메뉴 건너뛰기




Volumn 113, Issue 3, 2012, Pages 934-945

The hinge region of the scaffolding protein of cell contacts, zonula occludens protein 1, regulates interacting with various signaling proteins

Author keywords

Cell cell contacts; G proteins; Peptide binding assays; Protein protein interaction; Regulatory proteins; Surface plasmon resonance spectroscopy

Indexed keywords

ADRENALIN; CALCIUM CHANNEL; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA 12; GUANINE NUCLEOTIDE BINDING PROTEIN ALPHA I2; PROTEIN ZO1; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 84857611636     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.23422     Document Type: Article
Times cited : (9)

References (41)
  • 1
    • 33845212422 scopus 로고    scopus 로고
    • Normal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK protein
    • DOI 10.1128/MCB.01811-05
    • Adachi M, Inoko A, Hata M, Furuse K, Umeda K, Itoh M, Tsukita S. 2006. Normal establishment of epithelial tight junctions in mice and cultured cells lacking expression of ZO-3, a tight-junction MAGUK protein. Mol Cell Biol 26:9003-9015. (Pubitemid 44851957)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.23 , pp. 9003-9015
    • Adachi, M.1    Inoko, A.2    Hata, M.3    Furuse, K.4    Umeda, K.5    Itoh, M.6    Tsukita, S.7
  • 2
    • 27744493501 scopus 로고    scopus 로고
    • Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms
    • DOI 10.1016/j.biocel.2005.09.001, PII S1357272505002748
    • Andreeva AY, Piontek J, Blasig IE, Utepbergenov DI. 2006. Assembly of tight junction is regulated by the antagonism of conventional and novel protein kinase C isoforms. Int J Biochem Cell Biol 38:222-233. (Pubitemid 41619451)
    • (2006) International Journal of Biochemistry and Cell Biology , vol.38 , Issue.2 , pp. 222-233
    • Andreeva, A.Y.1    Piontek, J.2    Blasig, I.E.3    Utepbergenov, D.I.4
  • 3
    • 0030590868 scopus 로고    scopus 로고
    • The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain
    • DOI 10.1016/S0014-5793(96)01352-X, PII S001457939601352X
    • Balda MS, Anderson JM, Matter K. 1996. The SH3 domain of the tight junction protein ZO-1 binds to a serine protein kinase that phosphorylates a region C-terminal to this domain. FEBS Lett 399:326-332. (Pubitemid 26426876)
    • (1996) FEBS Letters , vol.399 , Issue.3 , pp. 326-332
    • Balda, M.S.1    Anderson, J.M.2    Matter, K.3
  • 4
    • 0034595219 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression
    • Balda MS, Matter K. 2000. The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. EMBO J 19:2024-2033. (Pubitemid 30237578)
    • (2000) EMBO Journal , vol.19 , Issue.9 , pp. 2024-2033
    • Balda, M.S.1    Matter, K.2
  • 5
    • 0039027605 scopus 로고    scopus 로고
    • Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin
    • DOI 10.1074/jbc.M905251199
    • Bazzoni G, Martinez-Estrada O, Orsenigo F, Cordenosi M, Citi S, Dejana E. 2000. Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. J Biol Chem 275:20520-20526. (Pubitemid 30457633)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20520-20526
    • Bazzoni, G.1    Martinez-Estrada, O.M.2    Orsenigo, F.3    Cordenonsi, M.4    Citi, S.5    Dejana, E.6
  • 6
    • 49149093447 scopus 로고    scopus 로고
    • The membrane association domain of RGS16 contains unique amphipathic features that are conserved in RGS4 and RGS5
    • Chen J, Pan L, Wei Z, Zhao Y, Zhang M. 2008. The membrane association domain of RGS16 contains unique amphipathic features that are conserved in RGS4 and RGS5. EMBO J 27:2113-2123.
    • (2008) EMBO J , vol.27 , pp. 2113-2123
    • Chen, J.1    Pan, L.2    Wei, Z.3    Zhao, Y.4    Zhang, M.5
  • 7
    • 9444225970 scopus 로고    scopus 로고
    • Enlargeosome, an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route
    • DOI 10.1091/mbc.E04-07-0577
    • Cocucci E, Racchetti G, Podini P, Rupnik M, Meldolesi J. 2004. Enlargeosome an exocytic vesicle resistant to nonionic detergents, undergoes endocytosis via a nonacidic route. Mol Biol Cell 15:5356-5368. (Pubitemid 39564730)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.12 , pp. 5356-5368
    • Cocucci, E.1    Racchetti, G.2    Podini, P.3    Rupnik, M.4    Meldolesi, J.5
  • 8
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • DOI 10.1529/biophysj.103.038422
    • Costes SV, Daelemans D, Cho EH, Dobbin Z, Pavlakis G, Lockett S. 2004. Automatic and quantitative measurement of protein-protein colocalization in live cells Biophys J 86:3993-4003. (Pubitemid 38780275)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3    Dobbin, Z.4    Pavlakis, G.5    Lockett, S.6
  • 9
    • 0029862538 scopus 로고    scopus 로고
    • Involvement of a heterotrimeric G protein α subunit in tight junction biogenesis
    • DOI 10.1074/jbc.271.42.25750
    • Denker BM, Saha C, Khawaja S, Nigam SK. 1996. Involvement of a heterotrimeric G protein a subunit in tight junction biogenesis. J Biol Chem 271:25750-25753. (Pubitemid 26347401)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 25750-25753
    • Denker, B.M.1    Saha, C.2    Khawaja, S.3    Nigam, S.K.4
  • 10
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • DOI 10.1074/jbc.273.45.29745
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson LM. 1998. The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273:29745-29753. (Pubitemid 28509986)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.45 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 11
    • 0036832157 scopus 로고    scopus 로고
    • Isolation and functional characterization of the actin-binding region in the tight junction protein ZO-1
    • Fanning AS, Ma TY, Anderson JM. 2002. Isolation and functional characterization of the actin-binding region in the tight junction protein ZO-1. FASEB J 16:1835-1837.
    • (2002) FASEB J , vol.16 , pp. 1835-1837
    • Fanning, A.S.1    Ma, T.Y.2    Anderson, J.M.3
  • 12
    • 33947133738 scopus 로고    scopus 로고
    • The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties
    • DOI 10.1091/mbc.E06-08-0764
    • Fanning AS, Little BP, Rahner C, Utepbergenov D, Walther Z, Anderson JM. 2007. The unique-5 and -6 motifs of ZO-1 regulate tight junction strand localization and scaffolding properties. Mol Biol Cell 18:721-731. (Pubitemid 46399480)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.3 , pp. 721-731
    • Fanning, A.S.1    Little, B.P.2    Rahner, C.3    Utepbergenov, D.4    Walther, Z.5    Anderson, J.M.6
  • 13
    • 0030329981 scopus 로고    scopus 로고
    • SPOT syn thesis: Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes
    • Frank R, Overwin H. 1996. SPOT synthesis: Epitope analysis with arrays of synthetic peptides prepared on cellulose membranes. Methods Mol Biol 66:149-169.
    • (1996) Methods Mol Biol , vol.66 , pp. 149-169
    • Frank, R.1    Overwin, H.2
  • 16
    • 0033580697 scopus 로고    scopus 로고
    • Differential involvement of G alpha(12) and G alpha(13) in receptor-mediated stress fiber formation
    • Gohla A, Offermanns S, Wilkie TM, Schultz G. 1999. Differential involvement of G alpha(12) and G alpha(13) in receptor-mediated stress fiber formation. J Biol Chem 274:17901-17907.
    • (1999) J Biol Chem , vol.274 , pp. 17901-17907
    • Gohla, A.1    Offermanns, S.2    Wilkie, T.M.3    Schultz, G.4
  • 17
    • 0032765048 scopus 로고    scopus 로고
    • Signaling from beta-adrenoceptor to L-type calcium channel: Identification of a novel cardiac protein kinase A target possessing similarities to AHNAK
    • Haase H, Podzuweit T, Lutsch G, Hohaus A, Kostka S, Lindschau C, Kott M, Kraft R, Morano I, 1999. Signaling from beta-adrenoceptor to L-type calcium channel: Identification of a novel cardiac protein kinase A target possessing similarities to AHNAK. FASEB J 13:2161-2172.
    • (1999) FASEB J , vol.13 , pp. 2161-2172
    • Haase, H.1    Podzuweit, T.2    Lutsch, G.3    Hohaus, A.4    Kostka, S.5    Lindschau, C.6    Kott, M.7    Kraft, R.8    Morano, I.9
  • 19
    • 33845563635 scopus 로고    scopus 로고
    • 2+ channel
    • DOI 10.1016/j.cardiores.2006.09.001, PII S0008636306004007
    • Haase H. 2007. Ahnak, a new player in beta-adrenergic regulation of the cardiac L-type Ca2+ channel Cardiovasc Res. 73:19-25. (Pubitemid 44937179)
    • (2007) Cardiovascular Research , vol.73 , Issue.1 , pp. 19-25
    • Haase, H.1
  • 20
    • 0036325857 scopus 로고    scopus 로고
    • 2+ channels and the actin-based cytoskeleton
    • DOI 10.1096/fj.01-0855com
    • Hohaus A, Person V, Behlke J, Schaper J, Morano I, Haase H. 2002. The carboxyl-terminal region of ahnak provides a link between cardiac Ltype Ca2+ channels and the actin-based cytoskeleton. FASEB J 16:1205-1216. (Pubitemid 34815408)
    • (2002) FASEB Journal , vol.16 , Issue.10 , pp. 1205-1216
    • Hohaus, A.1    Person, V.2    Behlke, J.3    Schaper, J.4    Morano, I.5    Haase, H.6
  • 21
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • DOI 10.1083/jcb.147.6.1351
    • Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. 1999. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2 and ZO-3, with the COOH termini of claudins. J Cell Biol 147:1351-1363. (Pubitemid 30012818)
    • (1999) Journal of Cell Biology , vol.147 , Issue.6 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 22
    • 84857564835 scopus 로고    scopus 로고
    • RGS5 is new a regulatory protein in tight junctions of endothelial cells is decreased in cerebral endothelial cells of SHRSP
    • Lippoldt A, Kirsch T, Rascher G, Kalbacher H, Wolburg H, Haller H. 2001. RGS5 is new a regulatory protein in tight junctions of endothelial cells is decreased in cerebral endothelial cells of SHRSP. Hypertension 38:964.
    • (2001) Hypertension , vol.38 , pp. 964
    • Lippoldt, A.1    Kirsch, T.2    Rascher, G.3    Kalbacher, H.4    Wolburg, H.5    Haller, H.6
  • 23
    • 77951613715 scopus 로고    scopus 로고
    • Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module
    • Lye MF, Fanning AS, Su Y, Anderson JM, Lavie A. 2010. Insights into regulated ligand binding sites from the structure of ZO-1 Src homology 3-guanylate kinase module. J Biol Chem 285:13907-13917.
    • (2010) J Biol Chem , vol.285 , pp. 13907-13917
    • Lye, M.F.1    Fanning, A.S.2    Su, Y.3    Anderson, J.M.4    Lavie, A.5
  • 24
    • 0033605143 scopus 로고    scopus 로고
    • Interaction of NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD- 95/SAP90: A possible regulatory role in molecular clustering at synaptic sites
    • DOI 10.1074/jbc.274.9.5782
    • Masuko N, Makino K, Kuwahara H, Fukunaga K, Sudo T, Araki N, Yamamoto H, Yamada Y, Miyamoto E, Saya H. 1999. Interaction of NE-dlg/SAP102, aneuronal and endocrine tissue-specific membrane-associated guanylate kinase protein, with calmodulin and PSD-95/SAP90-A possible regulatory role in molecular clustering at synaptic sites. J Biol Chem 274:5782-5790. (Pubitemid 29109234)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.9 , pp. 5782-5790
    • Masuko, N.1    Makino, K.2    Kuwahara, H.3    Fukunaga, K.4    Sudo, T.5    Araki, N.6    Yamamoto, H.7    Yamada, Y.8    Miyamoto, E.9    Saya, H.10
  • 25
    • 0035697173 scopus 로고    scopus 로고
    • Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins
    • DOI 10.1016/S1097-2765(01)00411-7
    • McGee AW, Dakoji SR, Olsen O, Bredt DS, Lim WA, Prehoda KE. 2001. Structure of the SH3-guanylate kinase module from PSD-95 suggests a mechanism for regulated assembly of MAGUK scaffolding proteins. Mol Cell 8:1291-1301. (Pubitemid 34085000)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1291-1301
    • McGee, A.W.1    Dakoji, S.R.2    Olsen, O.3    Bredt, D.S.4    Lim, W.A.5    Prehoda, K.E.6
  • 26
    • 0037067660 scopus 로고    scopus 로고
    • 12 directly binds to the Src homology 3 domain and regulates paracellular permeability in epithelial cells
    • DOI 10.1074/jbc.C200240200
    • Meyer TN, Schwesinger C, Denker BM. 2002. Zonula occludens-1 is a scaffolding protein for signaling molecules-G alpha(12) directly binds to the Src homology 3 domain and regulates paracellular permeability in epithelial cells. J Biol Chem 277:24855-24858. (Pubitemid 34951784)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 24855-24858
    • Meyer, T.N.1    Schwesinger, C.2    Denker, B.M.3
  • 27
    • 13544260880 scopus 로고    scopus 로고
    • The tight junction protein occludin and the adherens junction protein α-catenin share a common interaction mechanism with ZO-1
    • DOI 10.1074/jbc.M411365200
    • Mueller SL, Portwich M, Schmidt A, Utepbergenov DI, Huber O, Blasig IE, Krause G. 2005. The tight junction protein occludin and the adherens junction protein a-catenin share a common interaction mechanism with ZO-1. J Biol Chem 280:3747-3756. (Pubitemid 40223843)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3747-3756
    • Muller, S.L.1    Portwich, M.2    Schmidt, A.3    Utepbergenov, D.I.4    Huber, O.5    Blasig, I.E.6    Krause, G.7
  • 29
    • 33745967215 scopus 로고    scopus 로고
    • 2A- adrenergic receptor
    • DOI 10.1182/blood-2005-12-4835
    • Pozgajova M, Sachs UJH, Hein L, Nieswandt B. 2006. Reduced thrombus stability in mice lacking the alpha(2A)-adrenergic receptor. Blood 108:510-514. (Pubitemid 44061349)
    • (2006) Blood , vol.108 , Issue.2 , pp. 510-514
    • Pozgajova, M.1    Sachs, U.J.H.2    Hein, L.3    Nieswandt, B.4
  • 30
    • 78651392392 scopus 로고    scopus 로고
    • Synergistic Ca2+ responses by G{alpha}i-and G{alpha}q-coupled G-protein-coupled receptors require a single PLC{beta} isoform that is sensitive to both G{beta}{-gamma} and G{alpha}q
    • Rebres RA, Roach TI, Fraser ID, Philip F, Moon C, Lin KM, Liu J, Santat L, Cheadle L, Ross EM, Simon MI, Seaman WE. 2011. Synergistic Ca2+ responses by G{alpha}i-and G{alpha}q-coupled G-protein-coupled receptors require a single PLC{beta} isoform that is sensitive to both G{beta}{-gamma} and G{alpha}q. J Biol Chem 286:942-951.
    • (2011) J Biol Chem , vol.286 , pp. 942-951
    • Rebres, R.A.1    Roach, T.I.2    Fraser, I.D.3    Philip, F.4    Moon, C.5    Lin, K.M.6    Liu, J.7    Santat, L.8    Cheadle, L.9    Ross, E.M.10    Simon, M.I.11    Seaman, W.E.12
  • 31
    • 0032555295 scopus 로고    scopus 로고
    • Involvement of Gα(i2) in the maintenance and biogenesis of epithelial cell tight junctions
    • DOI 10.1074/jbc.273.34.21629
    • Saha C, Nigam SK, Denker BM. 1998. Involvement of G alpha(i2) in the maintenance and biogenesis of epithelial cell tight junctions. J Biol Chem 273:21629-21633. (Pubitemid 28405334)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.34 , pp. 21629-21633
    • Saha, C.1    Nigam, S.K.2    Denker, B.M.3
  • 34
    • 4644271738 scopus 로고    scopus 로고
    • 207 of claudin-5 is involved in size-selective loosening of the endothelial barrier by cyclic AMP
    • DOI 10.1016/j.yexcr.2004.07.012, PII S0014482704004045
    • Soma T, Chiba H, Kato-Mori Y, Wada T, Yamashita T, Kojima T, Sawada N. 2004. Thr207 of claudin-5 is involved in size-selective loosening of the endothelial barrier by cyclic AMP. Exp Cell Res 300:202-212. (Pubitemid 39286229)
    • (2004) Experimental Cell Research , vol.300 , Issue.1 , pp. 202-212
    • Soma, T.1    Chiba, H.2    Kato-Mori, Y.3    Wada, T.4    Yamashita, T.5    Kojima, T.6    Sawada, N.7
  • 35
    • 0035802119 scopus 로고    scopus 로고
    • Protein kinase B phosphorylates AHNAK and regulates its subcellular localization
    • DOI 10.1083/jcb.200105121
    • Sussman J, Stokoe D, Ossina N, Shtivelman E. 2001. Protein kinase B phosphorylates AHNAK and regulates its subcellular localization. J Cell Biol 154:1019-1030. (Pubitemid 34286181)
    • (2001) Journal of Cell Biology , vol.154 , Issue.5 , pp. 1019-1030
    • Sussman, J.1    Stokoe, D.2    Ossina, N.3    Shtivelman, E.4
  • 38
    • 33747686482 scopus 로고    scopus 로고
    • Dimerization of the scaffolding protein ZO-1 through the second PDZ domain
    • DOI 10.1074/jbc.M512820200
    • Utepbergenov DI, Fanning AS, Anderson JM. 2006. Dimerization of the scaffolding protein ZO-1 through the second PDZ domain. J Biol Chem 281:24671-24677. (Pubitemid 44274240)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.34 , pp. 24671-24677
    • Utepbergenov, D.I.1    Fanning, A.S.2    Anderson, J.M.3
  • 41
    • 0035895612 scopus 로고    scopus 로고
    • Characterization of RGS5 in regulation of G protein-coupled receptor signaling
    • DOI 10.1016/S0024-3205(01)00939-0, PII S0024320501009390
    • Zhou J, Moroi K, Nishiyama M, Usui H, Seki N, Ishida J, Fukamizu A, Kimura S. 2001. Characterization of RGS5 in regulation of G protein-coupled receptor signaling. Life Sci 68:1457-1469. (Pubitemid 32168073)
    • (2001) Life Sciences , vol.68 , Issue.13 , pp. 1457-1469
    • Zhou, J.1    Moroi, K.2    Nishiyama, M.3    Usui, H.4    Seki, N.5    Ishida, J.6    Fukamizu, A.7    Kimura, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.