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Volumn 11, Issue 2, 2010, Pages 103-112

PKC and the control of localized signal dynamics

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANOSINE TRIPHOSPHATASE; ISOENZYME; ISOPROTEIN; PROTEIN CDC42; PROTEIN KINASE; PROTEIN KINASE C; T LYMPHOCYTE RECEPTOR;

EID: 75149161903     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2847     Document Type: Review
Times cited : (363)

References (123)
  • 1
    • 46949084265 scopus 로고    scopus 로고
    • Defining the blueprint of the cancer genome
    • Velculescu, V. E. Defining the blueprint of the cancer genome. Carcinogenesis 29, 1087-1091 (2008).
    • (2008) Carcinogenesis , vol.29 , pp. 1087-1091
    • Velculescu, V.E.1
  • 3
    • 0014409136 scopus 로고
    • Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3', 5'-monophosphate
    • DeLange, R. J., Kemp, R. G., Riley, W. D., Cooper, R. A. & Krebs, E. G. Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3', 5'-monophosphate. J. Biol. Chem. 243, 2200-2208 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 2200-2208
    • Delange, R.J.1    Kemp, R.G.2    Riley, W.D.3    Cooper, R.A.4    Krebs, E.G.5
  • 4
    • 0035195491 scopus 로고    scopus 로고
    • The Ste5p scaffold
    • Elion, E. A. The Ste5p scaffold. J. Cell Sci. 114, 3967-3978 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3967-3978
    • Elion, E.A.1
  • 6
    • 0036769119 scopus 로고    scopus 로고
    • Regulation and targets of receptor tyrosine kinases
    • Pawson, T. Regulation and targets of receptor tyrosine kinases. Eur. J. Cancer 38, S3-S10 (2002).
    • (2002) Eur. J. Cancer , vol.38
    • Pawson, T.1
  • 7
    • 0035789886 scopus 로고    scopus 로고
    • PKA PKC and AKAP localization in and around the neuromuscular junction
    • Perkins, G. A. et al. PKA, PKC, and AKAP localization in and around the neuromuscular junction. BMC Neurosci. 2, 17 (2001)
    • (2001) BMC Neurosci. , vol.2 , pp. 17
    • Perkins, G.A.1
  • 8
    • 0036775910 scopus 로고    scopus 로고
    • Protein kinase C (PKC) isoforms in Drosophila
    • Shieh, B. h., Parker, L. & Popescu, D. Protein kinase C (PKC) isoforms in Drosophila. J. Biochem. 132, 523-527 (2002).
    • (2002) J. Biochem. , Issue.132 , pp. 523-527
    • Shieh, B.H.1    Parker, L.2    Popescu, D.3
  • 9
    • 0033458830 scopus 로고    scopus 로고
    • Targeting of, PKA, PKC and protein phosphatases to cellular microdomains
    • Sim, A. T. & Scott, J. D. Targeting of, PKA, PKC and protein phosphatases to cellular microdomains. Cell Calcium 26, 209-217 (1999).
    • (1999) Cell Calcium , vol.26 , pp. 209-217
    • Sim, A.T.1    Scott, J.D.2
  • 10
    • 0033119158 scopus 로고    scopus 로고
    • Pharmacologic modulation of protein kinase C isozymes: The role of RACKs and subcellular localisation
    • Csukai, M. & Mochly-Rosen, D. Pharmacologic modulation of protein kinase C isozymes: the role of RACKs and subcellular localisation. Pharmacol. Res. 39, 253-259 (1999).
    • (1999) Pharmacol. Res. , vol.39 , pp. 253-259
    • Csukai, M.1    Mochly-Rosen, D.2
  • 11
    • 0034057863 scopus 로고    scopus 로고
    • Protein kinase C binding partners
    • Jaken, S. & Parker, P. J. Protein kinase C binding partners. Bioessays 22, 245-254 (2000).
    • (2000) Bioessays , vol.22 , pp. 245-254
    • Jaken, S.1    Parker, P.J.2
  • 13
    • 0032104245 scopus 로고    scopus 로고
    • The extended protein kinase C superfamily
    • Mellor, h. & Parker, P. J. The extended protein kinase C superfamily. Biochem. J. 332, 281-292 (1998).
    • (1998) Biochem. J. , vol.332 , pp. 281-292
    • Mellor, H.1    Parker, P.J.2
  • 14
    • 36749045883 scopus 로고    scopus 로고
    • Functional PKC in vivo analysis using deficient mouse models
    • Leitges, M. Functional PKC in vivo analysis using deficient mouse models. Biochem. Soc. Trans. 35, 1018-1020 (2007).
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1018-1020
    • Leitges, M.1
  • 15
    • 0025198526 scopus 로고
    • Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation
    • Pears, C. J., Kour, G., house, C, Kemp, B. E. & Parker, P. J. Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation. Eur J. Biochem. 194, 89-94 (1990).
    • (1990) Eur J. Biochem. , Issue.194 , pp. 89-94
    • Pears, C.J.1    Kour, G.2    House, C.3    Kemp, B.E.4    Parker, P.J.5
  • 16
    • 0035818442 scopus 로고    scopus 로고
    • Membrane binding kinetics of protein kinase C (3II mediated by the C2 domain
    • Nalefski, E. A. & Newton, A. C. Membrane binding kinetics of protein kinase C (3II mediated by the C2 domain. Biochemistry 40, 13216-13229 (2001).
    • (2001) Biochemistry , vol.40 , pp. 13216-13229
    • Nalefski, E.A.1    Newton, A.C.2
  • 17
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea, E. & Meyer, T Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95, 307-318 (1998).
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 18
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionary conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki, A. et al. Atypical protein kinase C is involved in the evolutionary conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152, 1183-1196 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1
  • 19
    • 0032579489 scopus 로고    scopus 로고
    • Multiple interactions of PRK1 with RhoA. Functional assignment of the hr1 repeat motif
    • Flynn, P., Mellor, h., Palmer, R., Panayotou, G. & Parker, P. J. Multiple interactions of PRK1 with RhoA. Functional assignment of the hr1 repeat motif. J. Biol. Chem. 273, 2698-2705 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 2698-2705
    • Flynn, P.1    Mellor, H.2    Palmer, R.3    Panayotou, G.4    Parker, P.J.5
  • 21
    • 33744786565 scopus 로고    scopus 로고
    • The very C-terminus of PRK1 /PKN is essential for its activation by RhoA and downstream signaling
    • Lim, W. G. et al. The very C-terminus of PRK1 /PKN is essential for its activation by RhoA and downstream signaling. Cell Signal. 18, 1473-1481 (2006).
    • (2006) Cell Signal. , vol.18 , pp. 1473-1481
    • Lim, W.G.1
  • 22
    • 0034488768 scopus 로고    scopus 로고
    • Molecular associations and microdomains in antigen-presenting cell-T-cell interactions
    • Triantafilou, K., Triantafilou, M. & Fernandez, N. Molecular associations and microdomains in antigen-presenting cell-T-cell interactions. Crit. Rev. Immunol. 20, 359-373 (2000).
    • (2000) Crit. Rev. Immunol. , vol.20 , pp. 359-373
    • Triantafilou, K.1    Triantafilou, M.2    Fernandez, N.3
  • 23
    • 22244473678 scopus 로고    scopus 로고
    • Control of T helper 2 cell function and allergic airway inflammation by PKCC Proc
    • Martin, P. et al. Control of T helper 2 cell function and allergic airway inflammation by PKCC Proc. Natl Acad Sci. USA 102, 9866-9871 (2005).
    • (2005) Natl Acad Sci. USA , vol.102 , pp. 9866-9871
    • Martin, P.1
  • 24
    • 59049090061 scopus 로고    scopus 로고
    • Loss of PKC A/i impairs Th2 establishment and allergic airway inflammation in vivo
    • Yang, J. Q., Leitges, M., Duran, A., Diaz-Meco, M. T. & Moscat, J. Loss of PKC A/i impairs Th2 establishment and allergic airway inflammation in vivo. Proc. Natl Acad. Sci. USA 106, 1099-1104 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1099-1104
    • Yang, J.Q.1    Leitges, M.2    Duran, A.3    Diaz-Meco, M.T.4    Moscat, J.5
  • 25
    • 0027418818 scopus 로고
    • Molecular-cloning and characterization of pkc-8, a novel member of protein kinase c (pkc) gene family expressed predominantly in hematopoietic cells
    • Baier, G. et al. Molecular-cloning and characterization of pkc-8, a novel member of protein kinase c (pkc) gene family expressed predominantly in hematopoietic cells. J. Biol. Chem. 268, 4997-5004 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 4997-5004
    • Baier, G.1    Al, E.2
  • 26
    • 0026665459 scopus 로고
    • A new member of the protein kinase C family, nPKC theta, predominantly expressed in skeletal muscle
    • Osada, S. et al. A new member of the protein kinase C family, nPKC theta, predominantly expressed in skeletal muscle. Mol. Cell. Biol. 12, 3930-3938 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3930-3938
    • Osada, S.1    Al, E.2
  • 28
    • 3242790172 scopus 로고    scopus 로고
    • Protein kinase C 8 is critical for the development of in vivo T helper (Th)2 cell but not Th1 cell responses
    • Marsland, B. J., Soos, T. J., Spath, G., Littman, D. R. & Kopf, M. Protein kinase C 8 is critical for the development of in vivo T helper (Th)2 cell but not Th1 cell responses. J. Exp. Med. 200, 181-189 (2004).
    • (2004) J. Exp. Med. , vol.200 , pp. 181-189
    • Marsland, B.J.1    Soos, T.J.2    Spath, G.3    Littman, D.R.4    Kopf, M.5
  • 30
    • 41149167494 scopus 로고    scopus 로고
    • T-cell fate and function: PKC-8 and beyond
    • Marsland, B. J. & Kopf, M. T-cell fate and function: PKC-8 and beyond. Trends Immunol. 29, 179-185 (2008).
    • (2008) Trends Immunol. , vol.29 , pp. 179-185
    • Marsland, B.J.1    Kopf, M.2
  • 31
    • 0032973249 scopus 로고    scopus 로고
    • Interaction between B.7 and CD28 costimulatory molecules is essential for the activation of effector function mediating spontaneous tumour regression
    • Rao, K. L, Varalakshmi, C, Kumari, A. L. & Khar, A. Interaction between B.7 and CD28 costimulatory molecules is essential for the activation of effector function mediating spontaneous tumour regression. Scand. J. Immunol. 49, 633-640 (1999).
    • (1999) Scand. J. Immunol. , vol.49 , pp. 633-640
    • Rao, K.L.1    Varalakshmi, C.2    Kumari, A.L.3    Khar, A.4
  • 32
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks, C. R., Freiberg, B. A., Kupfer, h., Sciaky, N. & Kupfer, A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 395, 82-86 (1998).
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.R.1    Freiberg, B.A.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 33
    • 0037902559 scopus 로고    scopus 로고
    • Protein kinase C-8 (PKC8): It's all about location, location, location
    • Altman, A. & Villalba, M. Protein kinase C-8 (PKC8): it's all about location, location, location. Immunol. Rev 192, 53-63 (2003).
    • (2003) Immunol. Rev , vol.192 , pp. 53-63
    • Altman, A.1    Villalba, M.2
  • 34
    • 0036794399 scopus 로고    scopus 로고
    • Staging and resetting T cell activation in SMACs
    • Freiberg, B. A. et al. Staging and resetting T cell activation in SMACs. Nature Immunol. 3, 911-917 (2002).
    • (2002) Nature Immunol. , vol.3 , pp. 911-917
    • Freiberg, B.A.1
  • 35
    • 0742270964 scopus 로고    scopus 로고
    • Complex and dynamic redistribution of NF-KB signaling intermediates in response to T cell receptor stimulation
    • Schaefer, B. C, Kappler, J. W., Kupfer, A. & Marrack, P. Complex and dynamic redistribution of NF-KB signaling intermediates in response to T cell receptor stimulation. Proc. Natl Acad. Sci. USA 101, 1004-1009 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 1004-1009
    • Schaefer, B.C.1    Kappler, J.W.2    Kupfer, A.3    Marrack, P.4
  • 36
    • 28844500398 scopus 로고    scopus 로고
    • Phosphorylation of the CARMA1 linker controls NF-KB activation
    • Sommer, K. et al. Phosphorylation of the CARMA1 linker controls NF-KB activation. Immunity 23, 561-574 (2005).
    • (2005) Immunity , vol.23 , pp. 561-574
    • Sommer, K.1
  • 37
    • 0034602963 scopus 로고    scopus 로고
    • Regulation of protein kinase C8 function during T cell activation by Lck-mediated tyrosine phosphorylation
    • Liu, Y. et al. Regulation of protein kinase C8 function during T cell activation by Lck-mediated tyrosine phosphorylation. J. Biol. Chem. 275, 3603-3609 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3603-3609
    • Liu, Y.1    Al, E.2
  • 38
    • 27844439874 scopus 로고    scopus 로고
    • Critical role of novel Thr-219 autophosphorylation for the cellular function of PKC8 in T lymphocytes
    • Thuille, N. et al. Critical role of novel Thr-219 autophosphorylation for the cellular function of PKC8 in T lymphocytes. EMBO J. 24, 3869-3880 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3869-3880
    • Thuille, N.1
  • 39
    • 34250692040 scopus 로고    scopus 로고
    • Protein kinase C 8 (PKC 8): A key player in T cell life and death
    • hayashi, K. & Altman, A. Protein kinase C 8 (PKC 8): a key player in T cell life and death. Pharmacol. Res. 55, 537-544 (2007).
    • (2007) Pharmacol. Res. , vol.55 , pp. 537-544
    • Hayashi, K.1    Altman, A.2
  • 40
    • 38949197102 scopus 로고    scopus 로고
    • T-cell activation through immunological synapses and kinapses
    • Dustin, M. L. T-cell activation through immunological synapses and kinapses. Immunol. Rev. 221, 77-89 (2008).
    • (2008) Immunol. Rev. , vol.221 , pp. 77-89
    • Dustin, M.L.1
  • 41
    • 0025285657 scopus 로고
    • Crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia
    • Tepass, U., Theres, C. & Knust, E. crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia. Cell 61, 787-799 (1990).
    • (1990) Cell , vol.61 , pp. 787-799
    • Tepass, U.1    Theres, C.2    Knust, E.3
  • 42
    • 0032949091 scopus 로고    scopus 로고
    • PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos
    • hung, T. J. & Kemphues, K. J. PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos. Development 126, 127-135 (1999).
    • (1999) Development , vol.126 , pp. 127-135
    • Hung, T.J.1    Kemphues, K.J.2
  • 43
    • 0031674842 scopus 로고    scopus 로고
    • Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans
    • Tabuse, Y et al. Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans. Development 125, 3607-3614 (1998).
    • (1998) Development , vol.125 , pp. 3607-3614
    • Tabuse, Y.1
  • 44
    • 0029850113 scopus 로고    scopus 로고
    • Par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3
    • Watts, J. L. et al. par-6, a gene involved in the establishment of asymmetry in early C. elegans embryos, mediates the asymmetric localization of PAR-3. Development 122, 3133-3140 (1996).
    • (1996) Development , vol.122 , pp. 3133-3140
    • Watts, J.L.1
  • 45
    • 67449114979 scopus 로고    scopus 로고
    • Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells
    • horikoshi, Y et al. Interaction between PAR-3 and the aPKC-PAR-6 complex is indispensable for apical domain development of epithelial cells. J. Cell Sci. 122, 1595-1606 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1595-1606
    • Horikoshi, Y.1
  • 46
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty, G., Petersen, C, Gao, L. & Macara, I. G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nature Cell Biol. 2, 531-539 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    MacAra, I.G.4
  • 47
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi, Y. et al. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143, 95-106 (1998).
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1
  • 48
    • 0024284814 scopus 로고
    • Identification of genes required for cytoplasmic localization in early C. elegans embryos
    • Kemphues, K. J., Priess, J. R., Morton, D. G. & Cheng, N. S. Identification of genes required for cytoplasmic localization in early C. elegans embryos. Cell 52, 311-320 (1988).
    • (1988) Cell , vol.52 , pp. 311-320
    • Kemphues, K.J.1    Priess, J.R.2    Morton, D.G.3    Cheng, N.S.4
  • 49
    • 0034640089 scopus 로고    scopus 로고
    • PARsing embryonic polarity
    • Kemphues, K. PARsing embryonic polarity. Cell 101, 345-348 (2000).
    • (2000) Cell , vol.101 , pp. 345-348
    • Kemphues, K.1
  • 51
    • 33747886310 scopus 로고    scopus 로고
    • Cell signaling and function organized by PB1 domain interactions
    • Moscat, J., Diaz-Meco, M. T, Albert, A. & Campuzano, S. Cell signaling and function organized by PB1 domain interactions. Mol. Cell 23, 631-640 (2006).
    • (2006) Mol. Cell , vol.23 , pp. 631-640
    • Moscat, J.1    Diaz-Meco, M.T.2    Albert, A.3    Campuzano, S.4
  • 52
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac 1 and aPKC signalling and cell polarity
    • Lin, D. et al. A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac 1 and aPKC signalling and cell polarity. Nature Cell Biol. 2, 540-547 (2000).
    • (2000) Nature Cell Biol. , vol.2 , pp. 540-547
    • Lin, D.1
  • 53
    • 0034874862 scopus 로고    scopus 로고
    • PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex
    • Yamanaka, T. et al. PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex. Genes Cells 6, 721-731 (2001).
    • (2001) Genes Cells , vol.6 , pp. 721-731
    • Yamanaka, T.1
  • 54
    • 0037228253 scopus 로고    scopus 로고
    • Integrated activity of PDZ protein complexes regulates epithelial polarity
    • Bilder, D., Schober, M. & Perrimon, N. Integrated activity of PDZ protein complexes regulates epithelial polarity. Nature Cell Biol. 5, 53-58 (2003).
    • (2003) Nature Cell Biol. , vol.5 , pp. 53-58
    • Bilder, D.1    Schober, M.2    Perrimon, N.3
  • 55
    • 0037096161 scopus 로고    scopus 로고
    • Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation
    • hirose, T. et al. Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation. J. Cell Sci. 115, 2485-2495 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 2485-2495
    • Hirose, T.1
  • 56
    • 0037458707 scopus 로고    scopus 로고
    • Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse
    • Takekuni, K. et al. Direct binding of cell polarity protein PAR-3 to cell-cell adhesion molecule nectin at neuroepithelial cells of developing mouse. J. Biol. Chem. 278, 5497-5500 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 5497-5500
    • Takekuni, K.1    Al, E.2
  • 57
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • Ebnet, K. et al. The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). EMBO J. 20, 3738-3748 (2001).
    • (2001) EMBO J. , vol.20 , pp. 3738-3748
    • Ebnet, K.1
  • 58
    • 0042232080 scopus 로고    scopus 로고
    • Self-association of PAR-3-mediated by the conserved N-terminal domain contributes to the development of epithelial tight junctions
    • Mizuno, K. et al. Self-association of PAR-3-mediated by the conserved N-terminal domain contributes to the development of epithelial tight junctions. J. Biol. Chem. 278, 31240-31250 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 31240-31250
    • Mizuno, K.1    Al, E.2
  • 59
    • 0038032917 scopus 로고    scopus 로고
    • Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity
    • Yamanaka, T. et al. Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Curr. Biol. 13, 734-743 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 734-743
    • Yamanaka, T.1    Al, E.2
  • 60
    • 0037456795 scopus 로고    scopus 로고
    • The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl
    • Betschinger, J., Mechtler, K. & Knoblich, J. A. The Par complex directs asymmetric cell division by phosphorylating the cytoskeletal protein Lgl. Nature 422, 326-330 (2003).
    • (2003) Nature , vol.422 , pp. 326-330
    • Betschinger, J.1    Mechtler, K.2    Knoblich, J.A.3
  • 61
    • 33745217610 scopus 로고    scopus 로고
    • Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity
    • Yamanaka, T. et al. Lgl mediates apical domain disassembly by suppressing the PAR-3-aPKC-PAR-6 complex to orient apical membrane polarity. J. Cell Sci. 119, 2107-2118 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 2107-2118
    • Yamanaka, T.1
  • 62
    • 13444267951 scopus 로고    scopus 로고
    • Phosphorylation-induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae
    • Betschinger, J., Eisenhaber, F & Knoblich, J. A. Phosphorylation- induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae. Curr. Biol. 15, 276-282 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 276-282
    • Betschinger, J.1    Eisenhaber, F.2    Knoblich, J.A.3
  • 63
    • 2942626082 scopus 로고    scopus 로고
    • Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis
    • hutterer, A., Betschinger, J., Petronczki, M. & Knoblich, J. A. Sequential roles of Cdc42, Par-6, aPKC, and Lgl in the establishment of epithelial polarity during Drosophila embryogenesis. Dev Cell 6, 845-854 (2004).
    • (2004) Dev Cell , vol.6 , pp. 845-854
    • Hutterer, A.1    Betschinger, J.2    Petronczki, M.3    Knoblich, J.A.4
  • 64
    • 34547934017 scopus 로고    scopus 로고
    • P32 is a novel mammalian Lgl binding protein that enhances the activity of protein kinase Ci; And regulates cell polarity
    • Bialucha, C. U., Ferber, E. C, Pichaud, F, Peak-Chew, S. Y. & Fujita, Y. p32 is a novel mammalian Lgl binding protein that enhances the activity of protein kinase Ci; and regulates cell polarity. J. Cell Biol. 178, 575-581 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 575-581
    • Bialucha, C.U.1    Ferber, E.C.2    Pichaud, F.3    Peak-Chew, S.Y.4    Fujita, Y.5
  • 65
    • 33748923940 scopus 로고    scopus 로고
    • Scribble associates with two polarity proteins, Lgl2 and Vangl2, via distinct molecular domains
    • Kallay, L. M., McNickle, A., Brennwald, P. J., hubbard, A. L. & Braiterman, L. T Scribble associates with two polarity proteins, Lgl2 and Vangl2, via distinct molecular domains. J. Cell. Biochem. 99, 647-664 (2006).
    • (2006) J. Cell. Biochem. , Issue.99 , pp. 647-664
    • Kallay, L.M.1    McNickle, A.2    Brennwald, P.J.3    Hubbard, A.L.4    Braiterman, L.T.5
  • 66
    • 0034628471 scopus 로고    scopus 로고
    • Localization of apical epithelial determinants by the basolateral PDZ protein Scribble
    • Bilder, D. & Perrimon, N. Localization of apical epithelial determinants by the basolateral PDZ protein Scribble. Nature 403, 676-680 (2000).
    • (2000) Nature , vol.403 , pp. 676-680
    • Bilder, D.1    Perrimon, N.2
  • 67
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • Musch, A. et al. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol. Biol. Cell 13, 158-168 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 158-168
    • Musch, A.1    Al, E.2
  • 68
    • 24644490121 scopus 로고    scopus 로고
    • Atypical PKCi contributes to poor prognosis through loss of apical-basal polarity and cyclin e overexpression in ovarian cancer
    • Eder, A. M. et al. Atypical PKCi contributes to poor prognosis through loss of apical-basal polarity and cyclin E overexpression in ovarian cancer. Proc. Natl Acad. Sci. USA 102, 12519-12524 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12519-12524
    • Eder, A.M.1    Al, E.2
  • 69
    • 34250722131 scopus 로고    scopus 로고
    • Protein kinase C i: Human oncogene, prognostic marker and therapeutic target
    • Fields, A. P. & Regala, R. P. Protein kinase C i: human oncogene, prognostic marker and therapeutic target. Pharmacol. Res. 55, 487-497 (2007).
    • (2007) Pharmacol. Res. , vol.55 , pp. 487-497
    • Fields, A.P.1    Regala, R.P.2
  • 70
    • 44449152002 scopus 로고    scopus 로고
    • The overexpression and altered localization of the atypical protein kinase C X/i in breast cancer correlates with the pathologic type of these tumors
    • Kojima, Y. et al. The overexpression and altered localization of the atypical protein kinase C X/i in breast cancer correlates with the pathologic type of these tumors. Hum. Pathol. 39, 824-831 (2008).
    • (2008) Hum. Pathol. , vol.39 , pp. 824-831
    • Kojima, Y.1    Al, E.2
  • 71
    • 24744469442 scopus 로고    scopus 로고
    • Atypical protein kinase Ci plays a critical role in human lung cancer cell growth and tumorigenicity
    • Regala, R. P. et al. Atypical protein kinase Ci plays a critical role in human lung cancer cell growth and tumorigenicity. J. Biol. Chem. 280, 31109-31115 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 31109-31115
    • Regala, R.P.1    Al, E.2
  • 72
    • 54249140140 scopus 로고    scopus 로고
    • The polarity protein Par6 induces cell proliferation and is overexpressed in breast cancer
    • Nolan, M. E. et al. The polarity protein Par6 induces cell proliferation and is overexpressed in breast cancer. Cancer Res. 68, 8201-8209 (2008).
    • (2008) Cancer Res. , vol.68 , pp. 8201-8209
    • Nolan, M.E.1
  • 73
    • 27844539756 scopus 로고    scopus 로고
    • Protein kinase C and the regulation of the actin cytoskeleton
    • Larsson, C. Protein kinase C and the regulation of the actin cytoskeleton. Cell Signal. 18, 276-284 (2006).
    • (2006) Cell Signal. , vol.18 , pp. 276-284
    • Larsson, C.1
  • 74
    • 1642545636 scopus 로고    scopus 로고
    • Syndecan-4 regulates localization, activity and stability of protein kinase C-a
    • Keum, E. et al. Syndecan-4 regulates localization, activity and stability of protein kinase C-a. Biochem. J. 378, 1007-1014 (2004).
    • (2004) Biochem. J. , vol.378 , pp. 1007-1014
    • Keum, E.1
  • 75
    • 75149141179 scopus 로고    scopus 로고
    • PKCa regulates p1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng, T. et al. PKCa regulates p1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18, 3309-3923 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3309-3923
    • Ng, T.1
  • 76
    • 0037099313 scopus 로고    scopus 로고
    • PKCs controls the traffic of (31 integrins in motile cells
    • Ivaska, J., Whelan, R. D., Watson, R. & Parker, P. J. PKCs controls the traffic of (31 integrins in motile cells. EMBO J. 21, 3608-3619 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3608-3619
    • Ivaska, J.1    Whelan, R.D.2    Watson, R.3    Parker, P.J.4
  • 77
    • 0036303142 scopus 로고    scopus 로고
    • A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility
    • Legg, J. W., Lewis, C. A., Parsons, M., Ng, T & Isacke, C. M. A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility. Nature Cell Biol. 4, 399-407 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 399-407
    • Legg, J.W.1    Lewis, C.A.2    Parsons, M.3    Ng, T.4    Isacke, C.M.5
  • 78
    • 0024411035 scopus 로고
    • Lymphoma protein kinase C is associated with the transmembrane glycoprotein, GP85, and may function in GP85-ankyrin binding
    • Kalomiris, E. L. & Bourguignon, L. Y. Lymphoma protein kinase C is associated with the transmembrane glycoprotein, GP85, and may function in GP85-ankyrin binding. J. Biol. Chem. 264, 8113-8119 (1989)
    • (1989) J. Biol. Chem. , vol.264 , pp. 8113-8119
    • Kalomiris, E.L.1    Bourguignon, L.Y.2
  • 79
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • hood, J. D. & Cheresh, D. A. Role of integrins in cell invasion and migration. Nature Rev. Cancer 2, 91-100 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 81
    • 33847260150 scopus 로고    scopus 로고
    • Tyrosine kinase mutations in human cancer
    • Lengyel, E., Sawada, K. & Salgia, R. Tyrosine kinase mutations in human cancer. Curr. Mol. Med. 7, 77-84 (2007).
    • (2007) Curr. Mol. Med. , vol.7 , pp. 77-84
    • Lengyel, E.1    Sawada, K.2    Salgia, R.3
  • 82
    • 0038724909 scopus 로고    scopus 로고
    • C-Met: Structure functions and potential for therapeutic inhibition
    • Ma, P. C, Maulik, G., Christensen, J. & Salgia, R. c-Met: structure, functions and potential for therapeutic inhibition. Cancer Metastasis Rev. 22, 309-325 (2003).
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 309-325
    • Ma, P.C.1    Maulik, G.2    Christensen, J.3    Salgia, R.4
  • 83
    • 0036551486 scopus 로고    scopus 로고
    • Scatter-factor and semaphorin receptors: Cell signalling for invasive growth
    • Trusolino, L. & Comoglio, P. M. Scatter-factor and semaphorin receptors: cell signalling for invasive growth. Nature Rev. Cancer 2, 289-300 (2002).
    • (2002) Nature Rev. Cancer , vol.2 , pp. 289-300
    • Trusolino, L.1    Comoglio, P.M.2
  • 84
    • 0043208954 scopus 로고    scopus 로고
    • Protein kinase C controls microtubule-based traffic but not proteasomal degradation of c-Met
    • Kermorgant, S., Zicha, D. & Parker, P. J. Protein kinase C controls microtubule-based traffic but not proteasomal degradation of c-Met. J. Biol. Chem. 278, 28921-28929 (2003)
    • (2003) J. Biol. Chem. , vol.278 , pp. 28921-28929
    • Kermorgant, S.1    Zicha, D.2    Parker, P.J.3
  • 86
    • 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 274, 2086-2089 (1996).
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 87
    • 0032548865 scopus 로고    scopus 로고
    • Insulin-like growth factor-I receptor internalization regulates signaling via the Shc/mitogen-activated protein kinase pathway, but not the insulin receptor substrate-1 pathway
    • Chow, J. C, Condorelli, G. & Smith, R. J. Insulin-like growth factor-I receptor internalization regulates signaling via the Shc/mitogen-activated protein kinase pathway, but not the insulin receptor substrate-1 pathway. J. Biol. Chem. 273, 4672-4680 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4672-4680
    • Chow, J.C.1    Condorelli, G.2    Smith, R.J.3
  • 88
    • 0034255428 scopus 로고    scopus 로고
    • Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation
    • Zhang, Y, Moheban, D. B., Conway, B. R., Bhattacharyya, A. & Segal, R. A. Cell surface Trk receptors mediate NGF-induced survival while internalized receptors regulate NGF-induced differentiation. J. Neurosci. 20, 5671-5678 (2000)
    • (2000) J. Neurosci. , vol.20 , pp. 5671-5678
    • Zhang, Y.1    Moheban, D.B.2    Conway, B.R.3    Bhattacharyya, A.4    Segal, R.A.5
  • 89
    • 0035819073 scopus 로고    scopus 로고
    • NGF signaling from clathrin-coated vesicles: Evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway
    • howe, C. L, Valletta, J. S., Rusnak, A. S. & Mobley, W. C. NGF signaling from clathrin-coated vesicles: evidence that signaling endosomes serve as a platform for the Ras-MAPK pathway. Neuron 32, 801-814 (2001).
    • (2001) Neuron , vol.32 , pp. 801-814
    • Howe, C.L.1    Valletta, J.S.2    Rusnak, A.S.3    Mobley, W.C.4
  • 90
    • 0037144841 scopus 로고    scopus 로고
    • TGF (3 receptor internalization into EEA1-enriched early endosomes: Role in signaling to Smad2
    • Hayes, S., Chawla, A. & Corvera, S. TGF (3 receptor internalization into EEA1-enriched early endosomes: role in signaling to Smad2. J. Cell Biol. 158 1239-1249 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 1239-1249
    • Hayes, S.1    Chawla, A.2    Corvera, S.3
  • 91
    • 6344248651 scopus 로고    scopus 로고
    • PKC controls hGF-dependent c-Met traffic, signalling and cell migration
    • Kermorgant, S., Zicha, D. & Parker, P. J. PKC controls hGF-dependent c-Met traffic, signalling and cell migration. EMBO J. 23, 3721-3734 (2004)
    • (2004) EMBO J. , vol.23 , pp. 3721-3734
    • Kermorgant, S.1    Zicha, D.2    Parker, P.J.3
  • 92
    • 2942752110 scopus 로고    scopus 로고
    • Bi-directional regulation of Ser-985 phosphorylation of c-met via protein kinase C and protein phosphatase 2A involves c-Met activation and cellular responsiveness to hepatocyte growth factor
    • hashigasako, A., Machide, M., Nakamura, T, Matsumoto, K. & Nakamura, T Bi-directional regulation of Ser-985 phosphorylation of c-met via protein kinase C and protein phosphatase 2A involves c-Met activation and cellular responsiveness to hepatocyte growth factor. J. Biol. Chem. 279, 26445-26452 (2004).
    • (2004) J. Biol. Chem. , Issue.279 , pp. 26445-26452
    • Hashigasako, A.1    MacHide, M.2    Nakamura, T.3    Matsumoto, K.4    Nakamura, T.5
  • 94
    • 33846967126 scopus 로고    scopus 로고
    • Regulation of membrane trafficking and endocytosis by protein kinase C: Emerging role of the pericentrion, a novel protein kinase C-dependent subset of recycling endosomes
    • DOI 10.1007/s00018-006-6363-5
    • Alvi, F, Idkowiak-Baldys, J., Baldys, A., Raymond, J. R. & hannun, Y A. Regulation of membrane trafficking and endocytosis by protein kinase C: emerging role of the pericentrion, a novel protein kinase C-dependent subset of recycling endosomes. Cell. Mol. Life Sci. 64, 263-270 (2007). (Pubitemid 46440202)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.3 , pp. 263-270
    • Alvi, F.1    Idkowiak-Baldys, J.2    Baldys, A.3    Raymond, J.R.4    Hannun, Y.A.5
  • 95
    • 51649130231 scopus 로고    scopus 로고
    • Receptor trafficking controls weak signal delivery: A strategy used by c-Met for STAT3 nuclear accumulation
    • Kermorgant, S. & Parker, P. J. Receptor trafficking controls weak signal delivery: a strategy used by c-Met for STAT3 nuclear accumulation. J. Cell Biol. 182, 855-863 (2008).
    • (2008) J. Cell Biol. , vol.182 , pp. 855-863
    • Kermorgant, S.1    Parker, P.J.2
  • 96
    • 34247168703 scopus 로고    scopus 로고
    • Similar requirements for CDC-42 and the PAR-3/ PAR-6/PKC-3 complex in diverse cell types
    • Welchman, D. P., Mathies, L. D. & Ahringer, J. Similar requirements for CDC-42 and the PAR-3/ PAR-6/PKC-3 complex in diverse cell types. Dev Biol. 305, 347-357 (2007)
    • (2007) Dev Biol. , vol.305 , pp. 347-357
    • Welchman, D.P.1    Mathies, L.D.2    Ahringer, J.3
  • 97
    • 33745649658 scopus 로고    scopus 로고
    • XGAP, an ArfGAP, is required for polarized localization of PAR proteins and cell polarity in Xenopus gastrulation
    • hyodo-Miura, J. et al. XGAP, an ArfGAP, is required for polarized localization of PAR proteins and cell polarity in Xenopus gastrulation. Dev. Cell 11, 69-79 (2006).
    • (2006) Dev. Cell , vol.11 , pp. 69-79
    • Hyodo-Miura, J.1
  • 98
    • 9444269877 scopus 로고    scopus 로고
    • Requirement for Par-6 and Bazooka in Drosophila border cell migration
    • Pinheiro, E. M. & Montell, D. J. Requirement for Par-6 and Bazooka in Drosophila border cell migration. Development 131, 5243-5251 (2004).
    • (2004) Development , vol.131 , pp. 5243-5251
    • Pinheiro, E.M.1    Montell, D.J.2
  • 100
    • 30644463689 scopus 로고    scopus 로고
    • RalB mobilizes the exocyst to drive cell migration
    • Rosse, C. et al. RalB mobilizes the exocyst to drive cell migration. Mol. Cell. Biol. 26, 727-734 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 727-734
    • Rosse, C.1    Al, E.2
  • 101
    • 21644460380 scopus 로고    scopus 로고
    • Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways
    • Cau, J. & hall, A. Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways. J. Cell Sci. 118, 2579-2587 (2005).
    • (2005) J. Cell Sci. , vol.118 , pp. 2579-2587
    • Cau, J.1    Hall, A.2
  • 102
    • 34547604466 scopus 로고    scopus 로고
    • Cdc42 and noncanonical Wnt signal transduction pathways cooperate to promote cell polarity
    • Schlessinger, K., McManus, E. J. & hall, A. Cdc42 and noncanonical Wnt signal transduction pathways cooperate to promote cell polarity. J. Cell Biol. 178, 355-361 (2007).
    • (2007) J. Cell Biol. , vol.178 , pp. 355-361
    • Schlessinger, K.1    McManus, E.J.2    Hall, A.3
  • 103
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCC
    • Etienne-Manneville, S. & hall, A. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCC Cell 106, 489-498 (2001).
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 104
    • 0037434790 scopus 로고    scopus 로고
    • Cdc42 regulates GSK-3(3 and adenomatous polyposis coli to control cell polarity
    • Etienne-Manneville, S. & hall, A. Cdc42 regulates GSK-3(3 and adenomatous polyposis coli to control cell polarity. Nature 421, 753-756 (2003).
    • (2003) Nature , vol.421 , pp. 753-756
    • Etienne-Manneville, S.1    Hall, A.2
  • 105
    • 24944577909 scopus 로고    scopus 로고
    • Cdc42 and Par6-PKCi; Regulate the spatially localized association of Dlg 1 and APC to control cell polarization
    • Etienne-Manneville, S., Manneville, J. B., Nicholls, S., Ferenczi, M. A. & hall, A. Cdc42 and Par6-PKCi; regulate the spatially localized association of Dlg 1 and APC to control cell polarization. J. Cell Biol. 170, 895-901 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 895-901
    • Etienne-Manneville, S.1    Manneville, J.B.2    Nicholls, S.3    Ferenczi, M.A.4    Hall, A.5
  • 106
    • 0037307441 scopus 로고    scopus 로고
    • Fluorescence imaging of signaling networks
    • Meyer, T. & Teruel, M. N. Fluorescence imaging of signaling networks. Trends Cell Biol. 13, 101-106 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 101-106
    • Meyer, T.1    Teruel, M.N.2
  • 107
    • 0033605542 scopus 로고    scopus 로고
    • Imaging protein kinase Ca activation in cells
    • Ng, T et al. Imaging protein kinase Ca activation in cells. Science 283, 2085-2089 (1999).
    • (1999) Science , vol.283 , pp. 2085-2089
    • Ng, T.1
  • 108
    • 33750072605 scopus 로고    scopus 로고
    • Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling
    • Gallegos, L. L, Kunkel, M. T. & Newton, A. C. Targeting protein kinase C activity reporter to discrete intracellular regions reveals spatiotemporal differences in agonist-dependent signaling. J. Biol. Chem. 281, 30947-30956 (2006)
    • (2006) J. Biol. Chem. , vol.281 , pp. 30947-30956
    • Gallegos, L.L.1    Kunkel, M.T.2    Newton, A.C.3
  • 109
    • 0029737867 scopus 로고    scopus 로고
    • Dimeric ligands define a role for transcriptional activation domains in reinitiation
    • ho, S. N., Biggar, S. R., Spencer, D. M., Schreiber, S. L. & Crabtree, G. R. Dimeric ligands define a role for transcriptional activation domains in reinitiation. Nature 382, 822-826 (1996).
    • (1996) Nature , vol.382 , pp. 822-826
    • Ho, S.N.1    Biggar, S.R.2    Spencer, D.M.3    Schreiber, S.L.4    Crabtree, G.R.5
  • 110
    • 33750323504 scopus 로고    scopus 로고
    • Compartmental signal modulation: Endosomal phosphatidylinositol 3-phosphate controls endosome morphology and selective cargo sorting
    • Fili, N., Calleja, V., Woscholski, R., Parker, P. J. & Larijani, B. Compartmental signal modulation: endosomal phosphatidylinositol 3-phosphate controls endosome morphology and selective cargo sorting. Proc. Natl Acad. Sci. USA 103, 15473-15478 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15473-15478
    • Fili, N.1    Calleja, V.2    Woscholski, R.3    Parker, P.J.4    Larijani, B.5
  • 111
    • 33750730911 scopus 로고    scopus 로고
    • Rapidly inducible changes in phosphatidylinositol 4 5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells
    • Varnai, P., Thyagarajan, B., Rohacs, T & Balla, T Rapidly inducible changes in phosphatidylinositol 4, 5-bisphosphate levels influence multiple regulatory functions of the lipid in intact living cells. J. Cell Biol. 175, 377-382 (2006).
    • (2006) J. Cell Biol. , vol.175 , pp. 377-382
    • Varnai, P.1    Thyagarajan, B.2    Rohacs, T.3    Balla, T.4
  • 112
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh, D. B., Ziegler, W & Parker, P. J. Multiple pathways control protein kinase C phosphorylation. EMBO J. 19, 496-503 (2000).
    • (2000) EMBO J. , vol.19 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 113
    • 0037200043 scopus 로고    scopus 로고
    • The turn motif is a phosphorylation switch that regulates the binding of hsp70 to protein kinase
    • Gao, T & Newton, A. C. The turn motif is a phosphorylation switch that regulates the binding of hsp70 to protein kinase, C. J. Biol. Chem. 277, 31585-31592 (2002).
    • (2002) C. J. Biol. Chem. , vol.277 , pp. 31585-31592
    • Gao, T.1    Newton, A.C.2
  • 114
    • 47049109143 scopus 로고    scopus 로고
    • PKC a protein but not kinase activity is critical for glioma cell proliferation and survival
    • Cameron, A. J., Procyk, K. J., Leitges, M. & Parker, P. J. PKC a protein but not kinase activity is critical for glioma cell proliferation and survival. Int. J. Cancer 123, 769-779 (2008).
    • (2008) Int. J. Cancer , vol.123 , pp. 769-779
    • Cameron, A.J.1    Procyk, K.J.2    Leitges, M.3    Parker, P.J.4
  • 115
    • 0032563936 scopus 로고    scopus 로고
    • Regulation of protein kinase C t by PI 3-kinase and PDK-1
    • Chou, M. M. et al. Regulation of protein kinase C t by PI 3-kinase and PDK-1. Curr. Biol. 8, 1069-1077 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1069-1077
    • Chou, M.M.1    Al, E.2
  • 116
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1
    • Le Good, J. A. et al. Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1. Science 281, 2042-2045 (1998).
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, J.A.1
  • 118
    • 47949125486 scopus 로고    scopus 로고
    • The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase
    • Facchinetti, V. et al. The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase, C. EMBO J. 27, 1932-1943 (2008).
    • (2008) C. EMBO J. , Issue.27 , pp. 1932-1943
    • Facchinetti, V.1    Al, E.2
  • 119
    • 47949104258 scopus 로고    scopus 로고
    • Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling
    • Ikenoue, T., Inoki, K., Yang, Q., Zhou, X. & Guan, K. L. Essential function of TORC2 in PKC and Akt turn motif phosphorylation, maturation and signalling. EMBO J. 27, 1919-1931 (2008).
    • (2008) EMBO J. , vol.27 , pp. 1919-1931
    • Ikenoue, T.1    Inoki, K.2    Yang, Q.3    Zhou, X.4    Guan, K.L.5
  • 120
    • 33751570046 scopus 로고    scopus 로고
    • Structure of the catalytic domain of human protein kinase C p II complexed with a bisindolylmaleimide inhibitor
    • Grodsky, N. et al. Structure of the catalytic domain of human protein kinase C p II complexed with a bisindolylmaleimide inhibitor. Biochemistry 45, 13970-13981 (2006).
    • (2006) Biochemistry , vol.45 , pp. 13970-13981
    • Grodsky, N.1    Al, E.2
  • 121
    • 0034927336 scopus 로고    scopus 로고
    • Regulation of Phosphoinositide-specific Phospholipase
    • Rhee, S. G. Regulation of phosphoinositide-specific phospholipase, C. Annu. Rev. Biochem. 70, 281-312 (2001).
    • (2001) C. Annu. Rev. Biochem. , vol.70 , pp. 281-312
    • Rhee, S.G.1
  • 122
    • 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. Nature Rev. Mol. Cell Biol. 9, 690-701 (2008).
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 123
    • 0029996517 scopus 로고    scopus 로고
    • The role of the unique motifs in the amino-terminal region of PKN on its enzymatic activity
    • Kitagawa, M., Shibata, h., Toshimori, M., Mukai, h. & Ono, Y The role of the unique motifs in the amino-terminal region of PKN on its enzymatic activity. Biochem. Biophys. Res. Commun. 220, 963-968 (1996).
    • (1996) Biochem. Biophys. Res. Commun. , Issue.220 , pp. 963-968
    • Kitagawa, M.1    Shibata, H.2    Toshimori, M.3    Mukai, H.4    Ono, Y.5


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