메뉴 건너뛰기




Volumn 29, Issue 3, 2015, Pages 868-881

p18, a novel adaptor protein, regulates pulmonary endothelial barrier function via enhanced endocytic recycling of VE-cadherin

Author keywords

Adherens junction; Endocytosis; Endosome; Lung injury

Indexed keywords

GREEN FLUORESCENT PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MITOGEN ACTIVATED PROTEIN KINASE; MUTANT PROTEIN; PROTEIN P18; SMALL INTERFERING RNA; VASCULAR ENDOTHELIAL CADHERIN; CADHERIN; LEUKOCYTE ANTIGEN; LIPOPOLYSACCHARIDE; NME2 PROTEIN, MOUSE; NUCLEOSIDE DIPHOSPHATE KINASE NM23; PROTEIN TYROSINE KINASE; TYROSINE;

EID: 84937397602     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.14-257212     Document Type: Article
Times cited : (26)

References (51)
  • 5
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin)
    • Lampugnani, M. G., Corada, M., Caveda, L., Breviario, F., Ayalon, O., Geiger, B., and Dejana, E. (1995) The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, beta-catenin, and alpha-catenin with vascular endothelial cadherin (VE-cadherin). J. Cell Biol. 129, 203-217
    • (1995) J. Cell Biol. , vol.129 , pp. 203-217
    • Lampugnani, M.G.1    Corada, M.2    Caveda, L.3    Breviario, F.4    Ayalon, O.5    Geiger, B.6    Dejana, E.7
  • 7
    • 42449110795 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by the cadherin-catenin complex
    • Nelson, W. J. (2008) Regulation of cell-cell adhesion by the cadherin-catenin complex. Biochem. Soc. Trans. 36, 149-155
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 149-155
    • Nelson, W.J.1
  • 8
    • 65249178992 scopus 로고    scopus 로고
    • p120-catenin inhibits VE-cadherin internalization through a Rho-independent mechanism
    • Chiasson, C. M., Wittich, K. B., Vincent, P. A., Faundez, V., and Kowalczyk, A. P. (2009) p120-catenin inhibits VE-cadherin internalization through a Rho-independent mechanism. Mol. Biol. Cell 20, 1970-1980
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1970-1980
    • Chiasson, C.M.1    Wittich, K.B.2    Vincent, P.A.3    Faundez, V.4    Kowalczyk, A.P.5
  • 9
    • 0242708621 scopus 로고    scopus 로고
    • A core function for p120-catenin in cadherin turnover
    • Davis, M. A., Ireton, R. C., and Reynolds, A. B. (2003) A core function for p120-catenin in cadherin turnover. J. Cell Biol. 163, 525-534
    • (2003) J. Cell Biol. , vol.163 , pp. 525-534
    • Davis, M.A.1    Ireton, R.C.2    Reynolds, A.B.3
  • 15
    • 78651278017 scopus 로고    scopus 로고
    • Phosphorylation of VE-cadherin controls endothelial phenotypes via p120-catenin coupling and Rac1 activation
    • Hatanaka, K., Simons, M., and Murakami, M. (2011) Phosphorylation of VE-cadherin controls endothelial phenotypes via p120-catenin coupling and Rac1 activation. Am. J. Physiol. Heart Circ. Physiol. 300, H162-H172
    • (2011) Am. J. Physiol. Heart Circ. Physiol. , vol.300 , pp. H162-H172
    • Hatanaka, K.1    Simons, M.2    Murakami, M.3
  • 16
    • 33750529948 scopus 로고    scopus 로고
    • VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin
    • Gavard, J., and Gutkind, J. S. (2006) VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin. Nat. Cell Biol. 8, 1223-1234
    • (2006) Nat. Cell Biol. , vol.8 , pp. 1223-1234
    • Gavard, J.1    Gutkind, J.S.2
  • 17
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino, J. S., and Traub, L. M. (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 72, 395-447
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 18
    • 70350451708 scopus 로고    scopus 로고
    • A novel protein associated with membrane-type 1 matrix metalloproteinase binds p27(kip1) and regulates RhoA activation, actin remodeling, and matrigel invasion
    • Hoshino, D., Tomari, T., Nagano, M., Koshikawa, N., and Seiki, M. (2009) A novel protein associated with membrane-type 1 matrix metalloproteinase binds p27(kip1) and regulates RhoA activation, actin remodeling, and matrigel invasion. J. Biol. Chem. 284, 27315-27326
    • (2009) J. Biol. Chem. , vol.284 , pp. 27315-27326
    • Hoshino, D.1    Tomari, T.2    Nagano, M.3    Koshikawa, N.4    Seiki, M.5
  • 19
    • 84856228006 scopus 로고    scopus 로고
    • The late endosome/lysosome-anchored p18-mTORC1 pathway controls terminal maturation of lysosomes
    • Takahashi, Y., Nada, S., Mori, S., Soma-Nagae, T., Oneyama, C., and Okada, M. (2012) The late endosome/lysosome-anchored p18-mTORC1 pathway controls terminal maturation of lysosomes. Biochem. Biophys. Res. Commun. 417, 1151-1157
    • (2012) Biochem. Biophys. Res. Commun. , vol.417 , pp. 1151-1157
    • Takahashi, Y.1    Nada, S.2    Mori, S.3    Soma-Nagae, T.4    Oneyama, C.5    Okada, M.6
  • 20
    • 62049084764 scopus 로고    scopus 로고
    • The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes
    • Nada, S., Hondo, A., Kasai, A., Koike, M., Saito, K., Uchiyama, Y., and Okada, M. (2009) The novel lipid raft adaptor p18 controls endosome dynamics by anchoring the MEK-ERK pathway to late endosomes. EMBO J. 28, 477-489
    • (2009) EMBO J. , vol.28 , pp. 477-489
    • Nada, S.1    Hondo, A.2    Kasai, A.3    Koike, M.4    Saito, K.5    Uchiyama, Y.6    Okada, M.7
  • 21
    • 84883337775 scopus 로고    scopus 로고
    • The lysosomal signaling anchor p18/LAMTOR1 controls epidermal development by regulating lysosome-mediated catabolic processes
    • Soma-Nagae, T., Nada, S., Kitagawa, M., Takahashi, Y., Mori, S., Oneyama, C., and Okada, M. (2013) The lysosomal signaling anchor p18/LAMTOR1 controls epidermal development by regulating lysosome-mediated catabolic processes. J. Cell Sci. 126, 3575-3584
    • (2013) J. Cell Sci. , vol.126 , pp. 3575-3584
    • Soma-Nagae, T.1    Nada, S.2    Kitagawa, M.3    Takahashi, Y.4    Mori, S.5    Oneyama, C.6    Okada, M.7
  • 23
    • 73349090278 scopus 로고    scopus 로고
    • The G protein betagamma subunit mediates reannealing of adherens junctions to reverse endothelial permeability increase by thrombin
    • Knezevic, N., Tauseef, M., Thennes, T., and Mehta, D. (2009) The G protein betagamma subunit mediates reannealing of adherens junctions to reverse endothelial permeability increase by thrombin. J. Exp. Med. 206, 2761-2777
    • (2009) J. Exp. Med. , vol.206 , pp. 2761-2777
    • Knezevic, N.1    Tauseef, M.2    Thennes, T.3    Mehta, D.4
  • 24
    • 0032103369 scopus 로고    scopus 로고
    • In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism
    • Zhou, M. Y., Lo, S. K., Bergenfeldt, M., Tiruppathi, C., Jaffe, A., Xu, N., and Malik, A. B. (1998) In vivo expression of neutrophil inhibitory factor via gene transfer prevents lipopolysaccharide-induced lung neutrophil infiltration and injury by a beta2 integrin-dependent mechanism. J. Clin. Invest. 101, 2427-2437
    • (1998) J. Clin. Invest. , vol.101 , pp. 2427-2437
    • Zhou, M.Y.1    Lo, S.K.2    Bergenfeldt, M.3    Tiruppathi, C.4    Jaffe, A.5    Xu, N.6    Malik, A.B.7
  • 27
    • 77951212625 scopus 로고    scopus 로고
    • Src-induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers
    • Adam, A. P., Sharenko, A. L., Pumiglia, K., and Vincent, P. A. (2010) Src-induced tyrosine phosphorylation of VE-cadherin is not sufficient to decrease barrier function of endothelial monolayers. J. Biol. Chem. 285, 7045-7055
    • (2010) J. Biol. Chem. , vol.285 , pp. 7045-7055
    • Adam, A.P.1    Sharenko, A.L.2    Pumiglia, K.3    Vincent, P.A.4
  • 28
    • 84879088145 scopus 로고    scopus 로고
    • Arrestins as regulators of kinases and phosphatases
    • Luttrell, L. M., and Miller, W. E. (2013) Arrestins as regulators of kinases and phosphatases. Prog. Mol. Biol. Transl. Sci. 118, 115-147
    • (2013) Prog. Mol. Biol. Transl. Sci. , vol.118 , pp. 115-147
    • Luttrell, L.M.1    Miller, W.E.2
  • 29
    • 58149492762 scopus 로고    scopus 로고
    • Cell adhesion dynamics at endothelial junctions: VE-cadherin as a major player
    • Vestweber, D., Winderlich, M., Cagna, G., and Nottebaum, A. F. (2009) Cell adhesion dynamics at endothelial junctions: VE-cadherin as a major player. Trends Cell Biol. 19, 8-15
    • (2009) Trends Cell Biol. , vol.19 , pp. 8-15
    • Vestweber, D.1    Winderlich, M.2    Cagna, G.3    Nottebaum, A.F.4
  • 30
    • 78951469851 scopus 로고    scopus 로고
    • A p27(kip1)-binding protein, p27RF-Rho, promotes cancer metastasis via activation of RhoA and RhoC
    • Hoshino, D., Koshikawa, N., and Seiki, M. (2011) A p27(kip1)-binding protein, p27RF-Rho, promotes cancer metastasis via activation of RhoA and RhoC. J. Biol. Chem. 286, 3139-3148
    • (2011) J. Biol. Chem. , vol.286 , pp. 3139-3148
    • Hoshino, D.1    Koshikawa, N.2    Seiki, M.3
  • 34
    • 77249087643 scopus 로고    scopus 로고
    • Role of protein tyrosine phosphatase SHP2 in barrier function of pulmonary endothelium
    • Grinnell, K. L., Casserly, B., and Harrington, E. O. (2010) Role of protein tyrosine phosphatase SHP2 in barrier function of pulmonary endothelium. Am. J. Physiol. Lung Cell. Mol. Physiol. 298, L361-L370
    • (2010) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.298 , pp. L361-L370
    • Grinnell, K.L.1    Casserly, B.2    Harrington, E.O.3
  • 35
    • 84860523104 scopus 로고    scopus 로고
    • Protection against LPS-induced pulmonary edema through the attenuation of protein tyrosine phosphatase-1B oxidation
    • Grinnell, K. L., Chichger, H., Braza, J., Duong, H., and Harrington, E. O. (2012) Protection against LPS-induced pulmonary edema through the attenuation of protein tyrosine phosphatase-1B oxidation. Am. J. Respir. Cell Mol. Biol. 46, 623-632
    • (2012) Am. J. Respir. Cell Mol. Biol. , vol.46 , pp. 623-632
    • Grinnell, K.L.1    Chichger, H.2    Braza, J.3    Duong, H.4    Harrington, E.O.5
  • 36
    • 0028303390 scopus 로고
    • An improved setup for the isolated perfused rat lung
    • Uhlig, S., and Wollin, L. (1994) An improved setup for the isolated perfused rat lung. J. Pharmacol. Toxicol. Methods 31, 85-94
    • (1994) J. Pharmacol. Toxicol. Methods , vol.31 , pp. 85-94
    • Uhlig, S.1    Wollin, L.2
  • 37
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • Denizot, F., and Lang, R. (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89, 271-277
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 38
    • 84878393102 scopus 로고    scopus 로고
    • Effects of autocrine vascular endothelial growth factor (VEGF) in non-small cell lung cancer cell line A549
    • Wang, Y., Huang, L., Yang, Y., Xu, L., Yang, J., and Wu, Y. (2013) Effects of autocrine vascular endothelial growth factor (VEGF) in non-small cell lung cancer cell line A549. Mol. Biol. Rep. 40, 3093-3099
    • (2013) Mol. Biol. Rep. , vol.40 , pp. 3093-3099
    • Wang, Y.1    Huang, L.2    Yang, Y.3    Xu, L.4    Yang, J.5    Wu, Y.6
  • 41
    • 70349705635 scopus 로고    scopus 로고
    • Phosphorylation of caveolin-1 regulates oxidant-induced pulmonary vascular permeability via paracellular and transcellular pathways
    • Sun, Y., Hu, G., Zhang, X., and Minshall, R. D. (2009) Phosphorylation of caveolin-1 regulates oxidant-induced pulmonary vascular permeability via paracellular and transcellular pathways. Circ. Res. 105, 676-685
    • (2009) Circ. Res. , vol.105 , pp. 676-685
    • Sun, Y.1    Hu, G.2    Zhang, X.3    Minshall, R.D.4
  • 43
    • 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., Frank, P. G., Woodman, S. E., Hyogo, H., Cohen, D. E., Chow, C. W., and Lisanti, M. P. (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    Frank, P.G.2    Woodman, S.E.3    Hyogo, H.4    Cohen, D.E.5    Chow, C.W.6    Lisanti, M.P.7
  • 45
    • 0036094927 scopus 로고    scopus 로고
    • A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex
    • Nichols, B. J. (2002) A distinct class of endosome mediates clathrin-independent endocytosis to the Golgi complex. Nat. Cell Biol. 4, 374-378
    • (2002) Nat. Cell Biol. , vol.4 , pp. 374-378
    • Nichols, B.J.1
  • 48
    • 11144296871 scopus 로고    scopus 로고
    • Lysosomal targeting of E-cadherin: A unique mechanism for the down-regulation of cell-cell adhesion during epithelial to mesenchymal transitions
    • Palacios, F., Tushir, J. S., Fujita, Y., and D'Souza-Schorey, C. (2005) Lysosomal targeting of E-cadherin: a unique mechanism for the down-regulation of cell-cell adhesion during epithelial to mesenchymal transitions. Mol. Cell. Biol. 25, 389-402
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 389-402
    • Palacios, F.1    Tushir, J.S.2    Fujita, Y.3    D'Souza-Schorey, C.4
  • 49
    • 48049094159 scopus 로고    scopus 로고
    • The role of adherens junctions and VE-cadherin in the control of vascular permeability
    • Dejana, E., Orsenigo, F., and Lampugnani, M. G. (2008) The role of adherens junctions and VE-cadherin in the control of vascular permeability. J. Cell Sci. 121, 2115-2122
    • (2008) J. Cell Sci. , vol.121 , pp. 2115-2122
    • Dejana, E.1    Orsenigo, F.2    Lampugnani, M.G.3
  • 50
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach, A., Louvard, D., and Coudrier, E. (1996) Actin filaments facilitate two steps of endocytosis. J. Cell Sci. 109, 457-465
    • (1996) J. Cell Sci. , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.