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Volumn 118, Issue 7, 2005, Pages 1427-1436

Palmitoylation of claudins is required for efficient tight-junction localization

Author keywords

Claudin; Claudins; Palmitoylation; Tight junctions

Indexed keywords

CAVEOLIN; CLAUDIN; CLAUDIN 14; CYSTEINE; DETERGENT; MUTANT PROTEIN; PALMITIC ACID; SERINE; TRITIUM; UNCLASSIFIED DRUG;

EID: 17844408453     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.01735     Document Type: Article
Times cited : (161)

References (33)
  • 1
    • 0037115724 scopus 로고    scopus 로고
    • Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells
    • Amasheh, S., Meiri, N., Gitter, A. H., Schoneberg, T., Mankertz, J., Schulzke, J. D. and Fromm, M. (2002). Claudin-2 expression induces cation-selective channels in tight junctions of epithelial cells. J. Cell Sci. 115, 4969-4976.
    • (2002) J. Cell Sci. , vol.115 , pp. 4969-4976
    • Amasheh, S.1    Meiri, N.2    Gitter, A.H.3    Schoneberg, T.4    Mankertz, J.5    Schulzke, J.D.6    Fromm, M.7
  • 3
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling
    • Berditchevski, F., Odintsova, E., Sawada, S. and Gilbert, E. (2002). Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. J. Biol. Chem. 277, 36991-37000.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 4
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Bijlmakers, M. J. and Marsh, M. (2003). The on-off story of protein palmitoylation. Trends Cell Biol. 13, 32-42.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Bijlmakers, M.J.1    Marsh, M.2
  • 5
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • Charrin, S., Manie, S., Oualid, M., Billard, M., Boucheix, C. and Rubinstein, E. (2002). Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett. 516, 139-144.
    • (2002) FEBS Lett. , vol.516 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 8
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse, M., Sasaki, H., Fujimoto, K. and Tsukita, S. (1998). A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143, 391-401.
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 9
    • 0035897412 scopus 로고    scopus 로고
    • Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells
    • Furuse, M., Furuse, K., Sasaki, H. and Tsukita, S. (2001). Conversion of zonulae occludentes from tight to leaky strand type by introducing claudin-2 into Madin-Darby canine kidney I cells. J. Cell Biol. 153, 263-272.
    • (2001) J. Cell Biol. , vol.153 , pp. 263-272
    • Furuse, M.1    Furuse, K.2    Sasaki, H.3    Tsukita, S.4
  • 10
    • 0142026252 scopus 로고    scopus 로고
    • Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways
    • Ishizaki, T., Chiba, H., Kojima, T., Fujibe, M., Soma, T., Miyajima, H., Nagasawa, K., Wada, I. and Sawada, N. (2003). Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways. Exp. Cell Res. 290 275-288.
    • (2003) Exp. Cell Res. , vol.290 , pp. 275-288
    • Ishizaki, T.1    Chiba, H.2    Kojima, T.3    Fujibe, M.4    Soma, T.5    Miyajima, H.6    Nagasawa, K.7    Wada, I.8    Sawada, N.9
  • 11
    • 0038660604 scopus 로고    scopus 로고
    • Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking
    • Kalinina, E. V. and Fricker, L. D. (2003). Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking. J. Biol. Chem. 278, 9244-9249.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9244-9249
    • Kalinina, E.V.1    Fricker, L.D.2
  • 12
    • 0027999333 scopus 로고
    • Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor
    • Kawate, N. and Menon, K. M. (1994). Palmitoylation of luteinizing hormone/human choriogonadotropin receptors in transfected cells. Abolition of palmitoylation by mutation of Cys-621 and Cys-622 residues in the cytoplasmic tail increases ligand-induced internalization of the receptor. J. Biol. Chem. 269, 30651-30658.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30651-30658
    • Kawate, N.1    Menon, K.M.2
  • 15
    • 2442689137 scopus 로고    scopus 로고
    • Expression of claudin-7 and -8 along the mouse nephron
    • Li, W. Y., Huey, C. L. and Yu, A. S. (2004). Expression of claudin-7 and -8 along the mouse nephron. Am. J. Physiol. Renal Physiol. 286, F1063-F1071.
    • (2004) Am. J. Physiol. Renal Physiol. , vol.286
    • Li, W.Y.1    Huey, C.L.2    Yu, A.S.3
  • 16
    • 0033766722 scopus 로고    scopus 로고
    • Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells
    • McCarthy, K. M., Francis, S. A., McCormack, J. M., Lai, J., Rogers, R. A., Skare, I. B., Lynch, R. D. and Schneeberger, E. E. (2000). Inducible expression of claudin-1-myc but not occludin-VSV-G results in aberrant tight junction strand formation in MDCK cells. J. Cell Sci. 113, 3387-3398.
    • (2000) J. Cell Sci. , vol.113 , pp. 3387-3398
    • McCarthy, K.M.1    Francis, S.A.2    McCormack, J.M.3    Lai, J.4    Rogers, R.A.5    Skare, I.B.6    Lynch, R.D.7    Schneeberger, E.E.8
  • 17
    • 0034388122 scopus 로고    scopus 로고
    • Occludin localization at the tight junction requires the second extracellular loop
    • Medina, R., Rahner, C., Mitic, L. L., Anderson, J. M. and Van Itallie, C. M. (2000). Occludin localization at the tight junction requires the second extracellular loop. J. Membr. Biol. 178, 235-247.
    • (2000) J. Membr. Biol. , vol.178 , pp. 235-247
    • Medina, R.1    Rahner, C.2    Mitic, L.L.3    Anderson, J.M.4    Van Itallie, C.M.5
  • 18
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated
    • Melkonian, K. A., Ostermeyer, A. G., Chen, J. Z., Roth, M. G. and Brown, D. A. (1999). Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274, 3910-3917.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 19
    • 0026327392 scopus 로고
    • An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes
    • Nabi, I. R., Le Bivic, A., Fambrough, D. and Rodriguez-Boulan, E. (1991). An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115, 1573-1584.
    • (1991) J. Cell Biol. , vol.115 , pp. 1573-1584
    • Nabi, I.R.1    Le Bivic, A.2    Fambrough, D.3    Rodriguez-Boulan, E.4
  • 23
    • 0035129369 scopus 로고    scopus 로고
    • Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut
    • Rahner, C., Mitic, L. L. and Anderson, J. M. (2001). Heterogeneity in expression and subcellular localization of claudins 2, 3, 4, and 5 in the rat liver, pancreas, and gut. Gastroenterology 120, 411-422.
    • (2001) Gastroenterology , vol.120 , pp. 411-422
    • Rahner, C.1    Mitic, L.L.2    Anderson, J.M.3
  • 26
    • 0031732763 scopus 로고    scopus 로고
    • Palmitoylation of human thyrotropin receptor: Slower intracellular trafficking of the palmitoylation-defective mutant
    • Tanaka, K., Nagayama, Y., Nishihara, E., Namba, H., Yamashita, S. and Niwa, M. (1998). Palmitoylation of human thyrotropin receptor: slower intracellular trafficking of the palmitoylation-defective mutant. Endocrinology 139, 803-806.
    • (1998) Endocrinology , vol.139 , pp. 803-806
    • Tanaka, K.1    Nagayama, Y.2    Nishihara, E.3    Namba, H.4    Yamashita, S.5    Niwa, M.6
  • 27
    • 0035013499 scopus 로고    scopus 로고
    • Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability
    • Van Itallie, C., Rahner, C. and Anderson, J. M. (2001). Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. J. Clin. Invest 107, 1319-1327.
    • (2001) J. Clin. Invest. , vol.107 , pp. 1319-1327
    • Van Itallie, C.1    Rahner, C.2    Anderson, J.M.3
  • 28
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion selective epithelial lines by expression of different claudins
    • Van Itallie, C. M., Fanning, A. S. and Anderson, J. M. (2003). Reversal of charge selectivity in cation or anion selective epithelial lines by expression of different claudins. Am. J. Physiol. Renal Physiol. 285, F1078-F1O84.
    • (2003) Am. J. Physiol. Renal Physiol. , vol.285
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 29
    • 0347052880 scopus 로고    scopus 로고
    • Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95
    • Wong, W. and Schlichter, L. C. (2004). Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95. J. Biol. Chem. 279, 444-452.
    • (2004) J. Biol. Chem. , vol.279 , pp. 444-452
    • Wong, W.1    Schlichter, L.C.2
  • 31
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • Yang, X., Claas, C., Kraeft, S. K., Chen, L. B., Wang, Z., Kreidberg, J. A. and Hemler, M. E. (2002). Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Mol. Biol. Cell 13, 767-781.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 767-781
    • Yang, X.1    Claas, C.2    Kraeft, S.K.3    Chen, L.B.4    Wang, Z.5    Kreidberg, J.A.6    Hemler, M.E.7
  • 32
    • 0037930880 scopus 로고    scopus 로고
    • Claudin-8 expression in MDCK cells augments the paracellular barrier to cation permeation
    • Yu, A. S., Enck, A. H., Lencer, W. I. and Schneeberger, E. E. (2003). Claudin-8 expression in MDCK cells augments the paracellular barrier to cation permeation. J. Biol. Chem. 278 17350-17359.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17350-17359
    • Yu, A.S.1    Enck, A.H.2    Lencer, W.I.3    Schneeberger, E.E.4
  • 33
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., Trible, R. P. and Samelson, L. E. (1998). LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9, 239-246.
    • (1998) Immunity , vol.9 , pp. 239-246
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3


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