan, X.5
  • 55
  • 56
    • 77955572608 scopus 로고    scopus 로고
    • MIM and cortactin antagonism regulates ciliogenesis and hedgehog signaling
    • Bershteyn M., Atwood S.X., Woo W.M., Li M., Oro A.E. MIM and cortactin antagonism regulates ciliogenesis and hedgehog signaling. Dev Cell 2010, 19:270-283.
    • (2010) Dev Cell , vol.19 , pp. 270-283
    • Bershteyn, M.1    Atwood, S.X.2    Woo, W.M.3    Li, M.4    Oro, A.E.5
  • 59
    • 77951179216 scopus 로고    scopus 로고
    • I-BAR protein antagonism of endocytosis mediates directional sensing during guided cell migration
    • Quinones G.A., Jin J., Oro A.E. I-BAR protein antagonism of endocytosis mediates directional sensing during guided cell migration. J Cell Biol 2010, 189:353-367.
    • (2010) J Cell Biol , vol.189 , pp. 353-367
    • Quinones, G.A.1    Jin, J.2    Oro, A.E.3
  • 60
    • 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
    • Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H., Wen L., Brady-Kalnay S.M., Mei L., et al. Signal transduction in neuronal migration: roles of GTPase activating proteins and the small GTPase Cdc42 in the Slit-Robo pathway. Cell 2001, 107:209-221.
    • (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
  • 62
    • 66249118393 scopus 로고    scopus 로고
    • Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion
    • Yang C., Hoelzle M., Disanza A., Scita G., Svitkina T. Coordination of membrane and actin cytoskeleton dynamics during filopodia protrusion. PLoS One 2009, 4:e5678.
    • (2009) PLoS One , vol.4
    • Yang, C.1    Hoelzle, M.2    Disanza, A.3    Scita, G.4    Svitkina, T.5
  • 64
    • 49849101970 scopus 로고    scopus 로고
    • Cytonemes and tunneling nanotubules in cell-cell communication and viral pathogenesis
    • Sherer N.M., Mothes W. Cytonemes and tunneling nanotubules in cell-cell communication and viral pathogenesis. Trends Cell Biol 2008, 18:414-420.
    • (2008) Trends Cell Biol , vol.18 , pp. 414-420
    • Sherer, N.M.1    Mothes, W.2


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