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Volumn 20, Issue 13, 2014, Pages 2059-2073

MICAL-family proteins: Complex regulators of the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYBENZOATE 3 MONOOXYGENASE; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; CONTRACTILE PROTEIN; CONTRACTILE PROTEIN MICAL; METHIONINE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; ACTIN; CYTOSKELETON PROTEIN;

EID: 84898483100     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5487     Document Type: Review
Times cited : (87)

References (90)
  • 2
    • 27544432463 scopus 로고    scopus 로고
    • Dynamics involved in catalysis by single-component and two-component flavindependent aromatic hydroxylases
    • Ballou DP, Entsch B, and Cole LJ. Dynamics involved in catalysis by single-component and two-component flavindependent aromatic hydroxylases. Biochem Biophys Res Commun 338: 590-598, 2005
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 590-598
    • Ballou, D.P.1    Entsch, B.2    Cole, L.J.3
  • 3
    • 33947698424 scopus 로고    scopus 로고
    • Drosophila MICAL regulates myofilament organization and synaptic structure
    • Beuchle D, Schwarz H, Langegger M, Koch I, and Aberle H. Drosophila MICAL regulates myofilament organization and synaptic structure. Mech Dev 124: 390-406, 2007
    • (2007) Mech Dev , vol.124 , pp. 390-406
    • Beuchle, D.1    Schwarz, H.2    Langegger, M.3    Koch, I.4    Aberle, H.5
  • 4
    • 34548519907 scopus 로고    scopus 로고
    • A 30-Angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase
    • Binda C, Coda A, Angelini R, Federico R, Ascenzi P, and Mattevi A. A 30-Angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase. Structure 7: 265-276, 1999
    • (1999) Structure , vol.7 , pp. 265-276
    • Binda, C.1    Coda, A.2    Angelini, R.3    Federico, R.4    Ascenzi, P.5    Mattevi, A.6
  • 5
    • 37049003033 scopus 로고    scopus 로고
    • Boundary cap cells constrain spinal motor neuron somal migration at motor exit points by a semaphorin-plexin mechanism
    • Bron R, Vermeren M, Kokot N, Andrews W, Little GE, Mitchell KJ, and Cohen J. Boundary cap cells constrain spinal motor neuron somal migration at motor exit points by a semaphorin-plexin mechanism. Neural Dev 2: 21, 2007
    • (2007) Neural Dev , vol.2 , pp. 21
    • Bron, R.1    Vermeren, M.2    Kokot, N.3    Andrews, W.4    Little, G.E.5    Mitchell, K.J.6    Cohen, J.7
  • 6
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: Mechanisms and interplay
    • Chesarone MA and Goode BL. Actin nucleation and elongation factors: Mechanisms and interplay. Curr Opin Cell Biol 21: 28-37, 2009
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 7
    • 48949106158 scopus 로고    scopus 로고
    • New insights into mechanism and regulation of actin capping protein
    • Cooper JA and Sept D. New insights into mechanism and regulation of actin capping protein. Int Rev Cell Mol Biol 267: 183-206, 2008
    • (2008) Int Rev Cell Mol Biol , vol.267 , pp. 183-206
    • Cooper, J.A.1    Sept, D.2
  • 10
    • 9744270010 scopus 로고    scopus 로고
    • Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase
    • Entsch B, Cole LJ, and Ballou DP. Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. Arch Biochem Biophys 433: 297-311, 2005
    • (2005) Arch Biochem Biophys , vol.433 , pp. 297-311
    • Entsch, B.1    Cole, L.J.2    Ballou, D.P.3
  • 11
    • 77949837372 scopus 로고    scopus 로고
    • Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress
    • Fedorova M, Kuleva N, and Hoffmann R. Identification of cysteine, methionine and tryptophan residues of actin oxidized in vivo during oxidative stress. J Proteome Res 9: 1598-1609, 2010
    • (2010) J Proteome Res , vol.9 , pp. 1598-1609
    • Fedorova, M.1    Kuleva, N.2    Hoffmann, R.3
  • 12
    • 0033214990 scopus 로고    scopus 로고
    • Septins: Cytoskeletal polymers or signalling GTPases?
    • Field CM and Kellogg D. Septins: Cytoskeletal polymers or signalling GTPases?. Trends Cell Biol 9: 387-394, 1999
    • (1999) Trends Cell Biol , vol.9 , pp. 387-394
    • Field, C.M.1    Kellogg, D.2
  • 13
    • 13444309296 scopus 로고    scopus 로고
    • The MICAL proteins and rab1: A possible link to the cytoskeleton?
    • Fischer J, Weide T, and Barnekow A. The MICAL proteins and rab1: A possible link to the cytoskeleton?. Biochem Biophys Res Commun 328: 415-423, 2005
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 415-423
    • Fischer, J.1    Weide, T.2    Barnekow, A.3
  • 14
    • 63949088199 scopus 로고    scopus 로고
    • Alternative splicing formembers ofhumanmosaic domain superfamilies i the chand limdomains containing group of proteins
    • Friedberg F.Alternative splicing formembers ofhumanmosaic domain superfamilies. I. The CHand LIMdomains containing group of proteins. Mol Biol Rep 36: 1059-1081, 2009
    • (2009) Mol Biol Rep , vol.36 , pp. 1059-1081
    • Friedberg, F.1
  • 15
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-Actinin function
    • Fukami K, Furuhashi K, Inagaki M, Endo T, Hatano S, and Takenawa T. Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-Actinin function. Nature 359: 150-152, 1992
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Furuhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 17
    • 46749156739 scopus 로고    scopus 로고
    • Large scale screening for novel rab effectors reveals unexpected broad Rab binding specificity
    • Fukuda M, Kanno E, Ishibashi K, and Itoh T. Large scale screening for novel rab effectors reveals unexpected broad Rab binding specificity. Mol Cell Proteomics 7: 1031-1042, 2008
    • (2008) Mol Cell Proteomics , vol.7 , pp. 1031-1042
    • Fukuda, M.1    Kanno, E.2    Ishibashi, K.3    Itoh, T.4
  • 20
    • 84898471180 scopus 로고    scopus 로고
    • Trafficking cascades mediated by Rab35 and its membrane hub effector MICAL-L1
    • Giridharan SS, Cai B, Naslavsky N, and Caplan S. Trafficking cascades mediated by Rab35 and its membrane hub effector, MICAL-L1. Commun Integr Biol 5: 384-387, 2012
    • (2012) Commun Integr Biol , vol.5 , pp. 384-387
    • Giridharan, S.S.1    Cai, B.2    Naslavsky, N.3    Caplan, S.4
  • 21
    • 84878686056 scopus 로고    scopus 로고
    • Cooperation of MICAL-L1, syndapin2 and phosphatidic acid in tubular recycling endosome biogenesis
    • Giridharan SS, Cai B, Vitale N, Naslavsky N, and Caplan S. Cooperation of MICAL-L1, syndapin2 and phosphatidic acid in tubular recycling endosome biogenesis. Mol Biol Cell 24: 1776-1790, 2013
    • (2013) Mol Biol Cell , vol.24 , pp. 1776-1790
    • Giridharan, S.S.1    Cai, B.2    Vitale, N.3    Naslavsky, N.4    Caplan, S.5
  • 22
    • 84858119850 scopus 로고    scopus 로고
    • Differential regulation of actin microfilaments by human MICAL proteins
    • Giridharan SS, Rohn JL, Naslavsky N, and Caplan S. Differential regulation of actin microfilaments by human MICAL proteins. J Cell Sci 125: 614-624, 2012
    • (2012) J Cell Sci , vol.125 , pp. 614-624
    • Giridharan, S.S.1    Rohn, J.L.2    Naslavsky, N.3    Caplan, S.4
  • 24
    • 0037065995 scopus 로고    scopus 로고
    • Knowing how to navigate: Mechanisms of semaphorin signaling in the nervous system
    • He Z, Wang KC, Koprivica V, Ming G, and Song HJ. Knowing how to navigate: Mechanisms of semaphorin signaling in the nervous system. Sci STKE 2002: Re1, 2002
    • (2002) Sci STKE , vol.2002
    • He, Z.1    Wang, K.C.2    Koprivica, V.3    Ming, G.4    Song, H.J.5
  • 26
    • 0033584466 scopus 로고    scopus 로고
    • P130(Cas), an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts
    • Honda H, Nakamoto T, Sakai R, and Hirai H. p130(Cas), an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts. Biochem Biophys Res Commun 262: 25-30, 1999
    • (1999) Biochem Biophys Res Commun , vol.262 , pp. 25-30
    • Honda, H.1    Nakamoto, T.2    Sakai, R.3    Hirai, H.4
  • 27
    • 84455205549 scopus 로고    scopus 로고
    • Direct redox regulation of F-Actin assembly and disassembly by Mical
    • Hung RJ, Pak CW, and Terman Jr. Direct redox regulation of F-Actin assembly and disassembly by Mical. Science 334: 1710-1713, 2011
    • (2011) Science , vol.334 , pp. 1710-1713
    • Hung, R.J.1    Pak, C.W.2    Terman, J.R.3
  • 29
    • 0018801142 scopus 로고
    • Kinetic studies on the reaction of p-hydroxybenzoate hydroxylase. Agreement of steady state and rapid reaction data
    • Husain M and Massey V. Kinetic studies on the reaction of p-hydroxybenzoate hydroxylase. Agreement of steady state and rapid reaction data. J Biol Chem 254: 6657-6666, 1979
    • (1979) J Biol Chem , vol.254 , pp. 6657-6666
    • Husain, M.1    Massey, V.2
  • 30
    • 34547563475 scopus 로고    scopus 로고
    • Investigation of the four cooperative unfolding units existing in theMICAL-1 CH domain
    • Jin X, Zhang J, Dai H, Sun H, Wang D, Wu J, and Shi Y. Investigation of the four cooperative unfolding units existing in theMICAL-1 CH domain. Biophys Chem 129: 269-278, 2007
    • (2007) Biophys Chem , vol.129 , pp. 269-278
    • Jin, X.1    Zhang, J.2    Dai, H.3    Sun, H.4    Wang, D.5    Wu, J.6    Shi, Y.7
  • 31
    • 25844431756 scopus 로고    scopus 로고
    • Touch and go: Guidance cues signal to the growth cone cytoskeleton
    • Kalil K and Dent EW. Touch and go: Guidance cues signal to the growth cone cytoskeleton. Curr Opin Neurobiol 15: 521-526, 2005
    • (2005) Curr Opin Neurobiol , vol.15 , pp. 521-526
    • Kalil, K.1    Dent, E.W.2
  • 34
    • 0037112944 scopus 로고    scopus 로고
    • Syndapins integrate N-WASP in receptor-mediated endocytosis
    • Kessels MM and Qualmann B. Syndapins integrate N-WASP in receptor-mediated endocytosis. EMBO J 21: 6083-6094, 2002
    • (2002) EMBO J , vol.21 , pp. 6083-6094
    • Kessels, M.M.1    Qualmann, B.2
  • 35
    • 77950551801 scopus 로고    scopus 로고
    • Mechanism for the selective interaction of C-Terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners
    • Kieken F, Sharma M, Jovic M, Giridharan SS, Naslavsky N, Caplan S, and Sorgen PL. Mechanism for the selective interaction of C-Terminal Eps15 homology domain proteins with specific Asn-Pro-Phe-containing partners. J Biol Chem 285: 8687-8694, 2010
    • (2010) J Biol Chem , vol.285 , pp. 8687-8694
    • Kieken, F.1    Sharma, M.2    Jovic, M.3    Giridharan, S.S.4    Naslavsky, N.5    Caplan, S.6    Sorgen, P.L.7
  • 37
    • 84934441397 scopus 로고    scopus 로고
    • MICAL flavoprotein monooxygenases: Structure, function and role in semaphorin signaling
    • Kolk SM and Pasterkamp RJ. MICAL flavoprotein monooxygenases: Structure, function and role in semaphorin signaling. Adv Exp Med Biol 600: 38-51, 2007
    • (2007) Adv Exp Med Biol , vol.600 , pp. 38-51
    • Kolk, S.M.1    Pasterkamp, R.J.2
  • 38
    • 0037106588 scopus 로고    scopus 로고
    • Calponin homology domains at a glance
    • Korenbaum E and Rivero F. Calponin homology domains at a glance. J Cell Sci 115: 3543-3545, 2002
    • (2002) J Cell Sci , vol.115 , pp. 3543-3545
    • Korenbaum, E.1    Rivero, F.2
  • 39
    • 0037108204 scopus 로고    scopus 로고
    • Inhibition of PTPs by H (2)O(2) regulates the activation of distinct MAPK pathways Free Radic
    • Lee K and Esselman WJ. Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways. Free Radic Biol Med 33: 1121-1132, 2002
    • (2002) Biol Med , vol.33 , pp. 1121-1132
    • Lee, K.1    Esselman, W.J.2
  • 40
    • 77956020315 scopus 로고    scopus 로고
    • Regulation of actin cytoskeleton dynamics in cells
    • Lee SH and Dominguez R. Regulation of actin cytoskeleton dynamics in cells. Mol Cells 29: 311-325, 2010
    • (2010) Mol Cells , vol.29 , pp. 311-325
    • Lee, S.H.1    Dominguez, R.2
  • 41
    • 58149250201 scopus 로고    scopus 로고
    • Identification of interaction partners for individual SH3 domains of Fas ligand associated members of the PCH protein family in T lymphocytes
    • Linkermann A, Gelhaus C, Lettau M, Qian J, Kabelitz D, and Janssen O. Identification of interaction partners for individual SH3 domains of Fas ligand associated members of the PCH protein family in T lymphocytes. Biochim Biophys Acta 1794: 168-176, 2009
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 168-176
    • Linkermann, A.1    Gelhaus, C.2    Lettau, M.3    Qian, J.4    Kabelitz, D.5    Janssen, O.6
  • 42
    • 80052280261 scopus 로고    scopus 로고
    • Expression pattern of Mical-1 in the temporal neocortex of patients with intractable temporal epilepsy and pilocarpine-induced rat model
    • Luo J, Xu Y, Zhu Q, Zhao F, Zhang Y, Peng X, Wang W, and Wang X. Expression pattern of Mical-1 in the temporal neocortex of patients with intractable temporal epilepsy and pilocarpine-induced rat model. Synapse 65: 1213-1221, 2011
    • (2011) Synapse , vol.65 , pp. 1213-1221
    • Luo, J.1    Xu, Y.2    Zhu, Q.3    Zhao, F.4    Zhang, Y.5    Peng, X.6    Wang, W.7    Wang, X.8
  • 43
    • 34347246721 scopus 로고    scopus 로고
    • Mechanisms of axon guidance: Membrane dynamics and axonal transport in semaphorin signalling
    • Mann F and Rougon G. Mechanisms of axon guidance: Membrane dynamics and axonal transport in semaphorin signalling. J Neurochem 102: 316-323, 2007
    • (2007) J Neurochem , vol.102 , pp. 316-323
    • Mann, F.1    Rougon, G.2
  • 44
    • 0028450859 scopus 로고
    • Actin crosslinking proteins at the leading edge
    • Matsudaira P. Actin crosslinking proteins at the leading edge. Semin Cell Biol 5: 165-174, 1994
    • (1994) Semin Cell Biol , vol.5 , pp. 165-174
    • Matsudaira, P.1
  • 46
    • 0031005242 scopus 로고    scopus 로고
    • Electrostatic effects on substrate activation in para-hydroxybenzoate hydroxylase: Studies of the mutant lysine 297 methionine
    • Moran GR, Entsch B, Palfey BA, and Ballou DP. Electrostatic effects on substrate activation in para-hydroxybenzoate hydroxylase: Studies of the mutant lysine 297 methionine. Biochemistry 36: 7548-7556, 1997
    • (1997) Biochemistry , vol.36 , pp. 7548-7556
    • Moran, G.R.1    Entsch, B.2    Palfey, B.A.3    Ballou, D.P.4
  • 49
    • 79952322355 scopus 로고    scopus 로고
    • The filamins: Organizers of cell structure and function
    • Nakamura F, Stossel TP, and Hartwig JH. The filamins: Organizers of cell structure and function. Cell Adh Migr 5: 160-169, 2011
    • (2011) Cell Adh Migr , vol.5 , pp. 160-169
    • Nakamura, F.1    Stossel, T.P.2    Hartwig, J.H.3
  • 50
    • 43249083763 scopus 로고    scopus 로고
    • Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions
    • Nakatsuji H, Nishimura N, Yamamura R, Kanayama HO, and Sasaki T. Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions. Mol Cell Biol 28: 3324-3335, 2008
    • (2008) Mol Cell Biol , vol.28 , pp. 3324-3335
    • Nakatsuji, H.1    Nishimura, N.2    Yamamura, R.3    Kanayama, H.O.4    Sasaki, T.5
  • 51
    • 20744434543 scopus 로고    scopus 로고
    • Plexins: Axon guidance and signal transduction
    • Negishi M, Oinuma I, and Katoh H. Plexins: Axon guidance and signal transduction. Cell Mol Life Sci 62: 1363-1371, 2005
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1363-1371
    • Negishi, M.1    Oinuma, I.2    Katoh, H.3
  • 52
    • 67649344114 scopus 로고    scopus 로고
    • Involvement of ELKS, an active zone protein, in exocytotic release from RBL-2H3 cells
    • Nomura H, Ohtsuka T, Tadokoro S, Tanaka M, and Hirashima N. Involvement of ELKS, an active zone protein, in exocytotic release from RBL-2H3 cells. Cell Immunol 258: 204-211, 2009
    • (2009) Cell Immunol , vol.258 , pp. 204-211
    • Nomura, H.1    Ohtsuka, T.2    Tadokoro, S.3    Tanaka, M.4    Hirashima, N.5
  • 53
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono S. Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 258: 1-82, 2007
    • (2007) Int Rev Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 54
    • 0033594867 scopus 로고    scopus 로고
    • Use of free energy relationships to probe the individual steps of hydroxylation of p-hydroxybenzoate hydroxylase: Studies with a series of 8-substituted flavins
    • Ortiz-Maldonado M, Ballou DP, and Massey V. Use of free energy relationships to probe the individual steps of hydroxylation of p-hydroxybenzoate hydroxylase: Studies with a series of 8-substituted flavins. Biochemistry 38: 8124-8137, 1999
    • (1999) Biochemistry , vol.38 , pp. 8124-8137
    • Ortiz-Maldonado, M.1    Ballou, D.P.2    Massey, V.3
  • 55
    • 2442481067 scopus 로고    scopus 로고
    • Alpha-Actinin revisited: A fresh look at an old player
    • Otey CA and Carpen O. Alpha-Actinin revisited: A fresh look at an old player. Cell Motil Cytoskeleton 58: 104-111, 2004
    • (2004) Cell Motil Cytoskeleton , vol.58 , pp. 104-111
    • Otey, C.A.1    Carpen, O.2
  • 56
    • 72049124811 scopus 로고    scopus 로고
    • Control of catalysis in flavindependent monooxygenases
    • Palfey BA and McDonald CA. Control of catalysis in flavindependent monooxygenases. Arch Biochem Biophys 493: 26-36, 2010
    • (2010) Arch Biochem Biophys , vol.493 , pp. 26-36
    • Palfey, B.A.1    McDonald, C.A.2
  • 58
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/ 3 complex and formins
    • Pollard TD. Regulation of actin filament assembly by Arp2/ 3 complex and formins. Annu Rev Biophys Biomol Struct 36: 451-477, 2007
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 59
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard TD and Cooper JA. Actin, a central player in cell shape and movement. Science 326: 1208-1212, 2009
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 60
    • 77957781807 scopus 로고    scopus 로고
    • Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors
    • Rahajeng J, Giridharan SS, Naslavsky N, and Caplan S. Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors. J Biol Chem 285: 31918-31922, 2010
    • (2010) J Biol Chem , vol.285 , pp. 31918-31922
    • Rahajeng, J.1    Giridharan, S.S.2    Naslavsky, N.3    Caplan, S.4
  • 61
    • 0033956733 scopus 로고    scopus 로고
    • Semaphorins and their receptors in vertebrates and invertebrates
    • Raper JA. Semaphorins and their receptors in vertebrates and invertebrates. Curr Opin Neurobiol 10: 88-94, 2000
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 88-94
    • Raper, J.A.1
  • 63
    • 79952541830 scopus 로고    scopus 로고
    • Sox14 is required for transcriptional and developmental responses to 20-hydroxyecdysone at the onset of Drosophila metamorphosis
    • Ritter AR and Beckstead RB. Sox14 is required for transcriptional and developmental responses to 20-hydroxyecdysone at the onset of Drosophila metamorphosis. Dev Dyn 239: 2685-2694, 2010
    • (2010) Dev Dyn , vol.239 , pp. 2685-2694
    • Ritter, A.R.1    Beckstead, R.B.2
  • 64
    • 0025791007 scopus 로고
    • Oxidation of thiol in the vimentin cytoskeleton
    • Rogers KR, Morris CJ, and Blake DR. Oxidation of thiol in the vimentin cytoskeleton. Biochem J 275 (Pt 3): 789-791, 1991
    • (1991) Biochem J , vol.275 , Issue.PART 3 , pp. 789-791
    • Rogers, K.R.1    Morris, C.J.2    Blake, D.R.3
  • 65
    • 84871149106 scopus 로고    scopus 로고
    • Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development
    • Sakane A, Abdallah AA, Nakano K, Honda K, Ikeda W, Nishikawa Y, Matsumoto M, Matsushita N, Kitamura T, and Sasaki T. Rab13 small G protein and junctional Rab13-binding protein (JRAB) orchestrate actin cytoskeletal organization during epithelial junctional development. J Biol Chem 287: 42455-42468, 2012
    • (2012) J Biol Chem , vol.287 , pp. 42455-42468
    • Sakane, A.1    Abdallah, A.A.2    Nakano, K.3    Honda, K.4    Ikeda, W.5    Nishikawa, Y.6    Matsumoto, M.7    Matsushita, N.8    Kitamura, T.9    Sasaki, T.10
  • 66
    • 75749094781 scopus 로고    scopus 로고
    • Rab13 regulates neurite outgrowth in PC12 cells through its effector protein JRAB/ MICAL-L2
    • Sakane A, Honda K, and Sasaki T. Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/ MICAL-L2. Mol Cell Biol 30: 1077-1087, 2010
    • (2010) Mol Cell Biol , vol.30 , pp. 1077-1087
    • Sakane, A.1    Honda, K.2    Sasaki, T.3
  • 67
    • 39849089206 scopus 로고    scopus 로고
    • Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein
    • Schmidt EF, Shim SO, and Strittmatter SM. Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein. J Neurosci 28: 2287-2297, 2008
    • (2008) J Neurosci , vol.28 , pp. 2287-2297
    • Schmidt, E.F.1    Shim, S.O.2    Strittmatter, S.M.3
  • 68
    • 0028145298 scopus 로고
    • Crystal structures of wild-Type p-hydroxybenzoate hydroxylase complexed with 4-Aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4-Aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4-Aminobenzoate Evidence for a proton channel and a new binding mode of the flavin ring
    • Schreuder HA, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, and van Berkel WJ. Crystal structures of wild-Type p-hydroxybenzoate hydroxylase complexed with 4-Aminobenzoate,2,4-dihydroxybenzoate, and 2-hydroxy-4- Aminobenzoate and of the Tyr222Ala mutant complexed with 2-hydroxy-4- Aminobenzoate. Evidence for a proton channel and a new binding mode of the flavin ring. Biochemistry 33: 10161-10170, 1994
    • (1994) Biochemistry , vol.33 , pp. 10161-10170
    • Schreuder, H.A.1    Mattevi, A.2    Obmolova, G.3    Kalk, K.H.4    Hol, W.G.5    Van Der Bolt, F.J.6    Van Berkel, W.J.7
  • 69
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 19A resolution Analysis of the enzyme-substrate and enzyme-product complexes
    • Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, and Drenth J. Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9A resolution. Analysis of the enzyme-substrate and enzyme-product complexes. J Mol Biol 208: 679-696, 1989
    • (1989) J Mol Biol , vol.208 , pp. 679-696
    • Schreuder, H.A.1    Prick, P.A.2    Wierenga, R.K.3    Vriend, G.4    Wilson, K.S.5    Hol, W.G.6    Drenth, J.7
  • 71
    • 73849118696 scopus 로고    scopus 로고
    • MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling
    • Sharma M, Giridharan SS, Rahajeng J, Naslavsky N, and Caplan S. MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling. Mol Biol Cell 20: 5181-5194, 2009
    • (2009) Mol Biol Cell , vol.20 , pp. 5181-5194
    • Sharma, M.1    Giridharan, S.S.2    Rahajeng, J.3    Naslavsky, N.4    Caplan, S.5
  • 72
    • 0018786082 scopus 로고
    • On the stable enzymesubstrate complex of p-hydroxybenzoate hydroxylase Evidences for the proton uptake from the substrate
    • Shoun H, Beppu T, and Arima K. On the stable enzymesubstrate complex of p-hydroxybenzoate hydroxylase. Evidences for the proton uptake from the substrate. J Biol Chem 254: 899-904, 1979
    • (1979) J Biol Chem , vol.254 , pp. 899-904
    • Shoun, H.1    Beppu, T.2    Arima, K.3
  • 74
    • 77953590866 scopus 로고    scopus 로고
    • Regulation of microtubule organization and functions by septin GTPases
    • Spiliotis ET. Regulation of microtubule organization and functions by septin GTPases. Cytoskeleton (Hoboken) 67: 339-345, 2010
    • (2010) Cytoskeleton (Hoboken , vol.67 , pp. 339-345
    • Spiliotis, E.T.1
  • 80
    • 33745754458 scopus 로고    scopus 로고
    • JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin
    • Terai T, Nishimura N, Kanda I, Yasui N, and Sasaki T. JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin. Mol Biol Cell 17: 2465-2475, 2006
    • (2006) Mol Biol Cell , vol.17 , pp. 2465-2475
    • Terai, T.1    Nishimura, N.2    Kanda, I.3    Yasui, N.4    Sasaki, T.5
  • 81
    • 0037188897 scopus 로고    scopus 로고
    • MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion
    • Terman JR, Mao T, Pasterkamp RJ, Yu HH, and Kolodkin AL. MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion. Cell 109: 887-900, 2002
    • (2002) Cell , vol.109 , pp. 887-900
    • Terman, J.R.1    Mao, T.2    Pasterkamp, R.J.3    Yu, H.H.4    Kolodkin, A.L.5
  • 82
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • van Berkel WJ, Kamerbeek NM, and Fraaije MW. Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J Biotechnol 124: 670-689, 2006
    • (2006) J Biotechnol , vol.124 , pp. 670-689
    • Van Berkel, W.J.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 83
    • 2142796628 scopus 로고    scopus 로고
    • Semaphorins: Green light for redox signaling?
    • Ventura A and Pelicci PG. Semaphorins: Green light for redox signaling?. Sci STKE 2002: Pe44, 2002
    • (2002) Sci STKE , vol.2002 , pp. 44
    • Ventura, A.1    Pelicci, P.G.2
  • 84
    • 57649102412 scopus 로고    scopus 로고
    • NDR kinase is activated by RASSF1A/ MST1 in response to Fas receptor stimulation and promotes apoptosis
    • Vichalkovski A, Gresko E, Cornils H, Hergovich A, Schmitz D, and Hemmings BA. NDR kinase is activated by RASSF1A/ MST1 in response to Fas receptor stimulation and promotes apoptosis. Curr Biol 18: 1889-1895, 2008
    • (2008) Curr Biol , vol.18 , pp. 1889-1895
    • Vichalkovski, A.1    Gresko, E.2    Cornils, H.3    Hergovich, A.4    Schmitz, D.5    Hemmings, B.A.6
  • 86
    • 77958525374 scopus 로고    scopus 로고
    • Identification and expression analysis of mical family genes in zebrafish
    • Xue Y, Kuok C, Xiao A, Zhu Z, Lin S, and Zhang B. Identification and expression analysis of mical family genes in zebrafish. J Genet Genomics 37: 685-693, 2010
    • (2010) J Genet Genomics , vol.37 , pp. 685-693
    • Xue, Y.1    Kuok, C.2    Xiao, A.3    Zhu, Z.4    Lin, S.5    Zhang, B.6
  • 87
    • 41649098638 scopus 로고    scopus 로고
    • The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions
    • Yamamura R, Nishimura N, Nakatsuji H, Arase S, and Sasaki T. The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions. Mol Biol Cell 19: 971-983, 2008
    • (2008) Mol Biol Cell , vol.19 , pp. 971-983
    • Yamamura, R.1    Nishimura, N.2    Nakatsuji, H.3    Arase, S.4    Sasaki, T.5
  • 88
    • 34548420681 scopus 로고    scopus 로고
    • The diverse biofunctions of LIM domain proteins: Determined by subcellular localization and protein-protein interaction
    • Zheng Q and Zhao Y. The diverse biofunctions of LIM domain proteins: Determined by subcellular localization and protein-protein interaction. Biol Cell 99: 489-502, 2007
    • (2007) Biol Cell , vol.99 , pp. 489-502
    • Zheng, Q.1    Zhao, Y.2
  • 90
    • 80054008376 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1
    • Zucchini D, Caprini G, Pasterkamp RJ, Tedeschi G, and Vanoni MA. Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1. Arch Biochem Biophys 515: 1-13, 2011.
    • (2011) Arch Biochem Biophys , vol.515 , pp. 1-13
    • Zucchini, D.1    Caprini, G.2    Pasterkamp, R.J.3    Tedeschi, G.4    Vanoni, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.