메뉴 건너뛰기




Volumn 123, Issue 14, 2010, Pages 2434-2443

NHE3 mobility in brush borders increases upon NHERF2-dependent stimulation by lyophosphatidic acid

Author keywords

Brush border; Cytoskeleton; Exocytosis; FRAP; FRET; NHE3; NHERF2

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ACTIN; EZRIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LYSOPHOSPHATIDIC ACID; MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN NHERF2; SODIUM PROTON EXCHANGE PROTEIN 3; UNCLASSIFIED DRUG;

EID: 77954938862     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.056713     Document Type: Article
Times cited : (21)

References (38)
  • 2
    • 33744810075 scopus 로고    scopus 로고
    • Na+/H+ exchangers and the regulation of volume
    • Alexander, R. T. and Grinstein, S. (2006). Na+/H+ exchangers and the regulation of volume. Acta Physiol. (Oxf) 187, 159-167.
    • (2006) Acta Physiol. (Oxf) , vol.187 , pp. 159-167
    • Alexander, R.T.1    Grinstein, S.2
  • 6
    • 46749118449 scopus 로고    scopus 로고
    • The epithelial brush border Na+/H+ exchanger NHE3 associates with the actin cytoskeleton by binding to ezrin directly and via PDZ domaincontaining Na+/H+ exchanger regulatory factor (NHERF) proteins
    • Cha, B. and Donowitz, M. (2008). The epithelial brush border Na+/H+ exchanger NHE3 associates with the actin cytoskeleton by binding to ezrin directly and via PDZ domaincontaining Na+/H+ exchanger regulatory factor (NHERF) proteins. Clin. Exp. Pharmacol. Physiol. 35, 863-871.
    • (2008) Clin. Exp. Pharmacol. Physiol. , vol.35 , pp. 863-871
    • Cha, B.1    Donowitz, M.2
  • 7
    • 4344578072 scopus 로고    scopus 로고
    • The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP
    • DOI 10.1242/jcs.01180
    • Cha, B., Kenworthy, A., Murtazina, R. and Donowitz, M. (2004). The lateral mobility of NHE3 on the apical membrane of renal epithelial OK cells is limited by the PDZ domain proteins NHERF1/2, but is dependent on an intact actin cytoskeleton as determined by FRAP. J. Cell Sci. 117, 3353-3365. (Pubitemid 39139919)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3353-3365
    • Cha, B.1    Kenworthy, A.2    Murtazina, R.3    Donowitz, M.4
  • 8
    • 20444441935 scopus 로고    scopus 로고
    • CGMP inhibition of Na+/H+ antiporter 3 (NHE3) requires PDZ domain adapter NHERF2, a broad specificity protein kinase G-anchoring protein
    • Cha, B., Kim, J. H., Hut, H., Hogema, B. M., Nadarja, J., Zizak, M., Cavet, M., Lee-Kwon, W., Lohmann, S. M., Smolenski, A. et al. (2005). cGMP inhibition of Na+/H+ antiporter 3 (NHE3) requires PDZ domain adapter NHERF2, a broad specificity protein kinase G-anchoring protein. J. Biol. Chem. 280, 16642-16650.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16642-16650
    • Cha, B.1    Kim, J.H.2    Hut, H.3    Hogema, B.M.4    Nadarja, J.5    Zizak, M.6    Cavet, M.7    Lee-Kwon, W.8    Lohmann, S.M.9    Smolenski, A.10
  • 9
    • 33744779069 scopus 로고    scopus 로고
    • The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: Dual role in NHE3 trafficking and mobility in the brush border
    • DOI 10.1091/mbc.E05-09-0843
    • Cha, B., Tse, M., Yun, C., Kovbasnjuk, O., Mohan, S., Hubbard, A., Arpin, M. and Donowitz, M. (2006). The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: dual role in NHE3 trafficking and mobility in the brush border. Mol. Biol. Cell 17, 2661-2673. (Pubitemid 43825503)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.6 , pp. 2661-2673
    • Cha, B.1    Tse, M.2    Yun, C.3    Kovbasnjuk, O.4    Mohan, S.5    Hubbard, A.6    Arpin, M.7    Donowitz, M.8
  • 10
    • 3042662335 scopus 로고    scopus 로고
    • Lysophosphatidic acid induces exocytic trafficking of Na(+)/H(+) exchanger 3 by E3KARP-dependent activation of phospholipase C
    • Choi, J. W., Lee-Kwon, W., Jeon, E. S., Kang, Y. J., Kawano, K., Kim, H. S., Suh, P. G., Donowitz, M. and Kim, J. H. (2004). Lysophosphatidic acid induces exocytic trafficking of Na(+)/H(+) exchanger 3 by E3KARP-dependent activation of phospholipase C. Biochim. Biophys. Acta 1683, 59-68.
    • (2004) Biochim. Biophys. Acta , vol.1683 , pp. 59-68
    • Choi, J.W.1    Lee-Kwon, W.2    Jeon, E.S.3    Kang, Y.J.4    Kawano, K.5    Kim, H.S.6    Suh, P.G.7    Donowitz, M.8    Kim, J.H.9
  • 11
    • 0033669622 scopus 로고    scopus 로고
    • Lysophosphatidic acid receptors
    • Contos, J. J., Ishii, I. and Chun, J. (2000). Lysophosphatidic acid receptors. Mol. Pharmacol. 58, 1188-1196.
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1188-1196
    • Contos, J.J.1    Ishii, I.2    Chun, J.3
  • 12
    • 34447629085 scopus 로고    scopus 로고
    • Regulatory binding partners and complexes of NHE3
    • DOI 10.1152/physrev.00030.2006
    • Donowitz, M. and Li, X. (2007). Regulatory binding partners and complexes of NHE3. Physiol. Rev. 87, 825-872. (Pubitemid 47086280)
    • (2007) Physiological Reviews , vol.87 , Issue.3 , pp. 825-872
    • Donowitz, M.1    Li, X.2
  • 13
    • 0034525593 scopus 로고    scopus 로고
    • Short-term regulation of NHE3 by EGF and protein kinase C but not protein kinase a involves vesicle trafficking in epithelial cells and fibroblasts
    • Donowitz, M., Janecki, A., Akhter, S., Cavet, M. E., Sanchez, F., Lamprecht, G., Zizak, M., Kwon, W. L., Khurana, S., Yun, C. H. et al. (2000). Short-term regulation of NHE3 by EGF and protein kinase C but not protein kinase A involves vesicle trafficking in epithelial cells and fibroblasts. Ann. NY Acad. Sci. 915, 30-42.
    • (2000) Ann. NY Acad. Sci. , vol.915 , pp. 30-42
    • Donowitz, M.1    Janecki, A.2    Akhter, S.3    Cavet, M.E.4    Sanchez, F.5    Lamprecht, G.6    Zizak, M.7    Kwon, W.L.8    Khurana, S.9    Yun, C.H.10
  • 15
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • DOI 10.1083/jcb.138.6.1193
    • Ellenberg, J., Siggia, E. D., Moreira, J. E., Smith, C. L., Presley, J. F., Worman, H. J. and Lipincott-Schwartz, J. (1997). Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase ansd mitosis. J. Cell Biol. 138, 1193-1206. (Pubitemid 27415047)
    • (1997) Journal of Cell Biology , vol.138 , Issue.6 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 16
    • 0033153381 scopus 로고    scopus 로고
    • ++ of human adult vascular smooth muscle cells in culture
    • DOI 10.1016/S0049-3848(99)00004-3, PII S0049384899000043
    • Gennero, I., Xuereb, J. M., Simon, M. F., Girolami, J. P., Bascands, J. L., Chap, H., Boneu, B. and Sie, P. (1999). Effects of lysophosphatidic acid on proliferation and cytosolic Ca++ of human adult vascular smooth muscle cells in culture. Thromb. Res. 94, 317-326. (Pubitemid 29268350)
    • (1999) Thrombosis Research , vol.94 , Issue.5 , pp. 317-326
    • Gennero, I.1    Xuereb, J.-M.2    Simon, M.-F.3    Girolami, J.-P.4    Bascands, J.-L.5    Chap, H.6    Boneu, B.7    Sie, P.8
  • 17
    • 1242317020 scopus 로고    scopus 로고
    • Increased diffusional mobility of CFTR at the plasma membrane after deletion of its C-terminal PDZ binding motif
    • Haggie, P. M., Stanton, B. A. and Verkman, A. S. (2004). Increased diffusional mobility of CFTR at the plasma membrane after deletion of its C-terminal PDZ binding motif. J. Biol. Chem. 279, 5494-5500.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5494-5500
    • Haggie, P.M.1    Stanton, B.A.2    Verkman, A.S.3
  • 19
    • 0034677953 scopus 로고    scopus 로고
    • + exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase
    • DOI 10.1074/jbc.275.11.8133
    • Janecki, A. J., Janecki, M., Akhter, S. and Donowitz, M. (2000). Basic fibroblast growth factor stimulates surface expression and activity of Na(+)/H(+) exchanger NHE3 via mechanism involving phosphatidylinositol 3-kinase. J. Biol. Chem. 275, 8133-8142. (Pubitemid 30159728)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 8133-8142
    • Janecki, A.J.1    Janecki, M.2    Akhter, S.3    Donowitz, M.4
  • 20
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • DOI 10.1038/35055042
    • Keller, P., Toomre, D., Díaz, E., White, J. and Simons, K. (2001). Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat. Cell Biol. 3, 140-149. (Pubitemid 32118367)
    • (2001) Nature Cell Biology , vol.3 , Issue.2 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 21
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 a using imaging fluorescence resonance energy transfer
    • Kenworthy A. K. and Edidin, M. (1998). Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 A using imaging fluorescence resonance energy transfer. J. Cell Biol. 142, 69-84.
    • (1998) J. Cell Biol. , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 22
    • 0032516852 scopus 로고    scopus 로고
    • + exchanger NHE3 isoform is regulated by the phosphatidylinositol 3-kinase pathway
    • DOI 10.1074/jbc.273.33.20828
    • Kurashima, K., Szabo, E. Z., Lukacs, G., Orlowski, J. and Grinstein, S. (1998). Endosomal recycling of the Na+/H+ exchanger NHE3 isoform is regulated by the phosphatidylinositol 3-kinase pathway. J. Biol. Chem. 273, 20828-20836. (Pubitemid 28385361)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 20828-20836
    • Kurashima, K.1    Szabo, E.Z.2    Lukacs, G.3    Orlowski, J.4    Grinstein, S.5
  • 23
    • 59049089795 scopus 로고    scopus 로고
    • Engineered protein connectivity to actin mimics PDZ-dependent recycling of G protein-coupled receptors but not its regulation by Hrs
    • Lauffer, B. E., Chen, S., Melero, C., Kortemme, T., von Zastrow, M.and Vargas, G. A. (2009). Engineered protein connectivity to actin mimics PDZ-dependent recycling of G protein-coupled receptors but not its regulation by Hrs. J. Biol. Chem. 284, 2448-2458.
    • (2009) J. Biol. Chem. , vol.284 , pp. 2448-2458
    • Lauffer, B.E.1    Chen, S.2    Melero, C.3    Kortemme, T.4    Von Zastrow, M.5    Vargas, G.A.6
  • 25
    • 0038269099 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates brush border Na+/H+ exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase a regulatory protein-dependent mechanism
    • Lee-Kwon, W., Kawano, K., Choi, J. W., Kim, J. H. and Donowitz, M. (2003a). Lysophosphatidic acid stimulates brush border Na+/H+ exchanger 3 (NHE3) activity by increasing its exocytosis by an NHE3 kinase A regulatory protein-dependent mechanism. J. Biol. Chem. 278, 16494-16501.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16494-16501
    • Lee-Kwon, W.1    Kawano, K.2    Choi, J.W.3    Kim, J.H.4    Donowitz, M.5
  • 26
    • 0242594703 scopus 로고    scopus 로고
    • Ca2+-dependent inhibition of NHE3 requires PKC alpha which binds to E3KARP to decrease surface NHE3 containing plasma membrane complexes
    • Lee-Kwon, W., Kim, J. H., Choi, J. W., Kawano, K., Cha, B., Dartt, D. A., Zoukhri, D. and Donowitz, M. (2003b). Ca2+-dependent inhibition of NHE3 requires PKC alpha which binds to E3KARP to decrease surface NHE3 containing plasma membrane complexes. Am. J. Physiol. Cell Physiol. 285, C1527-C1536.
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285
    • Lee-Kwon, W.1    Kim, J.H.2    Choi, J.W.3    Kawano, K.4    Cha, B.5    Dartt, D.A.6    Zoukhri, D.7    Donowitz, M.8
  • 27
    • 0029031096 scopus 로고
    • Separate C-terminal domains of the epithelial specific brush border Na+/H+ exchanger isoform NHE3 are involved in stimulation and inhibition by protein kinases/growth factors
    • Levine, S. A., Nath, S. K., Yun, C. H., Yip, J. W., Montrose, M., Donowitz, M. and Tse, C. M. (1995). Separate C-terminal domains of the epithelial specific brush border Na+/H+ exchanger isoform NHE3 are involved in stimulation and inhibition by protein kinases/growth factors. J. Biol. Chem. 270, 13716-13725.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13716-13725
    • Levine, S.A.1    Nath, S.K.2    Yun, C.H.3    Yip, J.W.4    Montrose, M.5    Donowitz, M.6    Tse, C.M.7
  • 28
    • 2442657807 scopus 로고    scopus 로고
    • + exchanger 3 (NHE3) occurs through changes in NHE3 trafficking and complex formation and is Src dependent
    • DOI 10.1113/jphysiol.2004.060921
    • Li, X., Zhang, H., Cheong, A., Leu, S., Chen, Y., Elowsky, C. G. and Donowitz, M. (2004). Carbachol regulation of rabbit ileal brush border Na+-H+ exchanger 3 (NHE3) occurs through changes in NHE3 trafficking and complex formation and is Src dependent. J. Physiol. 556, 791-804. (Pubitemid 38660314)
    • (2004) Journal of Physiology , vol.556 , Issue.3 , pp. 791-804
    • Li, X.1    Zhang, H.2    Cheong, A.3    Yueping Chen, S.L.4    Elowsky, C.G.5    Donowitz, M.6
  • 29
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar, W. H. (1995). Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270, 12949-12952.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 30
    • 0033604620 scopus 로고    scopus 로고
    • Bioactive lysophospholipids and their G protein-coupled receptors
    • Moolenaar, W. H. (1999). Bioactive lysophospholipids and their G protein-coupled receptors. Exp. Cell Res. 253, 230-238.
    • (1999) Exp. Cell Res. , vol.253 , pp. 230-238
    • Moolenaar, W.H.1
  • 31
    • 0025177599 scopus 로고
    • Growth factor-like action of lysophosphatidic acid: Mitogenic signalling mediated by G proteins
    • Moolenaar, W. H. and van Corven, E. J. (1990). Growth factor-like action of lysophosphatidic acid: mitogenic signalling mediated by G proteins. Ciba Found. Symp. 150, 99-106.
    • (1990) Ciba Found. Symp. , vol.150 , pp. 99-106
    • Moolenaar, W.H.1    Van Corven, E.J.2
  • 32
    • 0030907226 scopus 로고    scopus 로고
    • Lysophosphatidic acid: G-protein signalling and cellular responses
    • DOI 10.1016/S0955-0674(97)80059-2
    • Moolenaar, W. H., Kranenburg, O., Postma, F. R. and Zondag, G. C. (1997). Lysophosphatidic acid: G-protein signalling and cellular responses. Curr. Opin. Cell Biol. 9, 168-173. (Pubitemid 27135983)
    • (1997) Current Opinion in Cell Biology , vol.9 , Issue.2 , pp. 168-173
    • Moolenaar, W.H.1    Kranenburg, O.2    Postma, F.R.3    Zondag, G.C.M.4
  • 33
    • 0038152846 scopus 로고    scopus 로고
    • 9/GPR23 as a novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family
    • DOI 10.1074/jbc.M302648200
    • Noguchi, K., Ishii, S. and Shimizu, T. (2003). Identification of p2y9/GPR23 as a novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family. J. Biol. Chem. 278, 25600-25606. (Pubitemid 36835313)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25600-25606
    • Noguchi, K.1    Ishii, S.2    Shimizu, T.3
  • 34
    • 0345932705 scopus 로고
    • A specific mutation abolishing Na+/H+ antiport activity in hamster fibroblasts precludes growth at neutral and acidic pH
    • Pouyssegur, J., Sardet, C., Franchi, A., L'Allemain, G. and Paris, S. (1984). A specific mutation abolishing Na+/H+ antiport activity in hamster fibroblasts precludes growth at neutral and acidic pH. Proc. Natl. Acad. Sci. USA 81, 4833-4837.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4833-4837
    • Pouyssegur, J.1    Sardet, C.2    Franchi, A.3    L'Allemain, G.4    Paris, S.5
  • 35
    • 0033749211 scopus 로고    scopus 로고
    • Lysophosphatidic acid-induced platelet shape change proceeds via Rho/Rho kinase-mediated myosin light-chain and moesin phosphorylation
    • Retzer, M. and Essler, M. (2000). Lysophosphatidic acid-induced platelet shape change proceeds via Rho/Rho kinase-mediated myosin light-chain and moesin phosphorylation. Cell Signal 12, 645-648.
    • (2000) Cell Signal , vol.12 , pp. 645-648
    • Retzer, M.1    Essler, M.2
  • 36
    • 0034889768 scopus 로고    scopus 로고
    • Ezrin binding domain-deficient NHERF attenuates cAMP-mediated inhibition of Na(+)/H(+) exchange in OK cells
    • Weinman, E. J., Steplock, D., Wade, J. B. and Shenolikar, S. (2001). Ezrin binding domain-deficient NHERF attenuates cAMP-mediated inhibition of Na(+)/H(+) exchange in OK cells. Am. J. Physiol. Renal. Physiol. 281, F374-F380.
    • (2001) Am. J. Physiol. Renal. Physiol. , vol.281
    • Weinman, E.J.1    Steplock, D.2    Wade, J.B.3    Shenolikar, S.4
  • 37
    • 0034624048 scopus 로고    scopus 로고
    • Lysophosphatidic acid-induced Ca2+ mobilization requires intracellular sphingosine 1-phosphate production. Potential involvement of endogenous EDG-4 receptors
    • Young, K. W., Bootman, M. D., Channing, D. R., Lipp, P., Maycox, P. R., Meakin, J., Challiss, R. A. and Nahorski, S. R. (2000). Lysophosphatidic acid-induced Ca2+ mobilization requires intracellular sphingosine 1-phosphate production. Potential involvement of endogenous EDG-4 receptors. J. Biol. Chem. 275, 38532-38539.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38532-38539
    • Young, K.W.1    Bootman, M.D.2    Channing, D.R.3    Lipp, P.4    Maycox, P.R.5    Meakin, J.6    Challiss, R.A.7    Nahorski, S.R.8
  • 38
    • 0032476006 scopus 로고    scopus 로고
    • NHE3 kinase a regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin
    • Yun, C. H., Lamprecht, G., Forster, D. V. and Sidor, A. (1998). NHE3 kinase A regulatory protein E3KARP binds the epithelial brush border Na+/H+ exchanger NHE3 and the cytoskeletal protein ezrin. J. Biol. Chem. 273, 25856-25863.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25856-25863
    • Yun, C.H.1    Lamprecht, G.2    Forster, D.V.3    Sidor, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.