메뉴 건너뛰기




Volumn 263, Issue 1, 1999, Pages 276-286

Endogenous casein kinase I catalyzes the phosphorylation of the lens fiber cell connexin49

Author keywords

Casein kinase I; Connexin; Lens; Protein phosphorylation; Sheep

Indexed keywords

CASEIN KINASE I; CONNEXIN 49; GAP JUNCTION PROTEIN; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 0033168865     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00502.x     Document Type: Article
Times cited : (15)

References (64)
  • 2
    • 0030028301 scopus 로고    scopus 로고
    • The gap junction communication channel
    • 2. Kumar, N.M. & Gilula, N.B. (1996) The gap junction communication channel. Cell 84, 381-388.
    • (1996) Cell , vol.84 , pp. 381-388
    • Kumar, N.M.1    Gilula, N.B.2
  • 3
    • 0027352474 scopus 로고
    • Gap junctions
    • Multiplicity of controls in differentiated and undifferentiated cells and possible functional implications
    • 3. Sáez, J.C., Berthoud, V.M., Moreno, A.P. & Spray, D.C. (1993) Gap junctions. Multiplicity of controls in differentiated and undifferentiated cells and possible functional implications. Adv. Second Messenger Phosphoprotein Res. 27, 163-198.
    • (1993) Adv. Second Messenger Phosphoprotein Res. , vol.27 , pp. 163-198
    • Sáez, J.C.1    Berthoud, V.M.2    Moreno, A.P.3    Spray, D.C.4
  • 4
    • 0029974655 scopus 로고    scopus 로고
    • Connections with connexins: The molecular basis of direct intercellular signaling
    • 4. Bruzzone, R., White, T.W. & Paul, D.L. (1996) Connections with connexins: the molecular basis of direct intercellular signaling, Eur. J. Biochem. 238, 1-27.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 1-27
    • Bruzzone, R.1    White, T.W.2    Paul, D.L.3
  • 5
    • 0028901331 scopus 로고
    • Structure-function relationships in gap junctions
    • 5. Wolburg, H. & Rohlmann, A. (1995) Structure-function relationships in gap junctions. Int. Rev. Cytol. 157, 315-373.
    • (1995) Int. Rev. Cytol. , vol.157 , pp. 315-373
    • Wolburg, H.1    Rohlmann, A.2
  • 6
    • 0018719555 scopus 로고
    • Lens gap junctions: A structural hypothesis for nonregulated low-resistance intercellular pathways
    • 6. Goodenough, D.A. (1979) Lens gap junctions: a structural hypothesis for nonregulated low-resistance intercellular pathways. Invest. Ophthalmol. Vis. Sci. 18, 1104-1122.
    • (1979) Invest. Ophthalmol. Vis. Sci. , vol.18 , pp. 1104-1122
    • Goodenough, D.A.1
  • 7
    • 0026815368 scopus 로고
    • The crystalline lens
    • A system networked by gap junctional intercellular communication
    • 7. Goodenough, D.A. (1992) The crystalline lens. A system networked by gap junctional intercellular communication. Semin. Cell Biol. 3, 49-58.
    • (1992) Semin. Cell Biol. , vol.3 , pp. 49-58
    • Goodenough, D.A.1
  • 8
    • 0024592298 scopus 로고
    • Anti-sera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues
    • 8. Beyer, E.C., Kistler, J., Paul, D.L. & Goodenough, D.A. (1989) Anti-sera directed against connexin43 peptides react with a 43-kD protein localized to gap junctions in myocardium and other tissues. J. Cell Biol. 108, 595-605.
    • (1989) J. Cell Biol. , vol.108 , pp. 595-605
    • Beyer, E.C.1    Kistler, J.2    Paul, D.L.3    Goodenough, D.A.4
  • 9
    • 0025287594 scopus 로고
    • Expression of the gap junction protein connexin43 in embryonic chicken lens: Molecular cloning, ultrastructural localization, and post-translational phosphorylation
    • 9. Musil, L.S., Beyer, E.C. & Goodenough, D.A. (1990) Expression of the gap junction protein connexin43 in embryonic chicken lens: molecular cloning, ultrastructural localization, and post-translational phosphorylation. J. Membr. Biol. 116, 163-175.
    • (1990) J. Membr. Biol. , vol.116 , pp. 163-175
    • Musil, L.S.1    Beyer, E.C.2    Goodenough, D.A.3
  • 10
    • 0021868690 scopus 로고
    • Identification of a 70,000-D protein in lens membrane junctional domains
    • 10. Kistler, J., Kirkland, B. & Billivant, S. (1985) Identification of a 70,000-D protein in lens membrane junctional domains. J. Cell Biol. 101, 28-35.
    • (1985) J. Cell Biol. , vol.101 , pp. 28-35
    • Kistler, J.1    Kirkland, B.2    Billivant, S.3
  • 11
    • 0026352039 scopus 로고
    • Connexin46, a novel gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes
    • 11. Paul, D.L., Ebihara, L., Takemoto, L.J., Swensen, K.I. & Goodenough, D.A. (1991) Connexin46, a novel gap junction protein, induces voltage-gated currents in nonjunctional plasma membrane of Xenopus oocytes. J. Cell Biol. 115, 1077-1089.
    • (1991) J. Cell Biol. , vol.115 , pp. 1077-1089
    • Paul, D.L.1    Ebihara, L.2    Takemoto, L.J.3    Swensen, K.I.4    Goodenough, D.A.5
  • 12
    • 0026786352 scopus 로고
    • The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens
    • 12. Tenbroek, E., Arneson, M., Jarvis, L. & Louis, C.F. (1992) The distribution of the fiber cell intrinsic membrane proteins MP20 and connexin46 in the bovine lens. J. Cell Sci. 103, 245-257.
    • (1992) J. Cell Sci. , vol.103 , pp. 245-257
    • Tenbroek, E.1    Arneson, M.2    Jarvis, L.3    Louis, C.F.4
  • 13
    • 0027070644 scopus 로고
    • Mouse Cx50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70
    • 13. White, T.W., Bruzzone, R., Goodenough, D.A. & Paul, D.L. (1992) Mouse Cx50, a functional member of the connexin family of gap junction proteins, is the lens fiber protein MP70. Mol. Biol. Cell 3, 711-720.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 711-720
    • White, T.W.1    Bruzzone, R.2    Goodenough, D.A.3    Paul, D.L.4
  • 14
    • 0028823838 scopus 로고
    • Characterization of the ovine-lens plasma-membrane protein-kinase substrates
    • 14. Arneson, M.L., Cheng, H.-L. & Louis, C.F. (1995) Characterization of the ovine-lens plasma-membrane protein-kinase substrates. Eur. J. Biochem. 234, 670-679.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 670-679
    • Arneson, M.L.1    Cheng, H.-L.2    Louis, C.F.3
  • 15
    • 0027770704 scopus 로고
    • Posttranslational phosphorylation of lens fiber connexin46: A slow occurrence
    • 15. Jiang, J.X., Paul, D.L. & Goodenough, D.A. (1993) Posttranslational phosphorylation of lens fiber connexin46: a slow occurrence. Invest. Ophthalmol. Vis. Sci. 34, 3558-3565.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 3558-3565
    • Jiang, J.X.1    Paul, D.L.2    Goodenough, D.A.3
  • 16
    • 0028267415 scopus 로고
    • Molecular cloning and functional characterization of chicken lens fiber connexin 45.6
    • 16. Jiang, J.X., White, T.W., Goodenough, D.A. & Paul, D.L. (1994) Molecular cloning and functional characterization of chicken lens fiber connexin 45.6. Mol. Biol Cell 5, 363-373.
    • (1994) Mol. Biol Cell , vol.5 , pp. 363-373
    • Jiang, J.X.1    White, T.W.2    Goodenough, D.A.3    Paul, D.L.4
  • 17
    • 0025155347 scopus 로고
    • Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines
    • 17. Musil, L.S., Cunningham, B.A., Edelman, G.M. & Goodenough, D.A. (1990) Differential phosphorylation of the gap junction protein connexin43 in junctional communication-competent and -deficient cell lines. J. Cell Biol. 111, 2077-2088.
    • (1990) J. Cell Biol. , vol.111 , pp. 2077-2088
    • Musil, L.S.1    Cunningham, B.A.2    Edelman, G.M.3    Goodenough, D.A.4
  • 18
    • 0025789648 scopus 로고
    • Biochemical analysis of connexin intercellular transport, phosphorylation and assembly into gap junctional plaques
    • 18. Musil, L.S. & Goodenough, D.A. (1991) Biochemical analysis of connexin intercellular transport, phosphorylation and assembly into gap junctional plaques. J. Cell Biol. 115, 1357-1374.
    • (1991) J. Cell Biol. , vol.115 , pp. 1357-1374
    • Musil, L.S.1    Goodenough, D.A.2
  • 19
    • 0024464862 scopus 로고
    • CAMP-dependent protein kinase phosphorylates gap junction protein in lens cortex but not in lens nucleus
    • 19. Voorter, C.E.M. & Kistler, J. (1989) cAMP-dependent protein kinase phosphorylates gap junction protein in lens cortex but not in lens nucleus. Biochim. Biophys. Acta 986, 8-10.
    • (1989) Biochim. Biophys. Acta , vol.986 , pp. 8-10
    • Voorter, C.E.M.1    Kistler, J.2
  • 20
    • 0028882497 scopus 로고
    • Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions
    • 20. Kwak, B.R., Hermans, M.M.P., De Jonge, H.R., Lohmann, S.M., Jongsma, H.J. & Chanson, M. (1995) Differential regulation of distinct types of gap junction channels by similar phosphorylating conditions. Mol. Biol. Cell 6, 1707-1719.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1707-1719
    • Kwak, B.R.1    Hermans, M.M.P.2    De Jonge, H.R.3    Lohmann, S.M.4    Jongsma, H.J.5    Chanson, M.6
  • 21
    • 0028584195 scopus 로고
    • Analyzing phorbol ester effects on gap junctional communication: A dramatic inhibition of assembly
    • 21. Lampe, P.D. (1994) Analyzing phorbol ester effects on gap junctional communication: a dramatic inhibition of assembly. J. Cell Biol. 127, 1895-1905.
    • (1994) J. Cell Biol. , vol.127 , pp. 1895-1905
    • Lampe, P.D.1
  • 22
    • 0026769766 scopus 로고
    • Phosphorylation shifts unitary conductance and modifies voltage dependent kinetics of human connexin43 gap junction channels
    • 22. Moreno, A.P., Fishman, G.I. & Spray, D.C. (1992) Phosphorylation shifts unitary conductance and modifies voltage dependent kinetics of human connexin43 gap junction channels. Biophys. J. 62, 51-53.
    • (1992) Biophys. J. , vol.62 , pp. 51-53
    • Moreno, A.P.1    Fishman, G.I.2    Spray, D.C.3
  • 23
    • 0029877202 scopus 로고    scopus 로고
    • Molecular cloning of sheep connexin49 and its identity with MP70
    • 23. Yang, D.-I. & Louis, C.F. (1996) Molecular cloning of sheep connexin49 and its identity with MP70. Curr. Eye Res. 15, 307-314.
    • (1996) Curr. Eye Res. , vol.15 , pp. 307-314
    • Yang, D.-I.1    Louis, C.F.2
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 24. 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
  • 26
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • 26. Schägger, H. & Von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 68-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 68-379
    • Schägger, H.1    Von Jagow, G.2
  • 27
    • 0029036113 scopus 로고
    • Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family
    • 27. Fish, K.J., Cegielska, A., Getman, M.E., Landes, G.M. & Virshup. D.M. (1995) Isolation and characterization of human casein kinase I epsilon (CKI), a novel member of the CKI gene family. J. Biol. Chem. 270, 14875-14883.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14875-14883
    • Fish, K.J.1    Cegielska, A.2    Getman, M.E.3    Landes, G.M.4    Virshup, D.M.5
  • 28
    • 0027418069 scopus 로고
    • Molecular cloning, expression, and characterization of a 49-kilodalton casein kinase I isoform from rat testis
    • 28. Graves, P.R., Hass, D.W., Hagedorn, C.H., DePaoli-Roach, A.A. & Roach, P.J. (1993) Molecular cloning, expression, and characterization of a 49-kilodalton casein kinase I isoform from rat testis. J. Biol. Chem. 268, 6394-6401.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6394-6401
    • Graves, P.R.1    Hass, D.W.2    Hagedorn, C.H.3    DePaoli-Roach, A.A.4    Roach, P.J.5
  • 29
    • 0026093758 scopus 로고
    • Purification of casein kinase I and isolation of cDNA encoding multiple casein kinase I-like enzymes
    • 29. Rowles, J., Slaughter, C., Moomaw, C., Hsu, J. & Cobb, M.H. (1991) Purification of casein kinase I and isolation of cDNA encoding multiple casein kinase I-like enzymes. Proc. Natl Acad. Sci. USA 88, 9548-9552.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9548-9552
    • Rowles, J.1    Slaughter, C.2    Moomaw, C.3    Hsu, J.4    Cobb, M.H.5
  • 32
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • 32. Chomezynski, P. & Sacchi, N. (1987) Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomezynski, P.1    Sacchi, N.2
  • 33
    • 0024358172 scopus 로고
    • A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel
    • 33. Kameshita, I. & Fujisawa, H. (1989) A sensitive method for detection of calmodulin-dependent protein kinase II activity in sodium dodecyl sulfate-polyacrylamide gel. Anal. Biochem. 183, 139-143.
    • (1989) Anal. Biochem. , vol.183 , pp. 139-143
    • Kameshita, I.1    Fujisawa, H.2
  • 34
    • 0027755244 scopus 로고
    • Identification of a family of casein kinases in Paramecium: Biochemical characterization and cellular localization
    • 34. Walczak, C.E., Anderson, R.A. & Nelson, D.L. (1993) Identification of a family of casein kinases in Paramecium: biochemical characterization and cellular localization. Biochem. J. 296, 729-735.
    • (1993) Biochem. J. , vol.296 , pp. 729-735
    • Walczak, C.E.1    Anderson, R.A.2    Nelson, D.L.3
  • 35
    • 0017337988 scopus 로고
    • Phosphorylation of rabbit and human erythrocyte membranes by soluble adenosine 3′:5′-monophosphate-dependent and -independent protein kinase
    • 35. Hosey, M.M. & Tao, M. (1977) Phosphorylation of rabbit and human erythrocyte membranes by soluble adenosine 3′:5′-monophosphate-dependent and -independent protein kinase. J. Biol. Chem. 252, 102-109.
    • (1977) J. Biol. Chem. , vol.252 , pp. 102-109
    • Hosey, M.M.1    Tao, M.2
  • 36
    • 0022931548 scopus 로고
    • 2+-dependent phosphorylation of human red cell membrane skeletal proteins
    • 2+-dependent phosphorylation of human red cell membrane skeletal proteins. J. Biol. Chem. 261, 7701-7709.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7701-7709
    • Cohen, C.M.1    Foley, S.F.2
  • 37
    • 0022381636 scopus 로고
    • Protein kinase C in the human erythrocyte
    • Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins
    • 37. Palfrey, H.C. & Waseem, A. (1985) Protein kinase C in the human erythrocyte. Translocation to the plasma membrane and phosphorylation of bands 4.1 and 4.9 and other membrane proteins. J. Biol. Chem. 260, 16021-16029.
    • (1985) J. Biol. Chem. , vol.260 , pp. 16021-16029
    • Palfrey, H.C.1    Waseem, A.2
  • 38
    • 0019310706 scopus 로고
    • Purification and characterization of a membrane-bound protein kinase from human erythrocytes
    • 38. Tao, M., Conway, R. & Cheta, S. (1980) Purification and characterization of a membrane-bound protein kinase from human erythrocytes. J. Biol. Chem. 255, 2563-2568.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2563-2568
    • Tao, M.1    Conway, R.2    Cheta, S.3
  • 39
    • 0026076717 scopus 로고
    • Identity and substrate specificity of human erythrocyte membrane-bound and cytosolic casein kinases
    • 39. Wei, T. & Tao, M. (1991) Identity and substrate specificity of human erythrocyte membrane-bound and cytosolic casein kinases. FEBS Lett. 292, 141-144.
    • (1991) FEBS Lett. , vol.292 , pp. 141-144
    • Wei, T.1    Tao, M.2
  • 40
    • 0027358479 scopus 로고
    • Human erythrocyte casein kinae II: Characterization and phosphorylation of membrane cytoskeletal proteins
    • 40. Wei, T. & Tao, M. (1993) Human erythrocyte casein kinae II: characterization and phosphorylation of membrane cytoskeletal proteins. Arch. Biochem. Biophys. 307, 206-216.
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 206-216
    • Wei, T.1    Tao, M.2
  • 41
    • 0020437026 scopus 로고
    • Casein kinases-multipotential protein kinases
    • 41. Hathaway, G.M. & Traugh, J.A. (1982) Casein kinases-multipotential protein kinases. Curr. Top. Cell. Regul. 21, 101-127.
    • (1982) Curr. Top. Cell. Regul. , vol.21 , pp. 101-127
    • Hathaway, G.M.1    Traugh, J.A.2
  • 42
    • 0022388397 scopus 로고
    • Phosphorylation of ankyrin decreases its affinity for spectrin
    • 42. Lu, P.-W., Soong, C.-J. & Tao, M. (1985) Phosphorylation of ankyrin decreases its affinity for spectrin. J. Biol. Chem. 260, 14958-14964.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14958-14964
    • Lu, P.-W.1    Soong, C.-J.2    Tao, M.3
  • 43
    • 0030705190 scopus 로고    scopus 로고
    • Identification, cloning, and mutational analysis of the casein kinase I cDNA of the malaria parasite, Plasmodium falciparum
    • 43. Barik. S., Taylor. R.E. & Chakrabarti, D. (1997) Identification, cloning, and mutational analysis of the casein kinase I cDNA of the malaria parasite, Plasmodium falciparum. J. Biol. Chem 272, 26132-26138.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26132-26138
    • Barik, S.1    Taylor, R.E.2    Chakrabarti, D.3
  • 44
    • 0024515028 scopus 로고
    • A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroiso-quinoline-8-sulfinamide, and affinity purification of casein kinase I from bovine testis
    • 44. Chijiwa, T., Hagiwara, M. & Hidaka, H. (1989) A newly synthesized selective casein kinase I inhibitor, N-(2-aminoethyl)-5-chloroiso-quinoline-8-sulfinamide, and affinity purification of casein kinase I from bovine testis. J. Biol. Chem. 264, 4924-4927.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4924-4927
    • Chijiwa, T.1    Hagiwara, M.2    Hidaka, H.3
  • 46
    • 0023232998 scopus 로고
    • Protein processing in lens intercellular junctions: Cleavage of MP70 to MP38
    • 46. Kistler, J. & Billivant, S. (1987) Protein processing in lens intercellular junctions: cleavage of MP70 to MP38. Invest. Ophthalmol. Vis. Sci. 28, 1687-1692.
    • (1987) Invest. Ophthalmol. Vis. Sci. , vol.28 , pp. 1687-1692
    • Kistler, J.1    Billivant, S.2
  • 47
    • 0025274271 scopus 로고
    • MP38 contains the membrane-embedded domain of the lens fiber gap junction protein MP70
    • 47. Kistler, J., Schaller, J. & Sigrist, H. (1990) MP38 contains the membrane-embedded domain of the lens fiber gap junction protein MP70. J. Biol. Chem. 265, 13357-13361.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13357-13361
    • Kistler, J.1    Schaller, J.2    Sigrist, H.3
  • 48
    • 0025299458 scopus 로고
    • Bovine lens membrane proteins: MP70, MP64, MP 38 are products of the same gene
    • 48. Rao, G.N., Gutekunst, K.A. & Church, R.L. (1990) Bovine lens membrane proteins: MP70, MP64, and MP 38 are products of the same gene. Ophthal. Res. 22, 166-172.
    • (1990) Ophthal. Res. , vol.22 , pp. 166-172
    • Rao, G.N.1    Gutekunst, K.A.2    Church, R.L.3
  • 49
    • 0025731508 scopus 로고
    • Role of acidic residues as substrate determinants for casein kinase I
    • 49. Flotow, H. & Roach. P.J. (1991) Role of acidic residues as substrate determinants for casein kinase I. J. Biol. Chem. 266, 3724-3727.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3724-3727
    • Flotow, H.1    Roach, P.J.2
  • 50
    • 0026558816 scopus 로고
    • Determinants on simian virus 40 large T antigen are important for recognition and phosphorylation by casein kinase I
    • 50. Umphress. J.L., Tuazon, P.T., Chen, C.-J. & Traugh, J.A. (1992) Determinants on simian virus 40 large T antigen are important for recognition and phosphorylation by casein kinase I. Eur. J. Biochem. 203, 239-243.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 239-243
    • Umphress, J.L.1    Tuazon, P.T.2    Chen, C.-J.3    Traugh, J.A.4
  • 51
    • 0030760308 scopus 로고    scopus 로고
    • Stimulus-dependent phosphorylation of g-protein-coupled receptors by casein kinase Iα
    • 51. Tobin, A.B., Totty, N.F., Sterlin, A.E. & Nahorski, S.R. (1997) Stimulus-dependent phosphorylation of G-protein-coupled receptors by casein kinase Iα. J. Biol. Chem. 272, 20844-20849.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20844-20849
    • Tobin, A.B.1    Totty, N.F.2    Sterlin, A.E.3    Nahorski, S.R.4
  • 52
    • 0026039891 scopus 로고
    • Casein kinase I and II-multi-potential serine protein kinases: Structure, function, and regulation
    • 52. Tuazon, P.T. & Traugh, J.A. (1991) Casein kinase I and II-multi-potential serine protein kinases: structure, function, and regulation. Adv. Second Messenger Phosphoprotein Res. 23, 123-164.
    • (1991) Adv. Second Messenger Phosphoprotein Res. , vol.23 , pp. 123-164
    • Tuazon, P.T.1    Traugh, J.A.2
  • 53
    • 0027396834 scopus 로고
    • Control of simian virus 40 DNA replication by the HeLa cell nuclear kinase casein kinase I
    • 53. Cegielska, A. & Virshup, D.M. (1993) Control of simian virus 40 DNA replication by the HeLa cell nuclear kinase casein kinase I. Mol. Cell. Biol. 13, 1202-1211.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1202-1211
    • Cegielska, A.1    Virshup, D.M.2
  • 54
    • 0022512219 scopus 로고
    • Phosphorylation reduces the affinity of protein 4.1 for spectrin
    • 54. Eder, P.S., Soong, C.-J. & Tao, M. (1986) Phosphorylation reduces the affinity of protein 4.1 for spectrin. Biochem. 25, 1764-1770.
    • (1986) Biochem. , vol.25 , pp. 1764-1770
    • Eder, P.S.1    Soong, C.-J.2    Tao, M.3
  • 55
    • 0032213106 scopus 로고    scopus 로고
    • Casein kinase I: Spatial organization and positioning of a multifunctional protein kinase family
    • 55. Gross, S.D. & Anderson, R.A. (1998) Casein kinase I: spatial organization and positioning of a multifunctional protein kinase family. Cell Signal 10, 699-711.
    • (1998) Cell Signal , vol.10 , pp. 699-711
    • Gross, S.D.1    Anderson, R.A.2
  • 56
    • 0028953284 scopus 로고
    • Modulation of erythrocyte membrane mechanical function by β-spectrin phosphorylation and dephosphorylation
    • 56. Manno, S., Takakuwa, Y., Nagao, K. & Mohandas, N. (1995) Modulation of erythrocyte membrane mechanical function by β-spectrin phosphorylation and dephosphorylation. J. Biol. Chem. 270, 5659-5665.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5659-5665
    • Manno, S.1    Takakuwa, Y.2    Nagao, K.3    Mohandas, N.4
  • 57
    • 0026768033 scopus 로고
    • Spatial variations in membrane properties in intact rat lens
    • 57. Baldo, G.J. & Mathias, R.T. (1992) Spatial variations in membrane properties in intact rat lens. Biophys. J. 63, 518-529.
    • (1992) Biophys. J. , vol.63 , pp. 518-529
    • Baldo, G.J.1    Mathias, R.T.2
  • 58
    • 0030958516 scopus 로고    scopus 로고
    • Processing of the gap junction protein connexin50 in the ocular lens is accomplished by calpain
    • 58. Lin, J.S., Fitzgerald, S., Dong, Y., Knight, C., Donaldson, P. & Kistler, J. (1997) Processing of the gap junction protein connexin50 in the ocular lens is accomplished by calpain. Eur. J. Cell Biol. 73, 141-149.
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 141-149
    • Lin, J.S.1    Fitzgerald, S.2    Dong, Y.3    Knight, C.4    Donaldson, P.5    Kistler, J.6
  • 59
    • 85085786923 scopus 로고    scopus 로고
    • Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage
    • 59. Lin, J.S., Eckert, R., Kistler, J. & Donaldson, P. (1998) Spatial differences in gap junction gating in the lens are a consequence of connexin cleavage. Eur. J. Cell Biol. 75, 1 -5.
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 1-5
    • Lin, J.S.1    Eckert, R.2    Kistler, J.3    Donaldson, P.4
  • 60
    • 0031059261 scopus 로고    scopus 로고
    • The gap-junction protein connexin 56 is phosphorylated in the intracellular loop and the carboxy-terminal region
    • 60. Berthoud, V.M., Beyer, E.C., Kurata, W.E., Lau, A.F. & Lampe, P.D. (1997) The gap-junction protein connexin 56 is phosphorylated in the intracellular loop and the carboxy-terminal region. Eur. J. Biochem. 244, 89-97.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 89-97
    • Berthoud, V.M.1    Beyer, E.C.2    Kurata, W.E.3    Lau, A.F.4    Lampe, P.D.5
  • 62
    • 0028283183 scopus 로고
    • Human connexin43 gap junction channels: Regulation of unitary conductance by phosphorylation
    • 62. Moreno, A.P., Sáez, J.C., Fishman, G.I. & Spray, D.C. (1994) Human connexin43 gap junction channels: regulation of unitary conductance by phosphorylation. Circ Res. 74, 1050-1057.
    • (1994) Circ Res. , vol.74 , pp. 1050-1057
    • Moreno, A.P.1    Sáez, J.C.2    Fishman, G.I.3    Spray, D.C.4
  • 63
    • 0030022421 scopus 로고    scopus 로고
    • Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein
    • 63. Warn-Cramer, B.J., Lampe, P.D., Kurata, W.E., Kanemitsu, M.Y., Loo, L.W.M., Eckhart, W. & Lau, A.F. (1996) Characterization of the mitogen-activated protein kinase phosphorylation sites on the connexin-43 gap junction protein. J. Biol. Chem. 271, 3779-3786.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3779-3786
    • Warn-Cramer, B.J.1    Lampe, P.D.2    Kurata, W.E.3    Kanemitsu, M.Y.4    Loo, L.W.M.5    Eckhart, W.6    Lau, A.F.7
  • 64
    • 0019882018 scopus 로고
    • Silver staining of proteins in polyacrylamide gels
    • 64. Wray, W., Boulikas, T., Wray, V.P. & Hancock, R. (1981) Silver staining of proteins in polyacrylamide gels. J. Biochem. 118, 197-203.
    • (1981) J. Biochem. , vol.118 , pp. 197-203
    • Wray, W.1    Boulikas, T.2    Wray, V.P.3    Hancock, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.