메뉴 건너뛰기




Volumn 1257, Issue 1, 2012, Pages 103-107

Caveolin binds independently to claudin-2 and occludin

Author keywords

Caveolin; Claudin; Occluding; Tight junction; ZO 1

Indexed keywords

CAVEOLIN 1; CHOLESTEROL; CLAUDIN 2; CLAUDIN 4; OCCLUDIN; PROTEIN ZO1; PROTEIN ZO2;

EID: 84861969094     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2012.06535.x     Document Type: Article
Times cited : (22)

References (20)
  • 1
    • 0020972379 scopus 로고
    • Junction formation between cultured normal rat hepatocytes. An ultrastructural study on the presence of cholesterol and the structure of developing tight-junction strands
    • Feltkamp, C.A. & A.W. Van der Waerden. 1983. Junction formation between cultured normal rat hepatocytes. An ultrastructural study on the presence of cholesterol and the structure of developing tight-junction strands. J. Cell Sci. 63: 271-286.
    • (1983) J. Cell Sci. , vol.63 , pp. 271-286
    • Feltkamp, C.A.1    Van der Waerden, A.W.2
  • 2
    • 0034068866 scopus 로고    scopus 로고
    • Tight junctions are membrane microdomains
    • Nusrat, A. et al. 2000. Tight junctions are membrane microdomains. J. Cell Sci. 113: 1771-1781.
    • (2000) J. Cell Sci. , vol.113 , pp. 1771-1781
    • Nusrat, A.1
  • 3
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane
    • Lajoie, P. et al. 2009. Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J. Cell Biol. 185: 381-385.
    • (2009) J. Cell Biol. , vol.185 , pp. 381-385
    • Lajoie, P.1
  • 4
    • 34250800879 scopus 로고    scopus 로고
    • Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin
    • Lynch, R.D. et al. 2007. Cholesterol depletion alters detergent-specific solubility profiles of selected tight junction proteins and the phosphorylation of occludin. Exp. Cell Res. 313: 2597-2610.
    • (2007) Exp. Cell Res. , vol.313 , pp. 2597-2610
    • Lynch, R.D.1
  • 5
    • 17644421069 scopus 로고    scopus 로고
    • Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins
    • Lambert, D., C.A. O'Neill & P.J. Padfield. 2005. Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins. Biochem. J. 387: 553-560.
    • (2005) Biochem. J. , vol.387 , pp. 553-560
    • Lambert, D.1    O'Neill, C.A.2    Padfield, P.J.3
  • 6
    • 0037131313 scopus 로고    scopus 로고
    • Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME, restores normal microvascular permeability in Cav-1 null mice
    • Schubert, W. et al. 2002. Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-NAME, restores normal microvascular permeability in Cav-1 null mice. J. Biol. Chem. 277: 40091-40098.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40091-40098
    • Schubert, W.1
  • 7
    • 0037040994 scopus 로고    scopus 로고
    • Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities
    • Razani, B. et al. 2002. Caveolin-1-deficient mice are lean, resistant to diet-induced obesity, and show hypertriglyceridemia with adipocyte abnormalities. J. Biol. Chem. 277: 8635-8647.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8635-8647
    • Razani, B.1
  • 8
    • 24344457031 scopus 로고    scopus 로고
    • Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis
    • Shen, L. & J.R. Turner 2005. Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Mol. Biol. Cell. 16: 3919-3936.
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 3919-3936
    • Shen, L.1    Turner, J.R.2
  • 9
    • 77950585581 scopus 로고    scopus 로고
    • Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo
    • Marchiando, A.M. et al. 2010. Caveolin-1-dependent occludin endocytosis is required for TNF-induced tight junction regulation in vivo. J. Cell Biol. 189: 111-126.
    • (2010) J. Cell Biol. , vol.189 , pp. 111-126
    • Marchiando, A.M.1
  • 10
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M. et al. 1994. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127: 1617-1626.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1
  • 11
    • 67249084776 scopus 로고    scopus 로고
    • Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions
    • Fanning, A.S. & J.M. Anderson. 2009. Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann. N. Y. Acad. Sci. 1165: 113-120.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1165 , pp. 113-120
    • Fanning, A.S.1    Anderson, J.M.2
  • 12
    • 44149105668 scopus 로고    scopus 로고
    • The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state
    • Shen, L., C.R. Weber & Turner, J.R. 2008. The tight junction protein complex undergoes rapid and continuous molecular remodeling at steady state. J. Cell Biol. 181: 683-695.
    • (2008) J. Cell Biol. , vol.181 , pp. 683-695
    • Shen, L.1    Weber, C.R.2    Turner, J.R.3
  • 13
    • 79956202699 scopus 로고    scopus 로고
    • Occludin S408 phosphorylation regulates tight junction protein interactions and barrier function
    • Raleigh, D.R. et al. 2011. Occludin S408 phosphorylation regulates tight junction protein interactions and barrier function. J. Cell Biol. 193: 565-582.
    • (2011) J. Cell Biol. , vol.193 , pp. 565-582
    • Raleigh, D.R.1
  • 14
    • 59449086585 scopus 로고    scopus 로고
    • Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions
    • Elias, B.C. et al. 2009. Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions. J. Biol. Chem. 284: 1559-1569.
    • (2009) J. Biol. Chem. , vol.284 , pp. 1559-1569
    • Elias, B.C.1
  • 15
    • 79952800345 scopus 로고    scopus 로고
    • Claudin-2 forms homodimers and is a component of a high molecular weight protein complex
    • Van Itallie, C.M., L.L. Mitic & J.M. Anderson. 2011. Claudin-2 forms homodimers and is a component of a high molecular weight protein complex. J. Biol. Chem. 286: 3442-3450.
    • (2011) J. Biol. Chem. , vol.286 , pp. 3442-3450
    • Van Itallie, C.M.1    Mitic, L.L.2    Anderson, J.M.3
  • 16
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio, O.R. et al. 2003. Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am. J. Physiol. Cell Physiol. 284: C1346-1354.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Colegio, O.R.1
  • 17
    • 2942659788 scopus 로고    scopus 로고
    • The cytoplasmic tails of claudins can influence tight junction barrier properties through effects on protein stability
    • Van Itallie, C.M., O.R. Colegio & J.M. Anderson. 2004. The cytoplasmic tails of claudins can influence tight junction barrier properties through effects on protein stability. J. Memb. Biol. 199: 29-38.
    • (2004) J. Memb. Biol , vol.199 , pp. 29-38
    • Van Itallie, C.M.1    Colegio, O.R.2    Anderson, J.M.3
  • 18
    • 0030941001 scopus 로고    scopus 로고
    • Identification of Peptide and Protein Ligands for the Caveolin-scaffolding Domain
    • Couet, J. et al 1997. Identification of Peptide and Protein Ligands for the Caveolin-scaffolding Domain. J. Biol. Chem. 272: 6525-6533.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1
  • 19
    • 20444481707 scopus 로고    scopus 로고
    • Interferon-gamma induces internalization of epithelial tight junction proteins via a macropinocytosis-like process
    • Bruewer, M. et al. 2005. Interferon-gamma induces internalization of epithelial tight junction proteins via a macropinocytosis-like process. Faseb. J. 19: 923-933.
    • (2005) Faseb. J. , vol.19 , pp. 923-933
    • Bruewer, M.1
  • 20
    • 79958744418 scopus 로고    scopus 로고
    • Epidermal growth factor increases clathrin-dependent endocytosis and degradation of claudin-2 protein in MDCK II cells
    • Ikari, A. et al. 2011. Epidermal growth factor increases clathrin-dependent endocytosis and degradation of claudin-2 protein in MDCK II cells. J. Cell. Physiol. 226: 2448-2456.
    • (2011) J. Cell. Physiol. , vol.226 , pp. 2448-2456
    • Ikari, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.