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Volumn 24, Issue 18, 2013, Pages 2849-2860

JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; AFADIN; CLAUDIN; GUANOSINE TRIPHOSPHATASE; JUNCTIONAL ADHESION MOLECULE A; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN PDZ GEF1; PROTEIN RAP2C; PROTEIN ZO2; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 84884469619     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-06-0298     Document Type: Article
Times cited : (109)

References (62)
  • 2
    • 27144489108 scopus 로고    scopus 로고
    • Protein database searches using compositionally adjusted substitution matrices
    • DOI 10.1111/j.1742-4658.2005.04945.x
    • Altschul SF, Wootton JC, Gertz EM, Agarwala R, Morgulis A, Schäffer AA, Yu Y-K (2005). Protein database searches using compositionally adjusted substitution matrices. FEBS J 272, 5101-5109. (Pubitemid 41503143)
    • (2005) FEBS Journal , vol.272 , Issue.20 , pp. 5101-5109
    • Altschul, S.F.1    Wootton, J.C.2    Gertz, E.M.3    Agarwala, R.4    Morgulis, A.5    Schaffer, A.A.6    Yu, Y.-K.7
  • 3
    • 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, Martínez-Estrada O, Orsenigo F, Cordenonsi 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
  • 4
    • 3242705077 scopus 로고    scopus 로고
    • RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin
    • DOI 10.1152/ajpcell.00087.2004
    • Bruewer M, Hopkins AM, Hobert ME, Nusrat A, Madara JL (2004). RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin. Am J Physiol Cell Physiol 287, C327-C335. (Pubitemid 38955223)
    • (2004) American Journal of Physiology - Cell Physiology , vol.287 , Issue.2
    • Bruewer, M.1    Hopkins, A.M.2    Hobert, M.E.3    Nusrat, A.4    Madara, J.L.5
  • 6
    • 0038701734 scopus 로고    scopus 로고
    • Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture
    • Colegio OR, Van Itallie C, Rahner C, Anderson JM (2003). Claudin extracellular domains determine paracellular charge selectivity and resistance but not tight junction fibril architecture. Am J Physiol Cell Physiol C1346-C1354. (Pubitemid 36583375)
    • (2003) American Journal of Physiology - Cell Physiology , vol.284 , Issue.6
    • Colegio, O.R.1    Van Itallie, C.2    Rahner, C.3    Anderson, J.M.4
  • 8
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K, Schulz C, Brickwedde MZ, Pendl GG, Vestweber D (2000). Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem 275, 27979-27988.
    • (2000) J Biol Chem , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.2    Brickwedde, M.Z.3    Pendl, G.G.4    Vestweber, D.5
  • 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 JM (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
    • 84863116784 scopus 로고    scopus 로고
    • Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia
    • Fanning AS, Van Itallie CM, Anderson JM (2012). Zonula occludens-1 and -2 regulate apical cell structure and the zonula adherens cytoskeleton in polarized epithelia. Mol Biol Cell 23, 577-590.
    • (2012) Mol Biol Cell , vol.23 , pp. 577-590
    • Fanning, A.S.1    Van Itallie, C.M.2    Anderson, J.M.3
  • 12
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • DOI 10.1083/jcb.141.7.1539
    • Furuse M (1998). Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 141, 1539-1550. (Pubitemid 28309169)
    • (1998) Journal of Cell Biology , vol.141 , Issue.7 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 13
    • 77952756845 scopus 로고    scopus 로고
    • Molecular basis of the core structure of tight junctions
    • Furuse M (2010). Molecular basis of the core structure of tight junctions. Cold Spring Harb Perspect Biol 2, a002907-a002907.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Furuse, M.1
  • 18
    • 34247092058 scopus 로고    scopus 로고
    • ZO-2 silencing in epithelial cells perturbs the gate and fence function of tight junctions and leads to an atypical monolayer architecture
    • Hernandez S, Munguia BC, González-Mariscal L (2007). ZO-2 silencing in epithelial cells perturbs the gate and fence function of tight junctions and leads to an atypical monolayer architecture. Exp Cell Res 313, 15-15.
    • (2007) Exp Cell Res , vol.313 , pp. 15-15
    • Hernandez, S.1    Munguia, B.C.2    González-Mariscal, L.3
  • 19
    • 0035971219 scopus 로고    scopus 로고
    • Regulation of tight junction permeability and occludin phosphorylation by RhoA-p160ROCK-dependent and -independent mechanisms
    • Hirase T, Kawashima S, Wong EYM, Ueyama T, Rikitake Y, Tsukita S, Yokoyama M, Staddon JM (2001). Regulation of tight junction permeability and occludin phosphorylation by RhoA-p160ROCK-dependent and -independent mechanisms. J Biol Chem 276, 10423-10431.
    • (2001) J Biol Chem , vol.276 , pp. 10423-10431
    • Hirase, T.1    Kawashima, S.2    Wong, E.Y.M.3    Ueyama, T.4    Rikitake, Y.5    Tsukita, S.6    Yokoyama, M.7    Staddon, J.M.8
  • 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
    • 39849103291 scopus 로고    scopus 로고
    • A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions
    • Ivanov AI, Bachar M, Babbin BA, Adelstein RS, Nusrat A, Parkos CA (2007). A unique role for nonmuscle myosin heavy chain IIA in regulation of epithelial apical junctions. PLoS One 2, e658.
    • (2007) PLoS One , vol.2
    • Ivanov, A.I.1    Bachar, M.2    Babbin, B.A.3    Adelstein, R.S.4    Nusrat, A.5    Parkos, C.A.6
  • 23
    • 0032514134 scopus 로고    scopus 로고
    • Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases
    • DOI 10.1083/jcb.142.1.101
    • Jou T-S, Schneeberger EE, Nelson WJ (1998). Structural and functional regulation of tight junctions by RhoA and Rac1 small GTPases. J Cell Biol 142, 101-115. (Pubitemid 28341143)
    • (1998) Journal of Cell Biology , vol.142 , Issue.1 , pp. 101-115
    • Jou, T.-S.1    Schneeberger, E.E.2    Nelson, W.J.3
  • 24
    • 84866523733 scopus 로고    scopus 로고
    • Compromised intestinal epithelial barrier induces adaptive immune compensation that protects from colitis
    • Khounlotham M et al. (2012). Compromised intestinal epithelial barrier induces adaptive immune compensation that protects from colitis. Immunity 37, 563-573.
    • (2012) Immunity , vol.37 , pp. 563-573
    • Khounlotham, M.1
  • 25
    • 58149263468 scopus 로고    scopus 로고
    • Structure of reovirus sigma1 in complex with its receptor junctional adhesion molecule-A
    • Kirchner E, Guglielmi KM, Strauss HM, Dermody TS, Stehle T (2008). Structure of reovirus sigma1 in complex with its receptor junctional adhesion molecule-A. PLoS Pathog 4, e1000235.
    • (2008) PLoS Pathog , vol.4
    • Kirchner, E.1    Guglielmi, K.M.2    Strauss, H.M.3    Dermody, T.S.4    Stehle, T.5
  • 27
    • 33846847701 scopus 로고    scopus 로고
    • Rap1: A key regulator in cell-cell junction formation
    • DOI 10.1242/jcs.03306
    • Kooistra M, Dube N, Bos J (2007). Rap1: a key regulator in cell-cell junction formation. J Cell Sci 120, 17-22. (Pubitemid 46206645)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 17-22
    • Kooistra, M.R.H.1    Dube, N.2    Bos, J.L.3
  • 30
    • 37549038994 scopus 로고    scopus 로고
    • JAM-A regulates permeability and inflammation in the intestine in vivo
    • Laukoetter MG et al. (2007). JAM-A regulates permeability and inflammation in the intestine in vivo. J Exp Med 204, 3067-3076.
    • (2007) J Exp Med , vol.204 , pp. 3067-3076
    • Laukoetter, M.G.1
  • 31
    • 0033639244 scopus 로고    scopus 로고
    • Characterization of huJAM: Evidence for involvement in cell-cell contact and tight junction regulation
    • Liang TW et al. (2000). Characterization of huJAM: evidence for involvement in cell-cell contact and tight junction regulation. Am J Physiol Cell Physiol 279, C1733-C1743.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Liang, T.W.1
  • 33
    • 0023510866 scopus 로고
    • Structural basis for physiological regulation of paracellular pathways in intestinal epithelia
    • Madara JL, Pappenheimer JR (1987). Structural basis for physiological regulation of paracellular pathways in intestinal epithelia. J Membrane Biol 100, 149-164. (Pubitemid 18004072)
    • (1987) Journal of Membrane Biology , vol.100 , Issue.2 , pp. 149-164
    • Madara, J.L.1    Pappenheimer, J.R.2
  • 35
    • 1942501686 scopus 로고    scopus 로고
    • Involvement of the Junctional Adhesion Molecule-1 (JAM1) Homodimer Interface in Regulation of Epithelial Barrier Function
    • DOI 10.1074/jbc.M309483200
    • Mandell KJ, McCall IC, Parkos CA (2004). Involvement of the junctional adhesion molecule-1 (JAM1) homodimer interface in regulation of epithelial barrier function. J Biol Chem 279, 16254-16262. (Pubitemid 38509319)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16254-16262
    • Mandell, K.J.1    McCall, I.C.2    Parkos, C.A.3
  • 36
    • 1842425828 scopus 로고    scopus 로고
    • The Rap GTPases Regulate Integrin-mediated Adhesion, Cell Spreading, Actin Polymerization, and Pyk2 Tyrosine Phosphorylation in B Lymphocytes
    • DOI 10.1074/jbc.M313098200
    • McLeod SJ, Shum AJ, Lee RL, Takei F, Gold MR (2004). The Rap GTPases regulate integrin-mediated adhesion, cell spreading, actin polymerization, and Pyk2 tyrosine phosphorylation in B lymphocytes. J Biol Chem 279, 12009-12019. (Pubitemid 38445762)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12009-12019
    • McLeod, S.J.1    Shum, A.J.2    Lee, R.L.3    Takei, F.4    Gold, M.R.5
  • 37
    • 69949168324 scopus 로고    scopus 로고
    • Regulation by afadin of cyclical activation and inactivation of Rap1, Rac1, and RhoA small G proteins at leading edges of moving NIH3T3 cells
    • Miyata M, Rikitake Y, Takahashi M, Nagamatsu Y, Yamauchi Y, Ogita H, Hirata K-I, Takai Y (2009). Regulation by afadin of cyclical activation and inactivation of Rap1, Rac1, and RhoA small G proteins at leading edges of moving NIH3T3 cells. J Biol Chem 284, 24595-24609.
    • (2009) J Biol Chem , vol.284 , pp. 24595-24609
    • Miyata, M.1    Rikitake, Y.2    Takahashi, M.3    Nagamatsu, Y.4    Yamauchi, Y.5    Ogita, H.6    Hirata, K.-I.7    Takai, Y.8
  • 38
    • 84861970173 scopus 로고    scopus 로고
    • Intracellular mediators of JAM-A-dependent epithelial barrier function
    • Monteiro AC, Parkos CA (2012). Intracellular mediators of JAM-A-dependent epithelial barrier function. Ann NY Acad Sci 1257, 115-124.
    • (2012) Ann NY Acad Sci , vol.1257 , pp. 115-124
    • Monteiro, A.C.1    Parkos, C.A.2
  • 39
    • 79953312227 scopus 로고    scopus 로고
    • JAM-A regulates epithelial proliferation through Akt/β-catenin signalling
    • Nava P et al. (2011). JAM-A regulates epithelial proliferation through Akt/β-catenin signalling. EMBO Rep 12, 314-320.
    • (2011) EMBO Rep , vol.12 , pp. 314-320
    • Nava, P.1
  • 41
    • 76649106741 scopus 로고    scopus 로고
    • Vascular endothelial-cadherin stabilizes at cell-cell junctions by anchoring to circumferential actin bundles through alpha- and beta-catenins in cyclic AMP-Epac-Rap1 signal-activated endothelial cells
    • Noda K, Zhang J, Fukuhara S, Kunimoto S, Yoshimura M, Mochizuki N (2010). Vascular endothelial-cadherin stabilizes at cell-cell junctions by anchoring to circumferential actin bundles through alpha- and beta-catenins in cyclic AMP-Epac-Rap1 signal-activated endothelial cells. Mol Biol Cell 21, 584-596.
    • (2010) Mol Biol Cell , vol.21 , pp. 584-596
    • Noda, K.1    Zhang, J.2    Fukuhara, S.3    Kunimoto, S.4    Yoshimura, M.5    Mochizuki, N.6
  • 42
    • 83355174042 scopus 로고    scopus 로고
    • The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1
    • Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM, Lavie A (2011). The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. J Biol Chem 286, 43352-43360.
    • (2011) J Biol Chem , vol.286 , pp. 43352-43360
    • Nomme, J.1    Fanning, A.S.2    Caffrey, M.3    Lye, M.F.4    Anderson, J.M.5    Lavie, A.6
  • 44
    • 0033672942 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: Nutrients, cytokines, and immune cells
    • Nusrat A, Turner JR, Madara JL (2000). Molecular physiology and pathophysiology of tight junctions. IV. Regulation of tight junctions by extracellular stimuli: nutrients, cytokines, and immune cells. Am J Physiol Gastrointest Liver Physiol 279, G851-G857.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Nusrat, A.1    Turner, J.R.2    Madara, J.L.3
  • 45
    • 80053262749 scopus 로고    scopus 로고
    • Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control
    • Pannekoek W-J et al. (2011). Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction control. Cell Signal 23, 2056-2064.
    • (2011) Cell Signal , vol.23 , pp. 2056-2064
    • Pannekoek, W.-J.1
  • 50
    • 51149109597 scopus 로고    scopus 로고
    • Constitutively active Rap2 transgenic mice display fewer dendritic spines, reduced extracellular signal-regulated kinase signaling, enhanced long-term depression, and impaired spatial learning and fear extinction
    • Ryu J, Futai K, Feliu M, Weinberg R, Sheng M (2008). Constitutively active Rap2 transgenic mice display fewer dendritic spines, reduced extracellular signal-regulated kinase signaling, enhanced long-term depression, and impaired spatial learning and fear extinction. J Neurosci 28, 8178-8188.
    • (2008) J Neurosci , vol.28 , pp. 8178-8188
    • Ryu, J.1    Futai, K.2    Feliu, M.3    Weinberg, R.4    Sheng, M.5
  • 52
    • 65249125248 scopus 로고    scopus 로고
    • Junctional adhesion molecule A interacts with afadin and PDZ-GEF2 to activate Rap1A, regulate b1 integrin levels, and enhance cell migration
    • Severson EA, Lee WY, Capaldo CT, Nusrat A, Parkos CA (2009). Junctional adhesion molecule A interacts with afadin and PDZ-GEF2 to activate Rap1A, regulate b1 integrin levels, and enhance cell migration. Mol Biol Cell 20, 1916-1925.
    • (2009) Mol Biol Cell , vol.20 , pp. 1916-1925
    • Severson, E.A.1    Lee, W.Y.2    Capaldo, C.T.3    Nusrat, A.4    Parkos, C.A.5
  • 55
    • 0031648724 scopus 로고    scopus 로고
    • Direct binding between two PDZ domain proteins canoe and ZO-1 and their roles in regulation of the Jun N-terminal kinase pathway in Drosophila morphogenesis
    • DOI 10.1016/S0925-4773(98)00151-8, PII S0925477398001518
    • Takahashi K, Matsuo T, Katsube T, Ueda R, Yamamoto D (1998). Direct binding between two PDZ domain proteins Canoe and ZO-1 and their roles in regulation of the Jun N-terminal kinase pathway in Drosophila morphogenesis. Mech Dev 78, 97-111. (Pubitemid 28566216)
    • (1998) Mechanisms of Development , vol.78 , Issue.1-2 , pp. 97-111
    • Takahashi, K.1    Matsuo, T.2    Katsube, T.3    Ueda, R.4    Yamamoto, D.5
  • 57
    • 77953444708 scopus 로고    scopus 로고
    • Downregulation of Rap1GAP in human tumor cells alters cell/matrix and cell/cell adhesion
    • Tsygankova O, Ma C, Tang W, Korch C, Meinkoth J (2010). Downregulation of Rap1GAP in human tumor cells alters cell/matrix and cell/cell adhesion. Mol Cell Biol 30, 3262-3274.
    • (2010) Mol Cell Biol , vol.30 , pp. 3262-3274
    • Tsygankova, O.1    Ma, C.2    Tang, W.3    Korch, C.4    Meinkoth, J.5
  • 58
    • 0242665742 scopus 로고    scopus 로고
    • Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins
    • Van Itallie CM, Fanning AS, Anderson JM (2003). Reversal of charge selectivity in cation or anion-selective epithelial lines by expression of different claudins. Am J Physiol Renal Physiol 285, F1078-F1084. (Pubitemid 37421043)
    • (2003) American Journal of Physiology - Renal Physiology , vol.285 , Issue.6
    • Van Itallie, C.M.1    Fanning, A.S.2    Anderson, J.M.3
  • 59
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • Van Itallie CM, Fanning AS, Bridges A, Anderson JM (2009). ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton. Mol Biol Cell 20, 3930-3940.
    • (2009) Mol Biol Cell , vol.20 , pp. 3930-3940
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 62
    • 77749255549 scopus 로고    scopus 로고
    • Investigation of the binding preference of reovirus sigma1 for junctional adhesion molecule A by classical and steered molecular dynamics
    • Zhang B, Lim TS, Vedula SRK, Li A, Lim CT, Tan VBC (2010). Investigation of the binding preference of reovirus sigma1 for junctional adhesion molecule A by classical and steered molecular dynamics. Biochemistry 49, 1776-1786.
    • (2010) Biochemistry , vol.49 , pp. 1776-1786
    • Zhang, B.1    Lim, T.S.2    Vedula, S.R.K.3    Li, A.4    Lim, C.T.5    Tan, V.B.C.6


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