메뉴 건너뛰기




Volumn 143, Issue 1, 1998, Pages 95-106

An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3

Author keywords

ASIP; Atypical PKC; Cell polarity; Par; Tight junction

Indexed keywords

PROTEIN KINASE C;

EID: 0032487494     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.143.1.95     Document Type: Article
Times cited : (449)

References (73)
  • 1
    • 0028298476 scopus 로고
    • A new member of the third class in the protein kinase C family, PKCλ, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells
    • Akimoto, K., K. Mizuno, S. Osada, S. Hirai, S. Tanuma, K. Suzuki, and S. Ohno. 1994. A new member of the third class in the protein kinase C family, PKCλ, expressed dominantly in an undifferentiated mouse embryonal carcinoma cell line and also in many tissues and cells. J. Biol. Chem. 269:12677-12683.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12677-12683
    • Akimoto, K.1    Mizuno, K.2    Osada, S.3    Hirai, S.4    Tanuma, S.5    Suzuki, K.6    Ohno, S.7
  • 4
    • 0031952083 scopus 로고    scopus 로고
    • Tight junctions
    • Balda, M.S., and K. Matter. 1998. Tight junctions. J. Cell Sci. 111:541-547.
    • (1998) J. Cell Sci. , vol.111 , pp. 541-547
    • Balda, M.S.1    Matter, K.2
  • 5
    • 0030812546 scopus 로고    scopus 로고
    • Evidence for involvement of protein kinase C (PKC)-ζ and noninvolvement of diacylglycerol-sensitive PKCs in insulin-stimulated glucose transport in L6 myotubes
    • Bandyopadhyay, G., M.L. Standaert, L. Galloway, J. Moscat, and R.V. Farese. 1997. Evidence for involvement of protein kinase C (PKC)-ζ and noninvolvement of diacylglycerol-sensitive PKCs in insulin-stimulated glucose transport in L6 myotubes. Endocrinology. 138:4721-4731.
    • (1997) Endocrinology , vol.138 , pp. 4721-4731
    • Bandyopadhyay, G.1    Standaert, M.L.2    Galloway, L.3    Moscat, J.4    Farese, R.V.5
  • 8
    • 0031213571 scopus 로고    scopus 로고
    • Mammalian homologues of C. elegans PAR-1 are asymmetrically localized in epithelial cells and may influence their polarity
    • Böhm. H., V. Brinkmann, M. Drab, A. Henske, and T.V. Kurzchalia. 1997. Mammalian homologues of C. elegans PAR-1 are asymmetrically localized in epithelial cells and may influence their polarity. Curr. Biol. 7:603-606.
    • (1997) Curr. Biol. , vol.7 , pp. 603-606
    • Böhm, H.1    Brinkmann, V.2    Drab, M.3    Henske, A.4    Kurzchalia, T.V.5
  • 9
    • 0030780536 scopus 로고    scopus 로고
    • The maternal par genes and the segregation of cell fate specification activities in early Caenorhabditis elegans embryos
    • Bowerman, B., M.K. Ingram, and C.P. Hunter. 1997. The maternal par genes and the segregation of cell fate specification activities in early Caenorhabditis elegans embryos. Development. 124:3815-3826.
    • (1997) Development , vol.124 , pp. 3815-3826
    • Bowerman, B.1    Ingram, M.K.2    Hunter, C.P.3
  • 11
    • 33751339795 scopus 로고    scopus 로고
    • Membrane polarity in epithelial cells: Protein sorting and establishment of polarized domains
    • Caplan, M.J. 1997. Membrane polarity in epithelial cells: protein sorting and establishment of polarized domains. Am. J. Physiol. 272:F425-F429.
    • (1997) Am. J. Physiol. , vol.272
    • Caplan, M.J.1
  • 12
    • 0029122307 scopus 로고
    • Phosphorylation of the light junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells
    • Citi, S., and N. Denisenko. 1995. Phosphorylation of the light junction protein cingulin and the effects of protein kinase inhibitors and activators in MDCK epithelial cells. J. Cell Sci. 108:2917-2926.
    • (1995) J. Cell Sci. , vol.108 , pp. 2917-2926
    • Citi, S.1    Denisenko, N.2
  • 13
    • 0024291701 scopus 로고
    • Cingulin, a new peripheral component of tight junctions
    • Citi, S., H. Sabanay, R. Jakes, B. Geiger, and J. Kendrick-Jones. 1988. Cingulin, a new peripheral component of tight junctions. Nature. 333:272-276.
    • (1988) Nature , vol.333 , pp. 272-276
    • Citi, S.1    Sabanay, H.2    Jakes, R.3    Geiger, B.4    Kendrick-Jones, J.5
  • 15
    • 0030572696 scopus 로고    scopus 로고
    • The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C
    • Diaz-Meco, M.T., M.M. Municio, S. Frutos, P. Sanchez, J. Lozano, L. Sanz, and J. Moscat. 1996a. The product of par-4, a gene induced during apoptosis, interacts selectively with the atypical isoforms of protein kinase C. Cell. 86: 777-786.
    • (1996) Cell , vol.86 , pp. 777-786
    • Diaz-Meco, M.T.1    Municio, M.M.2    Frutos, S.3    Sanchez, P.4    Lozano, J.5    Sanz, L.6    Moscat, J.7
  • 16
    • 0029655983 scopus 로고    scopus 로고
    • Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype λ/ι and stimulates its kinase activity in vitro and in vitro
    • Diaz-Meco, M.T., M.M. Municio, P. Sanchez, J. Lozano, and J. Moscat. 1996b. Lambda-interacting protein, a novel protein that specifically interacts with the zinc finger domain of the atypical protein kinase C isotype λ/ι and stimulates its kinase activity in vitro and in vitro. Mol. Cell. Biol. 16:105-114.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 105-114
    • Diaz-Meco, M.T.1    Municio, M.M.2    Sanchez, P.3    Lozano, J.4    Moscat, J.5
  • 17
    • 0029883798 scopus 로고    scopus 로고
    • Identification of isoforms of G proteins and PKC that colocalize with tight junctions
    • Dodane, V., and B. Kachar. 1996. Identification of isoforms of G proteins and PKC that colocalize with tight junctions. J. Membr. Biol. 149:199-209.
    • (1996) J. Membr. Biol. , vol.149 , pp. 199-209
    • Dodane, V.1    Kachar, B.2
  • 19
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ
    • Doyle, D.A., A. Lee, J. Lewis. E. Kim, M. Sheng, and R. MacKinnon. 1996. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell. 85:1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 20
    • 0030969575 scopus 로고    scopus 로고
    • MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption
    • Drewes, G., A. Ebneth, U. Preuss, E.M. Mandelkow, and E. Mandelkow. 1997. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 89:297-308.
    • (1997) Cell , vol.89 , pp. 297-308
    • Drewes, G.1    Ebneth, A.2    Preuss, U.3    Mandelkow, E.M.4    Mandelkow, E.5
  • 21
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin, D.G., and W.J. Nelson, 1996. Origins of cell polarity. Cell. 84:335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 22
    • 0029068244 scopus 로고
    • Apical, basal, and lateral cues for epithelial polarization
    • Eaton, S., and K. Simons. 1995. Apical, basal, and lateral cues for epithelial polarization. Cell. 82:5-8.
    • (1995) Cell , vol.82 , pp. 5-8
    • Eaton, S.1    Simons, K.2
  • 23
    • 0028843736 scopus 로고
    • Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos
    • Etemad-Moghadam, B., S. Guo, and K.J. Kemphues. 1995. Asymmetrically distributed PAR-3 protein contributes to cell polarity and spindle alignment in early C. elegans embryos. Cell. 83:743-752.
    • (1995) Cell , vol.83 , pp. 743-752
    • Etemad-Moghadam, B.1    Guo, S.2    Kemphues, K.J.3
  • 24
    • 0028152925 scopus 로고
    • Specificity of the high affinity interaction of protein kinase C with a physiological substrate, myristoylated alanine-rich protein kinase C substrate
    • Fujise, A., K. Mizuno, Y. Ueda, S. Osada, S. Hirai, A. Takayanagi, N. Shimizu, M.K. Owada, H. Nakajima, and S. Ohno. 1994. Specificity of the high affinity interaction of protein kinase C with a physiological substrate, myristoylated alanine-rich protein kinase C substrate. J. Biol. Chem. 269:31642-31648.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31642-31648
    • Fujise, A.1    Mizuno, K.2    Ueda, Y.3    Osada, S.4    Hirai, S.5    Takayanagi, A.6    Shimizu, N.7    Owada, M.K.8    Nakajima, H.9    Ohno, S.10
  • 25
    • 0029996765 scopus 로고    scopus 로고
    • Specification of the anteroposterior axis in Caenorhabditis elegans
    • Goldstein, B., and S.N. Hird. 1996. Specification of the anteroposterior axis in Caenorhabditis elegans. Development. 122:1467-1474.
    • (1996) Development , vol.122 , pp. 1467-1474
    • Goldstein, B.1    Hird, S.N.2
  • 27
    • 0020995629 scopus 로고
    • Immunoelectron microscopy using thin frozen section: Application to studies of the intracellular transport of Semliki forest virus spike glycoproteins
    • Griffiths, G., K. Simons, G. Warren, and K.T. Tokuyasu. 1986. Immunoelectron microscopy using thin frozen section: application to studies of the intracellular transport of Semliki forest virus spike glycoproteins. Methods Enzymol. 96:466-483.
    • (1986) Methods Enzymol. , vol.96 , pp. 466-483
    • Griffiths, G.1    Simons, K.2    Warren, G.3    Tokuyasu, K.T.4
  • 28
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner, B., T. Lowenkopf, and D. Apatira. 1991. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci USA. 88:3460-3464.
    • (1991) Proc. Natl. Acad. Sci USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 29
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B.M. 1996. Cell adhesion: the molecular basis of tissue architecture and morphogenesis. Cell. 84:345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 30
    • 0030217996 scopus 로고    scopus 로고
    • Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo
    • Guo, S., and K.J. Kemphues. 1996. Molecular genetics of asymmetric cleavage in the early Caenorhabditis elegans embryo. Curr. Opin. Genet. Dev. 6:408-415.
    • (1996) Curr. Opin. Genet. Dev. , vol.6 , pp. 408-415
    • Guo, S.1    Kemphues, K.J.2
  • 31
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3. a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins, J., L. Gu, E.S. Wittchen, J. Hibbard, and B.R. Stevenson. 1998. ZO-3. a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141:199-208.
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 32
    • 0026667606 scopus 로고
    • High-resolution mapping of mammalian genes by in situ hybridization to free chromatin
    • Heng, H.H., J. Squire, and L.C. Tsui. 1992. High-resolution mapping of mammalian genes by in situ hybridization to free chromatin. Proc. Natl. Acad. Sci. USA. 89:9509-9513.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9509-9513
    • Heng, H.H.1    Squire, J.2    Tsui, L.C.3
  • 33
    • 0027225483 scopus 로고
    • Modes of DAPI banding and simultaneous in situ hybridization
    • Heng, H.H., and L.C. Tsui. 1993. Modes of DAPI banding and simultaneous in situ hybridization. Chromosoma. 102:325-332.
    • (1993) Chromosoma , vol.102 , pp. 325-332
    • Heng, H.H.1    Tsui, L.C.2
  • 34
    • 0026603087 scopus 로고
    • Detection of the tight junction-associated protein ZO-1 in astrocytes and other nonepithelial cell types
    • Howarth, A.G., M.R. Hughes, and B.R. Stevenson. 1992. Detection of the tight junction-associated protein ZO-1 in astrocytes and other nonepithelial cell types. Am. J. Physiol. 262:C461-C469.
    • (1992) Am. J. Physiol. , vol.262
    • Howarth, A.G.1    Hughes, M.R.2    Stevenson, B.R.3
  • 35
    • 0027300689 scopus 로고
    • The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy
    • Itoh, M., A. Nagafuchi, S. Yonemura, T. Kitani-Yasuda, S. Tsukita, and S. Tsukita. 1993. The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J. Cell Biol. 121:491-502.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, S.5    Tsukita, S.6
  • 36
    • 0030614872 scopus 로고    scopus 로고
    • A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation
    • Izumi, Y., S. Hirai, Y. Tamai, A. Fujise-Matsuoka, Y. Nishimura, and S. Ohno. 1997. A protein kinase Cδ-binding protein SRBC whose expression is induced by serum starvation. J. Biol. Chem. 272:7381-7389.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7381-7389
    • Izumi, Y.1    Hirai, S.2    Tamai, Y.3    Fujise-Matsuoka, A.4    Nishimura, Y.5    Ohno, S.6
  • 37
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis, L.A., and D.A. Goodenough. 1994. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J. Cell Biol. 124:949-961.
    • (1994) J. Cell Biol. , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 38
    • 0029840160 scopus 로고    scopus 로고
    • Symplekin, a novel type of tight junction plaque protein
    • Keon, B.H., S. Schafer, C. Kuhn, C. Grund, and W.W. Franke. 1996. Symplekin, a novel type of tight junction plaque protein. J. Cell Biol. 134:1003-1018.
    • (1996) J. Cell Biol. , vol.134 , pp. 1003-1018
    • Keon, B.H.1    Schafer, S.2    Kuhn, C.3    Grund, C.4    Franke, W.W.5
  • 39
    • 0030666655 scopus 로고    scopus 로고
    • Mechanisms of asymmetric cell division during animal development
    • Knoblich, J.A. 1997. Mechanisms of asymmetric cell division during animal development. Curr. Opin. Cell Biol. 9:833-841.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 833-841
    • Knoblich, J.A.1
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou, W., H.J. Geuze, and J.W. Slot. 1996. Improving structural integrity of cryosections for immunogold labeling. Histochem. Cell Biol. 106:41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 42
    • 0027965006 scopus 로고
    • Protein kinase Cζ isoform is critical for κB-dependent promoter activation by sphingomyelinase
    • Lozano, J., E. Berra, M.M. Municio. M.T. Diaz-Meco, I. Dominguez, L. Sanz, and J. Moscat. 1994. Protein kinase Cζ isoform is critical for κB-dependent promoter activation by sphingomyelinase. J. Biol. Chem. 269:19200-19202.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19200-19202
    • Lozano, J.1    Berra, E.2    Municio, M.M.3    Diaz-Meco, M.T.4    Dominguez, I.5    Sanz, L.6    Moscat, J.7
  • 43
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen, D., and A.S. Gordon. 1998. Anchoring proteins for protein kinase C: a means for isozyme selectivity. FASEB J. 12:35-42.
    • (1998) FASEB J. , vol.12 , pp. 35-42
    • Mochly-Rosen, D.1    Gordon, A.S.2
  • 44
    • 0029003788 scopus 로고
    • PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid
    • Müller, G., M. Ayoub, P. Storz, J. Rennecke, D. Fabbro, and K. Pfizenmaier. 1995. PKCζ is a molecular switch in signal transduction of TNF-α, bifunctionally regulated by ceramide and arachidonic acid. EMBO (Eur. Mol. Biol. Organ.) J. 14:1961-1969.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 1961-1969
    • Müller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 45
    • 0027535742 scopus 로고
    • Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate
    • Nakanishi, H., K.A. Brewer, and J.H. Exton. 1993. Activation of the ζ isozyme of protein kinase C by phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 268:13-16.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13-16
    • Nakanishi, H.1    Brewer, K.A.2    Exton, J.H.3
  • 46
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. 1995. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9:484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 47
    • 0028340177 scopus 로고
    • Activation of novel protein kinases Cδ and ε upon mitogenic stimulation of quiescent rat 3Y1 fibroblasts
    • Ohno, S., K. Mizuno, Y. Adachi, A. Hata, Y. Akita, K. Akimoto, S. Osada, S. Hirai, and K. Suzuki. 1994. Activation of novel protein kinases Cδ and ε upon mitogenic stimulation of quiescent rat 3Y1 fibroblasts. J. Biol. Chem. 269:17495-17501.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17495-17501
    • Ohno, S.1    Mizuno, K.2    Adachi, Y.3    Hata, A.4    Akita, Y.5    Akimoto, K.6    Osada, S.7    Hirai, S.8    Suzuki, K.9
  • 48
    • 0026665459 scopus 로고
    • A new member of the protein kinase C family, nPKCθ, predominantly expressed in skeletal muscle
    • Osada, S., K. Mizuno, T.C. Saido, K. Suzuki, T. Kuroki, and S. Ohno. 1992. A new member of the protein kinase C family, nPKCθ, predominantly expressed in skeletal muscle. Mol. Cell Biol. 12:3930-3938.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3930-3938
    • Osada, S.1    Mizuno, K.2    Saido, T.C.3    Suzuki, K.4    Kuroki, T.5    Ohno, S.6
  • 49
    • 0023818801 scopus 로고
    • Loss of a Mr 78,000 marker in chemically induced transplantable carcinomas and primary carcinoma of human pancreas
    • Parsa, I. 1988. Loss of a Mr 78,000 marker in chemically induced transplantable carcinomas and primary carcinoma of human pancreas. Cancer Res. 48: 2265-2272.
    • (1988) Cancer Res. , vol.48 , pp. 2265-2272
    • Parsa, I.1
  • 50
    • 0030911597 scopus 로고    scopus 로고
    • Interaction of protein kinase Cζ with ZIP, a novel protein kinase C-binding protein
    • Puls, A., S. Schmidt, F. Grawe, and S. Stabel. 1997. Interaction of protein kinase Cζ with ZIP, a novel protein kinase C-binding protein. Proc. Natl. Acad. Sci. USA. 94:6191-6196.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6191-6196
    • Puls, A.1    Schmidt, S.2    Grawe, F.3    Stabel, S.4
  • 51
    • 0030039226 scopus 로고    scopus 로고
    • Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions
    • Rajasekaran, A.K., M. Hojo, T. Huima, and E. Rodriguez-Boulan. 1996. Catenins and zonula occludens-1 form a complex during early stages in the assembly of tight junctions. J. Cell Biol. 132:451-463.
    • (1996) J. Cell Biol. , vol.132 , pp. 451-463
    • Rajasekaran, A.K.1    Hojo, M.2    Huima, T.3    Rodriguez-Boulan, E.4
  • 52
    • 0029665589 scopus 로고    scopus 로고
    • The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts
    • Reynolds, A.B., J.M. Daniel, Y.Y. Mo, J. Wu, and Z. Zhang. 1996. The novel catenin p120cas binds classical cadherins and induces an unusual morphological phenotype in NIH3T3 fibroblasts. Exp. Cell Res. 225:328-337.
    • (1996) Exp. Cell Res. , vol.225 , pp. 328-337
    • Reynolds, A.B.1    Daniel, J.M.2    Mo, Y.Y.3    Wu, J.4    Zhang, Z.5
  • 53
    • 0031946369 scopus 로고    scopus 로고
    • Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62
    • Sanchez, P., G. De Career, I.V. Sandoval, J. Moscat, and M.T. Diaz-Meco. 1998. Localization of atypical protein kinase C isoforms into lysosome-targeted endosomes through interaction with p62. Mol. Cell Biol. 18:3069-3080.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3069-3080
    • Sanchez, P.1    De Career, G.2    Sandoval, I.V.3    Moscat, J.4    Diaz-Meco, M.T.5
  • 54
    • 0030473797 scopus 로고    scopus 로고
    • PDZ domains bind carboxy-teminal sequences of target proteins
    • Saras, J., and C.H. Heldin. 1996. PDZ domains bind carboxy-teminal sequences of target proteins. Trends Biochem. Sci. 21:455-458.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 455-458
    • Saras, J.1    Heldin, C.H.2
  • 55
    • 0028142091 scopus 로고
    • Activation of protein kinase C isozymes is associated with post-mitotic events in intestinal epithelial cells in situ
    • Saxon, M.L., X. Zhao, and J.D. Black. 1994. Activation of protein kinase C isozymes is associated with post-mitotic events in intestinal epithelial cells in situ. J. Cell Biol. 126:747-763.
    • (1994) J. Cell Biol. , vol.126 , pp. 747-763
    • Saxon, M.L.1    Zhao, X.2    Black, J.D.3
  • 56
    • 0030273003 scopus 로고    scopus 로고
    • PDZs and receptor/channel clustering: Rounding up the latest suspects
    • Sheng, M. 1996. PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron. 17:575-578.
    • (1996) Neuron , vol.17 , pp. 575-578
    • Sheng, M.1
  • 57
    • 0030810216 scopus 로고    scopus 로고
    • Protein kinase C-ζ as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport
    • Standaert, M.L., L. Galloway, P. Karnam, G. Bandyopadhyay, J. Moscat, and R.V. Farese. 1997. Protein kinase C-ζ as a downstream effector of phosphatidylinositol 3-kinase during insulin stimulation in rat adipocytes. Potential role in glucose transport. J. Biol. Chem. 272:30075-30082.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30075-30082
    • Standaert, M.L.1    Galloway, L.2    Karnam, P.3    Bandyopadhyay, G.4    Moscat, J.5    Farese, R.V.6
  • 58
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson, B.R., J.D. Siliciano, M.S. Mooseker, and D.A. Goodenough. 1986. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J. Cell Biol 103:755-766.
    • (1986) J. Cell Biol , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 59
    • 0029041046 scopus 로고
    • Regulated assembly of tight junctions by protein kinase C
    • Stuart, R.O., and S.K. Nigam. 1995. Regulated assembly of tight junctions by protein kinase C. Proc. Natl. Acad. Sci. USA. 92:6072-6076.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6072-6076
    • Stuart, R.O.1    Nigam, S.K.2
  • 60
    • 0031674842 scopus 로고    scopus 로고
    • Atypical Protein Kinase C Cooperates with PAR-3 to Establish Embryonic Polarity in Caenorhabditis elegans
    • Tabuse, Y., Y. Izumi, F. Piano, K.J. Kemphues, J. Miwa, and S. Ohno. 1998. Atypical Protein Kinase C Cooperates with PAR-3 to Establish Embryonic Polarity In Caenorhabditis elegans. Development. 125:3607-3614.
    • (1998) Development , vol.125 , pp. 3607-3614
    • Tabuse, Y.1    Izumi, Y.2    Piano, F.3    Kemphues, K.J.4    Miwa, J.5    Ohno, S.6
  • 61
    • 0030992837 scopus 로고    scopus 로고
    • Signaling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., and L.C. Cantley. 1997. Signaling through the lipid products of phosphoinositide-3-OH kinase. Nature. 387:673-676.
    • (1997) Nature , vol.387 , pp. 673-676
    • Toker, A.1    Cantley, L.C.2
  • 62
    • 0024318954 scopus 로고
    • Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy
    • Tokuyasu, K.T. 1989. Use of poly(vinylpyrrolidone) and poly(vinyl alcohol) for cryoultramicrotomy. Histochem. J. 21:163-171.
    • (1989) Histochem. J. , vol.21 , pp. 163-171
    • Tokuyasu, K.T.1
  • 63
    • 0030835610 scopus 로고    scopus 로고
    • A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade
    • Tsunoda, S., J. Sierralta, Y. Sun, R. Bodner, E. Suzuki, A. Becker, M. Socolich, and C.S. Zuker. 1997. A multivalent PDZ-domain protein assembles signaling complexes in a G-protein-coupled cascade. Nature. 388:243-249.
    • (1997) Nature , vol.388 , pp. 243-249
    • Tsunoda, S.1    Sierralta, J.2    Sun, Y.3    Bodner, R.4    Suzuki, E.5    Becker, A.6    Socolich, M.7    Zuker, C.S.8
  • 64
    • 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., B. Etemad-Moghadam, S. Guo, L. Boyd, B.W. Draper, C. C. Mello, J.R. Priess, and K.J. Kemphues. 1996. 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) Development , vol.122 , pp. 3133-3140
    • Watts, J.L.1    Etemad-Moghadam, B.2    Guo, S.3    Boyd, L.4    Draper, B.W.5    Mello, C.C.6    Priess, J.R.7    Kemphues, K.J.8
  • 67
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions
    • Willott, E., M.S. Balda, A.S. Fanning, B. Jameson, C. Van Itallie, and J.M. Anderson. 1993. The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions. Proc. Natl. Acad. Sci. USA. 90:7834-7838.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7834-7838
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jameson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 68
    • 0029819449 scopus 로고    scopus 로고
    • Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia
    • Woods, D.F., C. Hough, D. Peel, G. Callaini, and P.J. Bryant. 1996. Dlg protein is required for junction structure, cell polarity, and proliferation control in Drosophila epithelia. J. Cell Biol. 134:1469-1482.
    • (1996) J. Cell Biol. , vol.134 , pp. 1469-1482
    • Woods, D.F.1    Hough, C.2    Peel, D.3    Callaini, G.4    Bryant, P.J.5
  • 69
    • 0027977927 scopus 로고
    • A role for ζ, protein kinase C in nerve growth factor-induced differentiation of PC12 cells
    • Wooten, M.W., G. Zhou, M.L. Seibenhener, and E.S. Coleman. 1994. A role for ζ, protein kinase C in nerve growth factor-induced differentiation of PC12 cells. Cell Growth Differ. 5:395-403.
    • (1994) Cell Growth Differ. , vol.5 , pp. 395-403
    • Wooten, M.W.1    Zhou, G.2    Seibenhener, M.L.3    Coleman, E.S.4
  • 70
    • 0029758505 scopus 로고    scopus 로고
    • PDGF induction of α2 integrin gene expression is mediated by protein kinase C-ζ
    • Xu, J., M.M. Zutter, S.A. Santoro, and R.A. Clark. 1996. PDGF induction of α2 integrin gene expression is mediated by protein kinase C-ζ. J. Cell Biol. 134:1301-1311.
    • (1996) J. Cell Biol. , vol.134 , pp. 1301-1311
    • Xu, J.1    Zutter, M.M.2    Santoro, S.A.3    Clark, R.A.4
  • 71
    • 0030724368 scopus 로고    scopus 로고
    • The ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells
    • Yamamoto, T., N. Harada, K. Kano, S. Taya, E. Canaani, Y. Matsuura, A. Mizoguchi, C. Ide, and K. Kaibuchi. 1997. The ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells. J. Cell Biol. 139:785-795.
    • (1997) J. Cell Biol. , vol.139 , pp. 785-795
    • Yamamoto, T.1    Harada, N.2    Kano, K.3    Taya, S.4    Canaani, E.5    Matsuura, Y.6    Mizoguchi, A.7    Ide, C.8    Kaibuchi, K.9
  • 72
    • 0028821093 scopus 로고
    • Cell-to-cell adherens junction formation and actin filament organization: Similarities and differences between non-polarized fibroblasts and polarized epithelial cells
    • Yonemura, S., M. Itoh, A. Nagafuchi, and S. Tsukita. 1995. Cell-to-cell adherens junction formation and actin filament organization: similarities and differences between non-polarized fibroblasts and polarized epithelial cells. J. Cell Sci. 108:127-142,
    • (1995) J. Cell Sci. , vol.108 , pp. 127-142
    • Yonemura, S.1    Itoh, M.2    Nagafuchi, A.3    Tsukita, S.4
  • 73
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong, Y., T. Saitoh, T. Minase, N. Sawada, K. Enomoto, and M. Mori. 1993. Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J. Cell Biol. 120:477-483.
    • (1993) J. Cell Biol. , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, T.3    Sawada, N.4    Enomoto, K.5    Mori, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.