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Volumn 25, Issue 5, 2008, Pages 436-447

Identification and biochemical characterization of the SLC9A7 interactome

Author keywords

Lipid rafts; Na+ H+ exchanger; NHE7; Protein protein interaction

Indexed keywords

ACTIN; BINDING PROTEIN; CARRIER PROTEIN; CAVEOLIN 1; CELL ADHESION MOLECULE; CYTOSKELETON PROTEIN; HERMES ANTIGEN; PROTEIN KINASE (CALCIUM,CALMODULIN); SODIUM PROTON EXCHANGE PROTEIN 7; VIMENTIN;

EID: 48249108343     PISSN: 09687688     EISSN: 14645203     Source Type: Journal    
DOI: 10.1080/09687680802263046     Document Type: Article
Times cited : (22)

References (47)
  • 2
    • 1242272754 scopus 로고    scopus 로고
    • Diversity of the mammalian sodium/proton exchanger SLC9 gene family
    • Orlowski J, Grinstein S. 2004. Diversity of the mammalian sodium/proton exchanger SLC9 gene family. Pflugers Arch 447:549-565.
    • (2004) Pflugers Arch , vol.447 , pp. 549-565
    • Orlowski, J.1    Grinstein, S.2
  • 3
    • 0035907355 scopus 로고    scopus 로고
    • + exchanger localized to the trans-Golgi network
    • + exchanger localized to the trans-Golgi network. J Biol Chem 276: 17387-17394.
    • (2001) J Biol Chem , vol.276 , pp. 17387-17394
    • Numata, M.1    Orlowski, J.2
  • 4
    • 0033638350 scopus 로고    scopus 로고
    • The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae
    • Bowers K, Levi BP, Patel FI, Stevens TH. 2000. The sodium/proton exchanger Nhx1p is required for endosomal protein trafficking in the yeast Saccharomyces cerevisiae. Mol Biol Cell 11:4277-4294.
    • (2000) Mol Biol Cell , vol.11 , pp. 4277-4294
    • Bowers, K.1    Levi, B.P.2    Patel, F.I.3    Stevens, T.H.4
  • 7
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog CL, Foster LJ, Mann M. 2004. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117:649-662.
    • (2004) Cell , vol.117 , pp. 649-662
    • de Hoog, C.L.1    Foster, L.J.2    Mann, M.3
  • 8
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber J, Ishihama Y, Mann M. 2003. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal Chem 75:663-670.
    • (2003) Anal Chem , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 9
    • 33845973020 scopus 로고    scopus 로고
    • Quantitative comparison of caste differences in honeybee hemolymph
    • Chan QW, Howes CG, Foster LJ. 2006. Quantitative comparison of caste differences in honeybee hemolymph. Mol Cell Proteomics 5:2252-2262.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 2252-2262
    • Chan, Q.W.1    Howes, C.G.2    Foster, L.J.3
  • 14
    • 0028242352 scopus 로고
    • + exchanger isoform 1 (NHE1) is a novel member of the calmodulin-binding proteins. Identification and characterization of calmodulin-binding sites
    • + exchanger isoform 1 (NHE1) is a novel member of the calmodulin-binding proteins. Identification and characterization of calmodulin-binding sites. J Biol Chem 269:13703-13709.
    • (1994) J Biol Chem , vol.269 , pp. 13703-13709
    • Bertrand, B.1    Wakabayashi, S.2    Ikeda, T.3    Pouyssegur, J.4    Shigekawa, M.5
  • 15
    • 0034177673 scopus 로고    scopus 로고
    • +-bound calmodulin forms a compact globular structure on binding four trifluoperazine molecules in solution
    • +-bound calmodulin forms a compact globular structure on binding four trifluoperazine molecules in solution. Biochem J 347:211-215.
    • (2000) Biochem J , vol.347 , pp. 211-215
    • Matsushima, N.1    Hayashi, N.2    Jinbo, Y.3    Izumi, Y.4
  • 16
    • 0032512626 scopus 로고    scopus 로고
    • Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition
    • Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M. 1998. Solution structure of calmodulin-W-7 complex: The basis of diversity in molecular recognition. J Mol Biol 276:165-176.
    • (1998) J Mol Biol , vol.276 , pp. 165-176
    • Osawa, M.1    Swindells, M.B.2    Tanikawa, J.3    Tanaka, T.4    Mase, T.5    Furuya, T.6    Ikura, M.7
  • 18
    • 0018906488 scopus 로고
    • Calcium-regulated modulator protein interacting agents inhibit smooth muscle calcium-stimulated protein kinase and ATPase
    • Hidaka H, Yamaki T, Naka M, Tanaka T, Hayashi H, Kobayashi R. 1980. Calcium-regulated modulator protein interacting agents inhibit smooth muscle calcium-stimulated protein kinase and ATPase. Mol Pharmacol 17:66-72.
    • (1980) Mol Pharmacol , vol.17 , pp. 66-72
    • Hidaka, H.1    Yamaki, T.2    Naka, M.3    Tanaka, T.4    Hayashi, H.5    Kobayashi, R.6
  • 19
    • 0025101653 scopus 로고
    • Trifluoperazine binding to porcine brain calmodulin and skeletal muscle troponin C
    • Massom L, Lee H, Jarrett HW. 1990. Trifluoperazine binding to porcine brain calmodulin and skeletal muscle troponin C. Biochemistry 29:671-681.
    • (1990) Biochemistry , vol.29 , pp. 671-681
    • Massom, L.1    Lee, H.2    Jarrett, H.W.3
  • 20
    • 33845355027 scopus 로고    scopus 로고
    • Interaction of epithelial ion channels with the actin-based cytoskeleton
    • Mazzochi C, Benos DJ, Smith PR. 2006. Interaction of epithelial ion channels with the actin-based cytoskeleton. Am J Physiol Renal Physiol 291:F1113-1122.
    • (2006) Am J Physiol Renal Physiol , vol.291
    • Mazzochi, C.1    Benos, D.J.2    Smith, P.R.3
  • 22
    • 33744779069 scopus 로고    scopus 로고
    • The NHE3 juxtamembrane cytoplasmic domain directly binds ezrin: Dual role in NHE3 trafficking and mobility in the brush border.Mol
    • Cha B, Tse M, Yun C, Kovbasnjuk O, Mohan S, Hubbard A, Arpin M, 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.
    • (2006) Biol Cell , vol.17 , 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
  • 26
    • 15744367511 scopus 로고    scopus 로고
    • + exchanger regulates transepithelial HCO3-absorption through actin cytoskleton remodeling in renal thick ascending limb
    • + exchanger regulates transepithelial HCO3-absorption through actin cytoskleton remodeling in renal thick ascending limb. J Biol Chem 280:11439-11447.
    • (2005) J Biol Chem , vol.280 , pp. 11439-11447
    • Watts III, B.A.1    George, T.2    Good, D.W.3
  • 27
    • 1642503683 scopus 로고    scopus 로고
    • Intermediate filaments are dynamic and motile elements of cellular architecture
    • Helfand BT, Chang L, Goldman RD. 2004. Intermediate filaments are dynamic and motile elements of cellular architecture. J Cell Sci 117:133-141.
    • (2004) J Cell Sci , vol.117 , pp. 133-141
    • Helfand, B.T.1    Chang, L.2    Goldman, R.D.3
  • 28
    • 33750069729 scopus 로고    scopus 로고
    • A direct interaction between actin and vimentin filaments mediated by the tail domain of vimentin
    • Esue O, Carson AA, Tseng Y, Wirtz D. 2006. A direct interaction between actin and vimentin filaments mediated by the tail domain of vimentin. J Biol Chem 281:30393-30399.
    • (2006) J Biol Chem , vol.281 , pp. 30393-30399
    • Esue, O.1    Carson, A.A.2    Tseng, Y.3    Wirtz, D.4
  • 29
    • 0025745212 scopus 로고
    • + antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape
    • + antiporter by clustering and immobilizing integrin alpha 5 beta 1, independent of cell shape. Proc Natl Acad Sci USA 88:7849-7853.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7849-7853
    • Schwartz, M.A.1    Lechene, C.2    Ingber, D.E.3
  • 32
    • 33845302047 scopus 로고    scopus 로고
    • RACK1 associates with NHE5 in focal adhesions and positively regulates the transporter activity
    • Onishi I, Lin PJ, Diering GH, Williams WP, Numata M. 2007. RACK1 associates with NHE5 in focal adhesions and positively regulates the transporter activity. Cell Signal 19:194-203.
    • (2007) Cell Signal , vol.19 , pp. 194-203
    • Onishi, I.1    Lin, P.J.2    Diering, G.H.3    Williams, W.P.4    Numata, M.5
  • 33
    • 15044360781 scopus 로고    scopus 로고
    • The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions
    • Kreis S, Schonfeld HJ, Melchior C, Steiner B, Kieffer N. 2005. The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions. Exp Cell Res 305:110-121.
    • (2005) Exp Cell Res , vol.305 , pp. 110-121
    • Kreis, S.1    Schonfeld, H.J.2    Melchior, C.3    Steiner, B.4    Kieffer, N.5
  • 34
    • 0347513188 scopus 로고    scopus 로고
    • The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress
    • Tsuruta D, Jones JC. 2003. The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J Cell Sci 116:4977-4984.
    • (2003) J Cell Sci , vol.116 , pp. 4977-4984
    • Tsuruta, D.1    Jones, J.C.2
  • 37
    • 27844444696 scopus 로고    scopus 로고
    • PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility
    • Ivaska J, Vuoriluoto K, Huovinen T, Izawa I, Inagaki M, Parker PJ. 2005. PKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility. Embo J 24:3834-3845.
    • (2005) Embo J , vol.24 , pp. 3834-3845
    • Ivaska, J.1    Vuoriluoto, K.2    Huovinen, T.3    Izawa, I.4    Inagaki, M.5    Parker, P.J.6
  • 38
    • 0029112646 scopus 로고
    • N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding
    • Liao HX, Lee DM, Levesque MC, Haynes BF. 1995. N-terminal and central regions of the human CD44 extracellular domain participate in cell surface hyaluronan binding. J Immunol 155:3938-3945.
    • (1995) J Immunol , vol.155 , pp. 3938-3945
    • Liao, H.X.1    Lee, D.M.2    Levesque, M.C.3    Haynes, B.F.4
  • 39
    • 0028097742 scopus 로고
    • Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein
    • Yang B, Yang BL, Savani RC, Turley EA. 1994. Identification of a common hyaluronan binding motif in the hyaluronan binding proteins RHAMM, CD44 and link protein. Embo J 13:286-296.
    • (1994) Embo J , vol.13 , pp. 286-296
    • Yang, B.1    Yang, B.L.2    Savani, R.C.3    Turley, E.A.4
  • 41
    • 0036629343 scopus 로고    scopus 로고
    • Downregulated AP-1 activity is associated with inhibition of Protein-Kinase-C-dependent CD44 and ezrin localisation and upregulation of PKC theta in A431 cells
    • Stapleton G, Malliri A, Ozanne BW. 2002. Downregulated AP-1 activity is associated with inhibition of Protein-Kinase-C-dependent CD44 and ezrin localisation and upregulation of PKC theta in A431 cells. J Cell Sci 115:2713-2724.
    • (2002) J Cell Sci , vol.115 , pp. 2713-2724
    • Stapleton, G.1    Malliri, A.2    Ozanne, B.W.3
  • 42
    • 0036303142 scopus 로고    scopus 로고
    • A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility
    • Legg JW, Lewis CA, Parsons M, Ng T, Isacke CM. 2002. A novel PKC-regulated mechanism controls CD44 ezrin association and directional cell motility. Nat Cell Biol 4:399-407.
    • (2002) Nat Cell Biol , vol.4 , pp. 399-407
    • Legg, J.W.1    Lewis, C.A.2    Parsons, M.3    Ng, T.4    Isacke, C.M.5
  • 43
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M, Sala C. 2001. PDZ domains and the organization of supramolecular complexes. Annu Rev Neurosci 24:1-29.
    • (2001) Annu Rev Neurosci , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 44
    • 3042692979 scopus 로고    scopus 로고
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • + exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion. J Biol Chem 279:26991-27007.
    • (2004) J Biol Chem , vol.279 , pp. 26991-27007
    • Bourguignon, L.Y.1    Singleton, P.A.2    Diedrich, F.3    Stern, R.4    Gilad, E.5
  • 46
    • 33845722205 scopus 로고    scopus 로고
    • Spatial segregation of transport and signalling functions between human endothelial caveolae and lipid raft proteomes
    • Sprenger RR, Fontijn RD, Marle J, Pannekoek H, Horrevoets AJG. 2006. Spatial segregation of transport and signalling functions between human endothelial caveolae and lipid raft proteomes. Biochem J 400:401-410.
    • (2006) Biochem J , vol.400 , pp. 401-410
    • Sprenger, R.R.1    Fontijn, R.D.2    Marle, J.3    Pannekoek, H.4    Horrevoets, A.J.G.5
  • 47
    • 2342424240 scopus 로고    scopus 로고
    • Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase
    • Wang H, Haas M, Liang M, Cai T, Tian J, Li S, Xie Z. 2004. Ouabain assembles signaling cascades through the caveolar Na+/K+-ATPase. J Biol Chem 279:17250-17259.
    • (2004) J Biol Chem , vol.279 , pp. 17250-17259
    • Wang, H.1    Haas, M.2    Liang, M.3    Cai, T.4    Tian, J.5    Li, S.6    Xie, Z.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.