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Volumn 446, Issue 3, 2012, Pages 427-435

Characterization of cytoskeletal protein 4.1R interaction with NHE1 (Na+ /H+ exchanger isoform 1)

Author keywords

Calmodulin; Cytoskeleton; Na+ H+ exchanger isoform 1 (NHE1); Protein 4.1R; Sodium proton exchange

Indexed keywords

AMINO ACID; CYTOSKELETON PROTEIN; HYPERTONIC SOLUTION; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE; SODIUM PROTON EXCHANGE PROTEIN 1;

EID: 84865588105     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20120535     Document Type: Article
Times cited : (19)

References (47)
  • 2
    • 0036971109 scopus 로고    scopus 로고
    • + exchanger
    • DOI 10.1139/o02-151
    • Slepkov, E. and Fliegel, L. (2002) Structure and function of the NHE1 isoform of the Na+ /H+ exchanger. Biochem. Cell Biol. 80, 499-508 (Pubitemid 36124811)
    • (2002) Biochemistry and Cell Biology , vol.80 , Issue.5 , pp. 499-508
    • Slepkov, E.1    Fliegel, L.2
  • 3
    • 0036968259 scopus 로고    scopus 로고
    • Multiple modes of regulation of Na+ /H+ exchangers
    • Hayashi, H., Szaszi, K. and Grinstein, S. (2002) Multiple modes of regulation of Na+ /H+ exchangers. Ann. N.Y. Acad. Sci. 976, 248-258
    • (2002) Ann. N.Y. Acad. Sci. , vol.976 , pp. 248-258
    • Hayashi, H.1    Szaszi, K.2    Grinstein, S.3
  • 4
    • 34250683573 scopus 로고    scopus 로고
    • Beyond ion translocation: Structural functions of the sodium-hydrogen exchanger isoform-1
    • DOI 10.1097/MNH.0b013e3281bd888d, PII 0004155220070700000013
    • Meima, M. E., Mackley, J. R. and Barber, D. L. (2007) Beyond ion translocation: structural functions of the sodium-hydrogen exchanger isoform-1. Curr. Opin. Nephrol. Hypertens. 16, 365-372 (Pubitemid 46944336)
    • (2007) Current Opinion in Nephrology and Hypertension , vol.16 , Issue.4 , pp. 365-372
    • Meima, M.E.1    Mackley, J.R.2    Barber, D.L.3
  • 5
    • 33744832157 scopus 로고    scopus 로고
    • + exchanger NHE1 in cell migration
    • DOI 10.1111/j.1748-1716.2006.01543.x
    • Stock, C. and Schwab, A. (2006) Role of the Na+ / H+ exchanger NHE1 in cell migration. Acta Physiol. 187, 149-157 (Pubitemid 43828772)
    • (2006) Acta Physiologica , vol.187 , Issue.1-2 , pp. 149-157
    • Stock, C.1    Schwab, A.2
  • 6
    • 33846870761 scopus 로고    scopus 로고
    • Structural and functional analysis of the Na+ /H+ exchanger
    • Slepkov, E. R., Rainey, J. K., Sykes, B. D. and Fliegel, L. (2007) Structural and functional analysis of the Na+ /H+ exchanger. Biochem. J. 401, 623-633
    • (2007) Biochem. J. , vol.401 , pp. 623-633
    • Slepkov, E.R.1    Rainey, J.K.2    Sykes, B.D.3    Fliegel, L.4
  • 7
    • 0036532117 scopus 로고    scopus 로고
    • Ion transport proteins anchor and regulate the cytoskeleton
    • DOI 10.1016/S0955-0674(02)00304-6
    • Denker, S. P. and Barber, D. L. (2002) Ion transport proteins anchor and regulate the cytoskeleton. Curr. Opin. Cell Biol. 14, 214-220 (Pubitemid 34219511)
    • (2002) Current Opinion in Cell Biology , vol.14 , Issue.2 , pp. 214-220
    • Denker, S.P.1    Barber, D.L.2
  • 11
    • 33750727697 scopus 로고    scopus 로고
    • Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily
    • Diakowski, W., Grzybek, M. and Sikorski, A. F. (2006) Protein 4.1, a component of the erythrocyte membrane skeleton and its related homologue proteins forming the protein 4.1/FERM superfamily. Folia Histochem. Cytobiol. 44, 231-248 (Pubitemid 44696964)
    • (2006) Folia Histochemica et Cytobiologica , vol.44 , Issue.4 , pp. 231-248
    • Diakowski, W.1    Grzybek, M.2    Sikorski, A.F.3
  • 12
    • 32844459256 scopus 로고    scopus 로고
    • 2+ and calmodulin
    • Nunomura, W. and Takakuwa, Y. (2006) Regulation of protein 4.1R interactions with membrane proteins by Ca2 + and calmodulin. Front. Biosci. 11, 1522-1539 (Pubitemid 43253439)
    • (2006) Frontiers in Bioscience , vol.11 , Issue.2 P.1199-1590 , pp. 1522-1539
    • Nunomura, W.1    Takakuwa, Y.2
  • 13
    • 0021940465 scopus 로고
    • Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton
    • Pasternack, G. R., Anderson, R. A., Leto, T. L. and Marchesi, V. T. (1985) Interactions between protein 4.1 and band 3. An alternative binding site for an element of the membrane skeleton. J. Biol. Chem. 260, 3676-3683 (Pubitemid 15110960)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3676-3683
    • Pasternack, G.R.1    Anderson, R.A.2    Leto, T.L.3    Marchesi, V.T.4
  • 14
    • 0026772154 scopus 로고
    • Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger
    • Jöns, T. and Dreckahn, D. (1992) Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. EMBO J. 11, 2863-2867
    • (1992) EMBO J. , vol.11 , pp. 2863-2867
    • Jöns, T.1    Dreckahn, D.2
  • 15
    • 0026774620 scopus 로고
    • Localization of the protein 4.1-binding site on the cytoplasmic domain of erythrocyte membrane band 3
    • Lombardo, C. R., Willardson, B. M. and Low, P. S. (1992) Localization of the protein 4.1-binding site on the cytoplasmic domain of erythrocyte membrane band 3. J. Biol. Chem. 267, 9540-9546
    • (1992) J. Biol. Chem. , vol.267 , pp. 9540-9546
    • Lombardo, C.R.1    Willardson, B.M.2    Low, P.S.3
  • 16
    • 0021183609 scopus 로고
    • Glycophorin is linked by band 4.1 protein to human erythrocyte membrane skeleton
    • Anderson, R. A. and Lovrien, R. E. (1984) Glycophorin is linked by band 4.1 protein to the human erythrocyte membrane skeleton. Nature 307, 655-658 (Pubitemid 14129684)
    • (1984) Nature , vol.307 , Issue.5952 , pp. 655-658
    • Anderson, R.A.1    Lovrien, R.E.2
  • 17
    • 0030730935 scopus 로고    scopus 로고
    • 2+ and calmodulin. Implications for modulation of CD44-ankyrin interaction
    • DOI 10.1074/jbc.272.48.30322
    • Nunomura, W., Takakuwa, Y., Tokimitsu, R., Kawashima, M., Krauss, S. and Mohandas, N. (1997) Regulation of CD44-protein 4.1 interaction by Ca2+ and calmodulin: implications for modulation of CD44-ankyrin interaction. J. Biol. Chem. 272, 30322-30328 (Pubitemid 27512238)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 30322-30328
    • Nunomura, W.1    Takakuwa, Y.2    Tokimitsu, R.3    Krauss, S.W.4    Kawashima, M.5    Mohandas, N.6
  • 18
    • 0030763609 scopus 로고    scopus 로고
    • The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis
    • DOI 10.1074/jbc.272.39.24191
    • Marfatia, S. M., Morais-Cabral, J. H., Kim, A. C., Byron, O. and Chishti, A. H. (1997) The PDZ domain of human erythrocyte p55 mediates its binding to the cytoplasmic carboxyl terminus of glycophorin C. Analysis of the binding interface by in vitro mutagenesis. J. Biol. Chem. 272, 24191-24197 (Pubitemid 27418618)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.39 , pp. 24191-24197
    • Marfatia, S.M.1    Morais-Cabral, J.H.2    Kim, A.C.3    Byron, O.4    Chishti, A.H.5
  • 19
    • 0034637458 scopus 로고    scopus 로고
    • Regulation of protein 4.1R, p55, and Glycophorin C ternary complex in human erythrocyte membrane
    • DOI 10.1074/jbc.M002492200
    • Nunomura, W., Takakuwa, Y., Parra, M., Conboy, J. and Mohandas, N. (2000) Regulation of protein 4.1R, p55, and glycophorin C ternary complex in human erythrocyte membrane. J. Biol. Chem. 275, 24540-24546 (Pubitemid 30626549)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.32 , pp. 24540-24546
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.4    Mohandas, N.5
  • 20
    • 0025924751 scopus 로고
    • 2+-dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1
    • Tanaka, T., Kadowaki, K., Lazarides, E. and Sobue, K. (1991) Ca2+ -dependent regulation of the spectrin/actin interaction by calmodulin and protein 4.1. J. Biol. Chem. 266, 1134-1140 (Pubitemid 21907236)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.2 , pp. 1134-1140
    • Tanaka, T.1    Kadowaki, K.2    Lazarides, E.3    Sobue, K.4
  • 21
    • 0023687847 scopus 로고    scopus 로고
    • Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions
    • Takakuwa, Y. and Mohandas, N. (1998) Modulation of erythrocyte membrane material properties by Ca2+ and calmodulin. Implications for their role in regulation of skeletal protein interactions. J. Clin. Invest. 82, 394-400
    • (1998) J. Clin. Invest. , vol.82 , pp. 394-400
    • Takakuwa, Y.1    Mohandas, N.2
  • 22
    • 81555220907 scopus 로고    scopus 로고
    • Insights into the function of the unstructured N-terminal domain of proteins 4.1R and 4.1G in erythropoiesis
    • Nunomura, W., Gascard, P. and Takakuwa, Y. (2011) Insights into the function of the unstructured N-terminal domain of proteins 4.1R and 4.1G in erythropoiesis. Int. J. Cell Biol. 2011, 943272
    • (2011) Int. J. Cell Biol. , vol.2011 , pp. 943272
    • Nunomura, W.1    Gascard, P.2    Takakuwa, Y.3
  • 23
    • 0034096197 scopus 로고    scopus 로고
    • 2+-independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins
    • DOI 10.1074/jbc.275.9.6360
    • Nunomura, W., Takakuwa, Y., Parra, M., Conboy, J. and Mohandas, N. (2000) Ca2+ -dependent and Ca2+ -independent calmodulin binding sites in erythrocyte protein 4.1. Implications for regulation of protein 4.1 interactions with transmembrane proteins. J. Biol. Chem. 275, 6360-6367 (Pubitemid 30129930)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6360-6367
    • Nunomura, W.1    Takakuwa, Y.2    Parra, M.3    Conboy, J.G.4    Mohandas, N.5
  • 24
    • 34547423260 scopus 로고    scopus 로고
    • Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): Unique binding properties with transmembrane proteins and calmodulin
    • DOI 10.1016/j.cbpb.2007.05.001, PII S1096495907001728
    • Nunomura, W., Takakuwa, Y., Cherr, G. N. and Murata, K. (2007) Characterization of protein 4.1R in erythrocytes of zebrafish (Danio rerio): unique binding properties with transmembrane proteins and calmodulin. Comp. Biochem. Physiol. Part B 148, 124-138 (Pubitemid 47176431)
    • (2007) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.148 , Issue.2 , pp. 124-138
    • Nunomura, W.1    Takakuwa, Y.2    Cherr, G.N.3    Murata, K.4
  • 25
    • 0034631854 scopus 로고    scopus 로고
    • + exchange requires phosphatidylinositol 4,5-bisphosphate
    • DOI 10.1083/jcb.150.1.213
    • Aharonovitz, O., Zaun, H. C., Balla, T., York, J. D., Orlowski, J. and Grinstein, S. (2000) Intracellular pH regulation by Na+ /H+ exchange requires phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 150, 213-224 (Pubitemid 30480239)
    • (2000) Journal of Cell Biology , vol.150 , Issue.1 , pp. 213-224
    • Aharonovitz, O.1    Zaun, H.C.2    Balla, T.3    York, J.D.4    Orlowski, J.5    Grinstein, S.6
  • 26
    • 0034503095 scopus 로고    scopus 로고
    • + translocation
    • DOI 10.1016/S1097-2765(00)00139-8
    • Denker, S. P., Huang, D. C., Orlowski, J., Furthmayr, H. and Barber, D. L. (2000) Direct binding of the Na+ /H+ exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H + translocation. Mol. Cell 6, 1425-1436 (Pubitemid 32045934)
    • (2000) Molecular Cell , vol.6 , Issue.6 , pp. 1425-1436
    • Denker, S.P.1    Huang, D.C.2    Orlowski, J.3    Furthmayr, H.4    Barber, D.L.5
  • 27
    • 82455174789 scopus 로고    scopus 로고
    • Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: Novel insights into the biological significance of the calciumindependent binding of calmodulin to protein 4.1R
    • Nunomura, W., Sasakura, D., Shiba, K., Nakamura, S., Kidokoro, S. I. and Takakuwa, Y. (2011) Structural stabilization of protein 4.1R FERM domain upon binding to apo-calmodulin: novel insights into the biological significance of the calciumindependent binding of calmodulin to protein 4.1R. Biochem. J. 440, 367-374
    • (2011) Biochem. J. , vol.440 , pp. 367-374
    • Nunomura, W.1    Sasakura, D.2    Shiba, K.3    Nakamura, S.4    Kidokoro, S.I.5    Takakuwa, Y.6
  • 29
    • 77956741418 scopus 로고
    • Ultraviolet spectra of proteins and amino acids
    • Wetlaufer, D. B. (1962) Ultraviolet spectra of proteins and amino acids. Adv. Protein Chem. 17, 303-391
    • (1962) Adv. Protein Chem. , vol.17 , pp. 303-391
    • Wetlaufer, D.B.1
  • 30
    • 0028800154 scopus 로고
    • Identification of a phosphatidyl-inositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin
    • Niggli, V., Andr ́eoli, C., Roy, C. and Mangeat, P. (1995) Identification of a phosphatidyl-inositol-4,5-bisphosphate-binding domain in the N-terminal region of ezrin. FEBS Lett. 376, 172-176
    • (1995) FEBS Lett. , vol.376 , pp. 172-176
    • Niggli, V.1    Andracute2    eoli, C.3    Roy, C.4    Mangeat, P.5
  • 31
    • 33646478114 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins
    • An, X., Zhang, X., Debnath, G., Baines, A. J. and Mohandas, N. (2006) Phosphatidylinositol-4,5-biphosphate (PIP2) differentially regulates the interaction of human erythrocyte protein 4.1 (4.1R) with membrane proteins. Biochemistry 45, 5725-3572
    • (2006) Biochemistry , vol.45 , pp. 5725-13572
    • An, X.1    Zhang, X.2    Debnath, G.3    Baines, A.J.4    Mohandas, N.5
  • 32
    • 77957287814 scopus 로고    scopus 로고
    • High affinity of interaction between super-antigen and T cell receptor Vβ molecules induces a high level and prolonged expansion of superantigen-reactive CD4+ T cells
    • Omoe, K., Nunomura, W., Kato, H., Li, Z. J., Igarashi, O., Araake, M., Sano, K., Ono, H. K., Abe, Y., Hu, D. L. et al. (2010) High affinity of interaction between super-antigen and T cell receptor Vβ molecules induces a high level and prolonged expansion of superantigen-reactive CD4+ T cells. J. Biol. Chem. 285, 30427-30435
    • (2010) J. Biol. Chem. , vol.285 , pp. 30427-30435
    • Omoe, K.1    Nunomura, W.2    Kato, H.3    Li, Z.J.4    Igarashi, O.5    Araake, M.6    Sano, K.7    Ono, H.K.8    Abe, Y.9    Hu, D.L.10
  • 33
    • 0037164808 scopus 로고    scopus 로고
    • Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1
    • DOI 10.1083/jcb.200208050
    • Denker, S. P. and Barber, D. L. (2002) Cell migration requires both ion translocation and cytoskeletal anchoring by the Na-H exchanger NHE1. J. Cell Biol. 159, 1087-1096 (Pubitemid 36055762)
    • (2002) Journal of Cell Biology , vol.159 , Issue.6 , pp. 1087-1096
    • Denker, S.P.1    Barber, D.L.2
  • 34
    • 0027366806 scopus 로고
    • The resonant mirror: A novel optical biosensor for direct sensing of biomolecular interactions. Part I: Principle of operation and associated instrumentation
    • DOI 10.1016/0956-5663(93)80073-X
    • Cush, R., Cronin, J. M., Stewart, W. J., Maule, C. H., Molloy, J. and Goddard, N. J. (1993) The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions Part I: principle of operation and associated instrumentation. Biosens. Bioelectron. 8, 347-353 (Pubitemid 23356398)
    • (1993) Biosensors and Bioelectronics , vol.8 , Issue.7-8 , pp. 347-353
    • Cush, R.1    Cronin, J.M.2    Stewart, W.J.3    Maule, C.H.4    Molloy, J.5    Goddard, N.J.6
  • 35
    • 78649579937 scopus 로고    scopus 로고
    • Similarities and differences in the structure and function of 4.1G and 4.1R135, two protein 4.1 paralogs expressed in erythroid cells
    • Nunomura, W., Kinoshita, K., Parra, M., Gascard, P., An, X., Mohandas, N. and Takakuwa, Y. (2010) Similarities and differences in the structure and function of 4.1G and 4.1R135, two protein 4.1 paralogs expressed in erythroid cells. Biochem. J. 432, 407-446
    • (2010) Biochem. J. , vol.432 , pp. 407-446
    • Nunomura, W.1    Kinoshita, K.2    Parra, M.3    Gascard, P.4    An, X.5    Mohandas, N.6    Takakuwa, Y.7
  • 36
    • 58249084140 scopus 로고    scopus 로고
    • Marked difference in membrane-protein-binding properties of the two isoforms of protein 4.1R expressed at early and late stages of erythroid differentiation
    • Nunomura, W., Parra, M., Hebiguchi, H., Sawada, K., Mohandas, N. and Takakuwa, Y. (2009) Marked difference in membrane-protein-binding properties of the two isoforms of protein 4.1R expressed at early and late stages of erythroid differentiation. Biochem. J. 417, 141-148
    • (2009) Biochem. J. , vol.417 , pp. 141-148
    • Nunomura, W.1    Parra, M.2    Hebiguchi, H.3    Sawada, K.4    Mohandas, N.5    Takakuwa, Y.6
  • 37
    • 0027537715 scopus 로고
    • The role of inositol phospholipids in the association of band 4.1 with the human erythrocyte membrane
    • DOI 10.1111/j.1432-1033.1993.tb17595.x
    • Gascard, P., Pawelczyk, T., Lowenstein, J. M. and Cohen, C. M. (1993) The role of inositol phospholipids in the association of band 4.1 with the human erythrocyte membrane. Eur. J. Biochem. 211, 671-681 (Pubitemid 23050039)
    • (1993) European Journal of Biochemistry , vol.211 , Issue.3 , pp. 671-681
    • Gascard, P.1    Pawelczyk, T.2    Lowenstein, J.M.3    Cohen, C.M.4
  • 38
    • 0028277779 scopus 로고
    • Mutation of calmodulin-binding site renders the Na+ /H+ exchanger (NHEI) highly H+ -sensitive and Ca2+ regulation-defective
    • Wakabayashi, S., Bertrand, B., Ikeda, T., Pouysségur, J. and Shigekawa, M. (1994) Mutation of calmodulin-binding site renders the Na+ /H+ exchanger (NHEI) highly H+ -sensitive and Ca2+ regulation-defective. J. Biol. Chem. 269, 13710-13715
    • (1994) J. Biol. Chem. , vol.269 , pp. 13710-13715
    • Wakabayashi, S.1    Bertrand, B.2    Ikeda, T.3    Pouysségur, J.4    Shigekawa, M.5
  • 39
    • 0028242352 scopus 로고
    • The Na+ /H+ exchanger isoform 1 (NHEl) is a novel member of the calmodulin-binding proteins: Identification and characterization of calmodulin-binding sites
    • Bertrand, B., Wakabayashi, S., Ikeda, T., Pouysségur, J. and Shigekawa, M. (1994) The Na+ /H+ exchanger isoform 1 (NHEl) 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    Pouysségur, J.4    Shigekawa, M.5
  • 40
    • 0021846909 scopus 로고
    • Polyphosphoinositides and the shape of mammalian erythrocytes
    • DOI 10.1007/BF02534234
    • Quist, E. and Powell, P (1985) Polyphosphoinositides and the shape of mammalian erythrocytes. Lipids 20, 433-438 (Pubitemid 15007697)
    • (1985) Lipids , vol.20 , Issue.7 , pp. 433-438
    • Quist, E.1    Powell, P.2
  • 41
    • 0033790239 scopus 로고    scopus 로고
    • Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
    • Han, B. G., Nunomura, W., Takakuwa, Y., Mohandas, N. and Jap, J. K. (2000) Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization. Nat. Struct. Biol. 7, 871-875
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 871-875
    • Han, B.G.1    Nunomura, W.2    Takakuwa, Y.3    Mohandas, N.4    Jap, J.K.5
  • 42
    • 33745743608 scopus 로고    scopus 로고
    • Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation
    • DOI 10.1038/sj.emboj.7601145, PII 7601145
    • Ammar, Y. B., Takeda, S., Hisamitsu, T., Mori, H. and Wakabayashi, S. (2006) Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation. EMBO J. 25, 2315-2325 (Pubitemid 44012215)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2315-2325
    • Ammar, Y.B.1    Takeda, S.2    Hisamitsu, T.3    Mori, H.4    Wakabayashi, S.5
  • 43
    • 81755189047 scopus 로고    scopus 로고
    • Structure of human Na+ /H+ exchanger NHE1 regulatory region in complex with CaM and Ca2+
    • Köster, S., Pavkov-Keller, T., Kuhlbraandt, W. and Yildiz, Ö. (2011) Structure of human Na+ /H+ exchanger NHE1 regulatory region in complex with CaM and Ca2+. J. Biol. Chem. 286, 40954-40961
    • (2011) J. Biol. Chem. , vol.286 , pp. 40954-40961
    • Köster, S.1    Pavkov-Keller, T.2    Kuhlbraandt, W.3    Yildiz, Ö.4
  • 44
    • 79955365244 scopus 로고    scopus 로고
    • The intracellular distal tail of the Na+ /H+ exchanger NHE1 is intrinsically disordered: Implications for NHE1 trafficking
    • Nørholm, A. B., Hendus-Altenburger, R., Bjerre, G., Kjaergaard, M., Pedersen, S. F. and Kragelund, B. B. (2011) The intracellular distal tail of the Na+ /H+ exchanger NHE1 is intrinsically disordered: implications for NHE1 trafficking. Biochemistry 50, 3469-3480
    • (2011) Biochemistry , vol.50 , pp. 3469-3480
    • Nørholm, A.B.1    Hendus-Altenburger, R.2    Bjerre, G.3    Kjaergaard, M.4    Pedersen, S.F.5    Kragelund, B.B.6
  • 46
    • 63649146487 scopus 로고    scopus 로고
    • Membrane targeting and coupling of NHE1-integrinα IIbβ3-NCX1 by lipid rafts following integrin-ligand interactions trigger Ca2+ oscillations
    • Yi, Y. H., Ho, P. Y., Chen, T. W., Lin, W. J., Gukassyan, V., Tsai, T. H., Wang, D. W., Lew, T. S., Tang, C. Y., Lo, S. J. et al. (2009) Membrane targeting and coupling of NHE1-integrinα IIbβ3-NCX1 by lipid rafts following integrin-ligand interactions trigger Ca2+ oscillations. J. Biol. Chem. 284, 3855-3864
    • (2009) J. Biol. Chem. , vol.284 , pp. 3855-3864
    • Yi, Y.H.1    Ho, P.Y.2    Chen, T.W.3    Lin, W.J.4    Gukassyan, V.5    Tsai, T.H.6    Wang, D.W.7    Lew, T.S.8    Tang, C.Y.9    Lo, S.J.10
  • 47
    • 33947531619 scopus 로고    scopus 로고
    • Physiological role and regulation of the Na+ /H+ exchanger
    • Malo, M. E. and Fliegel, L. (2006) Physiological role and regulation of the Na+ /H+ exchanger. Can. J. Physiol. Pharmacol. 84, 1081-1095
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 1081-1095
    • Malo, M.E.1    Fliegel, L.2


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