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Volumn 14, Issue 2, 2013, Pages 3595-3620

Epidermal growth factor stimulates extracellular-signal regulated kinase phosphorylation of a novel site on cytoplasmic dynein intermediate chain 2

Author keywords

Dynactin; Dynein; ERK; Phosphorylation

Indexed keywords

CYTOPLASMIC DYNEIN; CYTOPLASMIC DYNEIN INTERMEDIATE CHAIN 2; DYNACTIN; EPIDERMAL GROWTH FACTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; SERINE; THREONINE; UNCLASSIFIED DRUG; UO 126;

EID: 84875116092     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14023595     Document Type: Article
Times cited : (8)

References (67)
  • 1
    • 0342965191 scopus 로고
    • Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431
    • Haigler, H.; Ash, J.F.; Singer, S.J.; Cohen, S. Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431. Proc. Natl. Acad. Sci. USA 1978, 75, 3317-3321.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3317-3321
    • Haigler, H.1    Ash, J.F.2    Singer, S.J.3    Cohen, S.4
  • 2
    • 0022310980 scopus 로고
    • Epidermal growth factor: Biology and receptor metabolism
    • Carpenter, G. Epidermal growth factor: Biology and receptor metabolism. J. Cell Sci. 1985, 3, 1-9.
    • (1985) J. Cell Sci. , vol.3 , pp. 1-9
    • Carpenter, G.1
  • 3
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • Di, G.M.; Baass, P.C.; Ou, W.J.; Posner, B.I.; Bergeron, J.J. Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 1994, 13, 4269-4277.
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 6
    • 0034597554 scopus 로고    scopus 로고
    • Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy
    • Sorkin, A.; McClure, M.; Huang, F.; Carter, R. Interaction of EGF receptor and grb2 in living cells visualized by fluorescence resonance energy transfer (FRET) microscopy. Curr. Biol. 2000, 10, 1395-1398.
    • (2000) Curr. Biol. , vol.10 , pp. 1395-1398
    • Sorkin, A.1    McClure, M.2    Huang, F.3    Carter, R.4
  • 7
    • 0036787904 scopus 로고    scopus 로고
    • Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival
    • Wang, Y.; Pennock, S.; Chen, X.; Wang, Z. Endosomal signaling of epidermal growth factor receptor stimulates signal transduction pathways leading to cell survival. Mol. Cell Biol. 2002, 22, 7279-7290.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7279-7290
    • Wang, Y.1    Pennock, S.2    Chen, X.3    Wang, Z.4
  • 8
    • 0042130366 scopus 로고    scopus 로고
    • Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling
    • Pennock, S.; Wang, Z. Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling. Mol. Cell Biol. 2003, 23, 5803-5815.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5803-5815
    • Pennock, S.1    Wang, Z.2
  • 9
    • 1542289711 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-mediated signal transduction from endosomes
    • Wang, Y.; Pennock, S.D.; Chen, X.; Kazlauskas, A.; Wang, Z. Platelet-derived growth factor receptor-mediated signal transduction from endosomes. J. Biol. Chem. 2004, 279, 8038-8046.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8038-8046
    • Wang, Y.1    Pennock, S.D.2    Chen, X.3    Kazlauskas, A.4    Wang, Z.5
  • 10
    • 2542421751 scopus 로고    scopus 로고
    • Dynein motors transport activated Trks to promote survival of target-dependent neurons
    • Heerssen, H.M.; Pazyra, M.F.; Segal, R.A. Dynein motors transport activated Trks to promote survival of target-dependent neurons. Nat. Neurosci. 2004, 7, 596-604.
    • (2004) Nat. Neurosci. , vol.7 , pp. 596-604
    • Heerssen, H.M.1    Pazyra, M.F.2    Segal, R.A.3
  • 11
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A.V.; Lamaze, C.; Schmid, S.L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 1996, 274, 2086-2089.
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 12
    • 37049019067 scopus 로고    scopus 로고
    • Late endosomal traffic of the epidermal growth factor receptor ensures spatial and temporal fidelity of mitogen-activated protein kinase signaling
    • Taub, N.; Teis, D.; Ebner, H.L.; Hess, M.W.; Huber, L.A. Late endosomal traffic of the epidermal growth factor receptor ensures spatial and temporal fidelity of mitogen-activated protein kinase signaling. Mol. Biol. Cell 2007, 18, 4698-4710.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4698-4710
    • Taub, N.1    Teis, D.2    Ebner, H.L.3    Hess, M.W.4    Huber, L.A.5
  • 13
    • 0029943566 scopus 로고    scopus 로고
    • The pool of MAP kinase associated with microtubules is small but constitutively active
    • Morishima-Kawashima, M.; Kosik, K.S. The pool of MAP kinase associated with microtubules is small but constitutively active. Mol. Biol. Cell 1996, 7, 893-905.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 893-905
    • Morishima-Kawashima, M.1    Kosik, K.S.2
  • 15
    • 0030855766 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions
    • Reszka, A.A.; Bulinski, J.C.; Krebs, E.G.; Fischer, E.H. Mitogen-activated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions. Mol. Biol. Cell 1997, 8, 1219-1232.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1219-1232
    • Reszka, A.A.1    Bulinski, J.C.2    Krebs, E.G.3    Fischer, E.H.4
  • 16
    • 0005261734 scopus 로고
    • Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro
    • Ray, L.B.; Sturgill, T.W. Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro. Proc. Natl. Acad. Sci. USA 1987, 84, 1502-1506.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1502-1506
    • Ray, L.B.1    Sturgill, T.W.2
  • 17
    • 14744272478 scopus 로고    scopus 로고
    • Regulation of bidirectional melanosome transport by organelle bound MAP kinase
    • Deacon, S.W.; Nascimento, A.; Serpinskaya, A.S.; Gelfand, V.I. Regulation of bidirectional melanosome transport by organelle bound MAP kinase. Curr. Biol. 2005, 15, 459-463.
    • (2005) Curr. Biol. , vol.15 , pp. 459-463
    • Deacon, S.W.1    Nascimento, A.2    Serpinskaya, A.S.3    Gelfand, V.I.4
  • 24
    • 1542284071 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase feedback phosphorylation regulates MEK1 complex formation and activation during cellular adhesion
    • Eblen, S.T.; Slack-Davis, J.K.; Tarcsafalvi, A.; Parsons, J.T.; Weber, M.J.; Catling, A.D. Mitogen-activated protein kinase feedback phosphorylation regulates MEK1 complex formation and activation during cellular adhesion. Mol. Cell Biol. 2004, 24, 2308-2317.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 2308-2317
    • Eblen, S.T.1    Slack-Davis, J.K.2    Tarcsafalvi, A.3    Parsons, J.T.4    Weber, M.J.5    Catling, A.D.6
  • 25
    • 0029164688 scopus 로고
    • A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function
    • Catling, A.D.; Schaeffer, H.J.; Reuter, C.W.; Reddy, G.R.; Weber, M.J. A proline-rich sequence unique to MEK1 and MEK2 is required for Raf binding and regulates MEK function. Mol. Cell Biol. 1995, 15, 5214-5225.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 5214-5225
    • Catling, A.D.1    Schaeffer, H.J.2    Reuter, C.W.3    Reddy, G.R.4    Weber, M.J.5
  • 26
    • 0028276218 scopus 로고
    • Growth factor-stimulated MAP kinase induces rapid retrophosphorylation and inhibition of MAP kinase kinase (MEK1)
    • Brunet, A.; Pages, G.; Pouyssegur, J. Growth factor-stimulated MAP kinase induces rapid retrophosphorylation and inhibition of MAP kinase kinase (MEK1). FEBS Lett. 1994, 346, 299-303.
    • (1994) FEBS Lett. , vol.346 , pp. 299-303
    • Brunet, A.1    Pages, G.2    Pouyssegur, J.3
  • 27
    • 0028091983 scopus 로고
    • Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles
    • Dillman, J.F., III; Pfister, K.K. Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles. J. Cell Biol. 1994, 127, 1671-1681.
    • (1994) J. Cell Biol. , vol.127 , pp. 1671-1681
    • Dillman III, J.F.1    Pfister, K.K.2
  • 28
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan, K.T.; Vallee, R.B. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J. Cell Biol. 1995, 131, 1507-1516.
    • (1995) J. Cell Biol. , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 29
    • 77955362436 scopus 로고    scopus 로고
    • Mouse cytoplasmic dynein intermediate chains: Identification of new isoforms, alternative splicing and tissue distribution of transcripts
    • Kuta, A.; Deng, W.; Morsi El-Kadi, A.; Banks, G.T.; Hafezparast, M.; Pfister, K.K.; Fisher, E.M. Mouse cytoplasmic dynein intermediate chains: Identification of new isoforms, alternative splicing and tissue distribution of transcripts. PLoS One 2010, 5, e11682.
    • (2010) PLoS One , vol.5
    • Kuta, A.1    Deng, W.2    Morsi El-Kadi, A.3    Banks, G.T.4    Hafezparast, M.5    Pfister, K.K.6    Fisher, E.M.7
  • 30
    • 0030066783 scopus 로고    scopus 로고
    • Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia
    • Pfister, K.K.; Salata, M.W.; Dillman, J.F., III; Vaughan, K.T.; Vallee, R.B.; Torre, E.; Lye, R.J. Differential expression and phosphorylation of the 74-kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia. J. Biol. Chem. 1996, 271, 1687-1694.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1687-1694
    • Pfister, K.K.1    Salata, M.W.2    Dillman III, J.F.3    Vaughan, K.T.4    Vallee, R.B.5    Torre, E.6    Lye, R.J.7
  • 31
    • 0030065813 scopus 로고    scopus 로고
    • Identification and developmental regulation of a neuron-specific subunit of cytoplasmic dynein
    • Pfister, K.K.; Salata, M.W.; Dillman, J.F., III; Torre, E.; Lye, R.J. Identification and developmental regulation of a neuron-specific subunit of cytoplasmic dynein. Mol. Biol. Cell 1996, 7, 331-343.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 331-343
    • Pfister, K.K.1    Salata, M.W.2    Dillman III, J.F.3    Torre, E.4    Lye, R.J.5
  • 32
    • 0035854775 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin
    • Vaughan, P.S.; Leszyk, J.D.; Vaughan, K.T. Cytoplasmic dynein intermediate chain phosphorylation regulates binding to dynactin. J. Biol. Chem. 2001, 276, 26171-26179.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26171-26179
    • Vaughan, P.S.1    Leszyk, J.D.2    Vaughan, K.T.3
  • 34
    • 0035449118 scopus 로고    scopus 로고
    • Growth factor regulation of cytoplasmic dynein intermediate chain subunit expression preceding neurite extension
    • Salata, M.W.; Dillman, J.F., III; Lye, R.J.; Pfister, K.K. Growth factor regulation of cytoplasmic dynein intermediate chain subunit expression preceding neurite extension. J. Neurosci. Res. 2001, 65, 408-416.
    • (2001) J. Neurosci. Res. , vol.65 , pp. 408-416
    • Salata, M.W.1    Dillman III, J.F.2    Lye, R.J.3    Pfister, K.K.4
  • 38
    • 84868130014 scopus 로고    scopus 로고
    • Trk activation of the ERK1/2 kinase pathway stimulates intermediate chain phosphorylation and recruits cytoplasmic dynein to signaling endosomes for retrograde axonal transport
    • Mitchell, D.J.; Blasier, K.R.; Jeffery, E.D.; Ross, M.W.; Pullikuth, A.K.; Suo, D.; Park, J.; Smiley, W.R.; Lo, K.W.; Shabanowitz, J.; et al. Trk activation of the ERK1/2 kinase pathway stimulates intermediate chain phosphorylation and recruits cytoplasmic dynein to signaling endosomes for retrograde axonal transport. J. Neurosci. 2012, 32, 15495-15510.
    • (2012) J. Neurosci. , vol.32 , pp. 15495-15510
    • Mitchell, D.J.1    Blasier, K.R.2    Jeffery, E.D.3    Ross, M.W.4    Pullikuth, A.K.5    Suo, D.6    Park, J.7    Smiley, W.R.8    Lo, K.W.9    Shabanowitz, J.10
  • 39
    • 0029742626 scopus 로고    scopus 로고
    • Functionally distinct isoforms of dynactin are expressed in human neurons
    • Tokito, M.K.; Howland, D.S.; Lee, V.M.; Holzbaur, E.L. Functionally distinct isoforms of dynactin are expressed in human neurons. Mol. Biol. Cell 1996, 7, 1167-1180.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1167-1180
    • Tokito, M.K.1    Howland, D.S.2    Lee, V.M.3    Holzbaur, E.L.4
  • 40
    • 77952359189 scopus 로고    scopus 로고
    • Aurora A contributes to p150(glued) phosphorylation and function during mitosis
    • Rome, P.; Montembault, E.; Franck, N.; Pascal, A.; Glover, D.M.; Giet, R. Aurora A contributes to p150(glued) phosphorylation and function during mitosis. J. Cell Biol. 2010, 189, 651-659.
    • (2010) J. Cell Biol. , vol.189 , pp. 651-659
    • Rome, P.1    Montembault, E.2    Franck, N.3    Pascal, A.4    Glover, D.M.5    Giet, R.6
  • 41
    • 0037157845 scopus 로고    scopus 로고
    • A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport
    • Vaughan, P.S.; Miura, P.; Henderson, M.; Byrne, B.; Vaughan, K.T. A role for regulated binding of p150(Glued) to microtubule plus ends in organelle transport. J. Cell Biol. 2002, 158, 305-319.
    • (2002) J. Cell Biol. , vol.158 , pp. 305-319
    • Vaughan, P.S.1    Miura, P.2    Henderson, M.3    Byrne, B.4    Vaughan, K.T.5
  • 42
    • 0033522642 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase II phosphorylates the epidermal growth factor receptor on multiple sites in the cytoplasmic tail and serine 744 within the kinase domain to regulate signal generation
    • 2+/calmodulin-dependent kinase II phosphorylates the epidermal growth factor receptor on multiple sites in the cytoplasmic tail and serine 744 within the kinase domain to regulate signal generation. J. Biol. Chem. 1999, 274, 16168-16173.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16168-16173
    • Feinmesser, R.L.1    Wicks, S.J.2    Taverner, C.J.3    Chantry, A.4
  • 44
    • 45349098064 scopus 로고    scopus 로고
    • A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes
    • Ha, J.; Lo, K.W.; Myers, K.R.; Carr, T.M.; Humsi, M.K.; Rasoul, B.A.; Segal, R.A.; Pfister, K.K. A neuron-specific cytoplasmic dynein isoform preferentially transports TrkB signaling endosomes. J. Cell Biol. 2008, 181, 1027-1039.
    • (2008) J. Cell Biol. , vol.181 , pp. 1027-1039
    • Ha, J.1    Lo, K.W.2    Myers, K.R.3    Carr, T.M.4    Humsi, M.K.5    Rasoul, B.A.6    Segal, R.A.7    Pfister, K.K.8
  • 46
    • 39149138988 scopus 로고    scopus 로고
    • Cargo transport: Molecular motors navigate a complex cytoskeleton
    • Ross, J.L.; Ali, M.Y.; Warshaw, D.M. Cargo transport: Molecular motors navigate a complex cytoskeleton. Curr. Opin. Cell Biol. 2008, 20, 41-47.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 41-47
    • Ross, J.L.1    Ali, M.Y.2    Warshaw, D.M.3
  • 47
    • 13844275312 scopus 로고    scopus 로고
    • Long-distance retrograde neurotrophic signaling
    • Howe, C.L.; Mobley, W.C. Long-distance retrograde neurotrophic signaling. Curr. Opin. Neurobiol. 2005, 15, 40-48.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 40-48
    • Howe, C.L.1    Mobley, W.C.2
  • 48
    • 0842333851 scopus 로고    scopus 로고
    • Dynein: An ancient motor protein involved in multiple modes of transport
    • Vallee, R.B.; Williams, J.C.; Varma, D.; Barnhart, L.E. Dynein: An ancient motor protein involved in multiple modes of transport. J. Neurobiol. 2004, 58, 189-200.
    • (2004) J. Neurobiol. , vol.58 , pp. 189-200
    • Vallee, R.B.1    Williams, J.C.2    Varma, D.3    Barnhart, L.E.4
  • 49
    • 33644507718 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin function and dysfunction in motor neurons
    • Levy, J.R.; Holzbaur, E.L. Cytoplasmic dynein/dynactin function and dysfunction in motor neurons. Int. J. Dev. Neurosci. 2006, 24, 103-111.
    • (2006) Int. J. Dev. Neurosci. , vol.24 , pp. 103-111
    • Levy, J.R.1    Holzbaur, E.L.2
  • 51
    • 33845905221 scopus 로고    scopus 로고
    • Dynein is required for receptor sorting and the morphogenesis of early endosomes
    • Driskell, O.J.; Mironov, A.; Allan, V.J.; Woodman, P.G. Dynein is required for receptor sorting and the morphogenesis of early endosomes. Nat. Cell Biol. 2007, 9, 113-120.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 113-120
    • Driskell, O.J.1    Mironov, A.2    Allan, V.J.3    Woodman, P.G.4
  • 52
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J.K.; Echeverri, C.J.; Nilsson, T.; Vallee, R.B. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 1997, 139, 469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 53
    • 0031770948 scopus 로고    scopus 로고
    • Cytoplasmic dynein intermediate-chain isoforms with different targeting properties created by tissue-specific alternative splicing
    • Nurminsky, D.I.; Nurminskaya, M.V.; Benevolenskaya, E.V.; Shevelyov, Y.Y.; Hartl, D.L.; Gvozdev, V.A. Cytoplasmic dynein intermediate-chain isoforms with different targeting properties created by tissue-specific alternative splicing. Mol. Cell Biol. 1998, 18, 6816-6825.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 6816-6825
    • Nurminsky, D.I.1    Nurminskaya, M.V.2    Benevolenskaya, E.V.3    Shevelyov, Y.Y.4    Hartl, D.L.5    Gvozdev, V.A.6
  • 54
    • 0034862996 scopus 로고    scopus 로고
    • Light chains of mammalian cytoplasmic dynein: Identification and characterization of a family of LC8 light chains
    • Wilson, M.J.; Salata, M.W.; Susalka, S.J.; Pfister, K.K. Light chains of mammalian cytoplasmic dynein: Identification and characterization of a family of LC8 light chains. Cell Motil. Cytoskeleton 2001, 49, 229-240.
    • (2001) Cell Motil. Cytoskeleton , vol.49 , pp. 229-240
    • Wilson, M.J.1    Salata, M.W.2    Susalka, S.J.3    Pfister, K.K.4
  • 55
    • 0343177223 scopus 로고    scopus 로고
    • A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and ERK1
    • Songyang, Z.; Lu, K.P.; Kwon, Y.T.; Tsai, L.H.; Filhol, O.; Cochet, C.; Brickey, D.A.; Soderling, T.R.; Bartleson, C.; Graves, D.J.; et al. A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and ERK1. Mol. Cell Biol. 1996, 16, 6486-6493.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6486-6493
    • Songyang, Z.1    Lu, K.P.2    Kwon, Y.T.3    Tsai, L.H.4    Filhol, O.5    Cochet, C.6    Brickey, D.A.7    Soderling, T.R.8    Bartleson, C.9    Graves, D.J.10
  • 56
    • 0031047830 scopus 로고    scopus 로고
    • Casein kinase II binds to and phosphorylates cytoplasmic dynein
    • Karki, S.; Tokito, M.K.; Holzbaur, E.L. Casein kinase II binds to and phosphorylates cytoplasmic dynein. J. Biol. Chem. 1997, 272, 5887-5891.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5887-5891
    • Karki, S.1    Tokito, M.K.2    Holzbaur, E.L.3
  • 60
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S.; Holzbaur, E.L. Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 1999, 11, 45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 62
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C.J. Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation. Cell 1995, 80, 179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 64
    • 20344379187 scopus 로고    scopus 로고
    • The MEK1 scaffolding protein MP1 regulates cell spreading by integrating PAK1 and Rho signals
    • Pullikuth, A.; McKinnon, E.; Schaeffer, H.J.; Catling, A.D. The MEK1 scaffolding protein MP1 regulates cell spreading by integrating PAK1 and Rho signals. Mol. Cell Biol. 2005, 25, 5119-5133.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 5119-5133
    • Pullikuth, A.1    McKinnon, E.2    Schaeffer, H.J.3    Catling, A.D.4
  • 67
    • 0032508538 scopus 로고    scopus 로고
    • MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade
    • Schaeffer, H.J.; Catling, A.D.; Eblen, S.T.; Collier, L.S.; Krauss, A.; Weber, M.J. MP1: A MEK binding partner that enhances enzymatic activation of the MAP kinase cascade. Science 1998, 281, 1668-1671.
    • (1998) Science , vol.281 , pp. 1668-1671
    • Schaeffer, H.J.1    Catling, A.D.2    Eblen, S.T.3    Collier, L.S.4    Krauss, A.5    Weber, M.J.6


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