메뉴 건너뛰기




Volumn 367, Issue 1, 2007, Pages 65-79

Phospholamban Interacts with HAX-1, a Mitochondrial Protein with Anti-apoptotic Function

Author keywords

calcium homeostasis; cardiac muscle; HAX 1; phospholamban; sarcoplasmic reticulum

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM ION; COMPLEMENTARY DNA; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HISTIDINE; MITOCHONDRIAL PROTEIN; PHOSPHOLAMBAN; PROTEIN HAX 1; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 33847012674     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.10.057     Document Type: Article
Times cited : (86)

References (61)
  • 1
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: a crucial regulator of cardiac contractility
    • MacLennan D.H., and Kranias E.G. Phospholamban: a crucial regulator of cardiac contractility. Nature Rev. Mol. Cell. Biol. 4 (2003) 566-577
    • (2003) Nature Rev. Mol. Cell. Biol. , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 2
    • 0031722958 scopus 로고    scopus 로고
    • Phospholamban: protein structure, mechanism of action, and role in cardiac function
    • Simmerman H.K., and Jones L.R. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev. 78 (1998) 921-947
    • (1998) Physiol. Rev. , vol.78 , pp. 921-947
    • Simmerman, H.K.1    Jones, L.R.2
  • 3
    • 0022931531 scopus 로고
    • The nature of the modulation of Ca2+ transport as studied by reconstitution of cardiac sarcoplasmic reticulum
    • Inui M., Chamberlain B.K., Saito A., and Fleischer S. The nature of the modulation of Ca2+ transport as studied by reconstitution of cardiac sarcoplasmic reticulum. J. Biol. Chem. 261 (1986) 1794-1800
    • (1986) J. Biol. Chem. , vol.261 , pp. 1794-1800
    • Inui, M.1    Chamberlain, B.K.2    Saito, A.3    Fleischer, S.4
  • 4
    • 0016689752 scopus 로고
    • Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase
    • Tada M., Kirchberger M.A., and Katz A.M. Phosphorylation of a 22,000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 250 (1975) 2640-2647
    • (1975) J. Biol. Chem. , vol.250 , pp. 2640-2647
    • Tada, M.1    Kirchberger, M.A.2    Katz, A.M.3
  • 5
    • 0020015867 scopus 로고
    • Phosphorylation of the sarcoplasmic reticulum and sarcolemma
    • Tada M., and Katz A.M. Phosphorylation of the sarcoplasmic reticulum and sarcolemma. Annu. Rev. Physiol. 44 (1982) 401-423
    • (1982) Annu. Rev. Physiol. , vol.44 , pp. 401-423
    • Tada, M.1    Katz, A.M.2
  • 6
    • 0022921924 scopus 로고
    • Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains
    • Simmerman H.K., Collins J.H., Theibert J.L., Wegener A.D., and Jones L.R. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem. 261 (1986) 13333-13341
    • (1986) J. Biol. Chem. , vol.261 , pp. 13333-13341
    • Simmerman, H.K.1    Collins, J.H.2    Theibert, J.L.3    Wegener, A.D.4    Jones, L.R.5
  • 7
    • 0023119953 scopus 로고
    • Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban
    • Fujii J., Ueno A., Kitano K., Tanaka S., Kadoma M., and Tada M. Complete complementary DNA-derived amino acid sequence of canine cardiac phospholamban. J. Clin. Invest. 79 (1987) 301-304
    • (1987) J. Clin. Invest. , vol.79 , pp. 301-304
    • Fujii, J.1    Ueno, A.2    Kitano, K.3    Tanaka, S.4    Kadoma, M.5    Tada, M.6
  • 8
    • 0033040491 scopus 로고    scopus 로고
    • Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer
    • Pollesello P., Annila A., and Ovaska M. Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer. Biophys. J. 76 (1999) 1784-1795
    • (1999) Biophys. J. , vol.76 , pp. 1784-1795
    • Pollesello, P.1    Annila, A.2    Ovaska, M.3
  • 9
    • 0037077536 scopus 로고    scopus 로고
    • Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban
    • Mascioni A., Karim C., Zamoon J., Thomas D.D., and Veglia G. Solid-state NMR and rigid body molecular dynamics to determine domain orientations of monomeric phospholamban. J. Am. Chem. Soc. 124 (2002) 9392-9393
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9392-9393
    • Mascioni, A.1    Karim, C.2    Zamoon, J.3    Thomas, D.D.4    Veglia, G.5
  • 10
    • 0141530952 scopus 로고    scopus 로고
    • NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles
    • Zamoon J., Mascioni A., Thomas D.D., and Veglia G. NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles. Biophys. J. 85 (2003) 2589-2598
    • (2003) Biophys. J. , vol.85 , pp. 2589-2598
    • Zamoon, J.1    Mascioni, A.2    Thomas, D.D.3    Veglia, G.4
  • 11
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura Y., Kurzydlowski K., Tada M., and MacLennan D.H. Phospholamban inhibitory function is activated by depolymerization. J. Biol. Chem. 272 (1997) 15061-15064
    • (1997) J. Biol. Chem. , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 13
    • 0028168416 scopus 로고
    • Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban
    • Toyofuku T., Kurzydlowski K., Tada M., and MacLennan D.H. Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J. Biol. Chem. 269 (1994) 22929-22932
    • (1994) J. Biol. Chem. , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 14
    • 0028169263 scopus 로고
    • Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum
    • Toyofuku T., Kurzydlowski K., Tada M., and MacLennan D.H. Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 269 (1994) 3088-3094
    • (1994) J. Biol. Chem. , vol.269 , pp. 3088-3094
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 15
    • 0035339677 scopus 로고    scopus 로고
    • Cytoplasmic interactions between phospholamban residues 1-20 and the calcium-activated ATPase of the sarcoplasmic reticulum
    • Sharma P., Patchell V.B., Gao Y., Evans J.S., and Levine B.A. Cytoplasmic interactions between phospholamban residues 1-20 and the calcium-activated ATPase of the sarcoplasmic reticulum. Biochem. J. 335 (2001) 699-706
    • (2001) Biochem. J. , vol.335 , pp. 699-706
    • Sharma, P.1    Patchell, V.B.2    Gao, Y.3    Evans, J.S.4    Levine, B.A.5
  • 16
    • 0032486465 scopus 로고    scopus 로고
    • Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum
    • Kimura Y., Asahi M., Kurzydlowski K., Tada M., and MacLennan D.H. Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum. J. Biol. Chem. 273 (1998) 14238-14241
    • (1998) J. Biol. Chem. , vol.273 , pp. 14238-14241
    • Kimura, Y.1    Asahi, M.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 18
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi V.J., Ponniah S., Harrer J.M., Hoit B.D., Dorn G.W.n., Walsh R.A., and Kranias E.G. Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J. Clin. Invest. 97 (1996) 533-539
    • (1996) J. Clin. Invest. , vol.97 , pp. 533-539
    • Kadambi, V.J.1    Ponniah, S.2    Harrer, J.M.3    Hoit, B.D.4    Dorn, G.W.n.5    Walsh, R.A.6    Kranias, E.G.7
  • 19
    • 0035852663 scopus 로고    scopus 로고
    • Interactions between phospholamban and beta-adrenergic drive may lead to cardiomyopathy and early mortality
    • Dash R., Kadambi V., Schmidt A.G., Tepe N.M., Biniakiewicz D., Gerst M.J., et al. Interactions between phospholamban and beta-adrenergic drive may lead to cardiomyopathy and early mortality. Circulation 103 (2001) 889-896
    • (2001) Circulation , vol.103 , pp. 889-896
    • Dash, R.1    Kadambi, V.2    Schmidt, A.G.3    Tepe, N.M.4    Biniakiewicz, D.5    Gerst, M.J.6
  • 20
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • Luo W., Grupp I.L., Harrer J., Ponniah S., Grupp G., Duffy J.J., et al. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circulat. Res. 75 (1994) 401-409
    • (1994) Circulat. Res. , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6
  • 21
    • 0034973920 scopus 로고    scopus 로고
    • The enhanced contractility of the phospholamban-deficient mouse heart persists with aging
    • Slack J.P., Grupp I.L., Dash R., Holder D., Schmidt A., Gerst M.J., et al. The enhanced contractility of the phospholamban-deficient mouse heart persists with aging. J. Mol. Cell. Cardiol. 33 (2001) 1031-1040
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1031-1040
    • Slack, J.P.1    Grupp, I.L.2    Dash, R.3    Holder, D.4    Schmidt, A.5    Gerst, M.J.6
  • 22
    • 0031569110 scopus 로고    scopus 로고
    • HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family of tyrosine kinases
    • Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., and Watanabe T. HAX-1, a novel intracellular protein, localized on mitochondria, directly associates with HS1, a substrate of Src family of tyrosine kinases. J. Immunol. 158 (1997) 2736-2744
    • (1997) J. Immunol. , vol.158 , pp. 2736-2744
    • Suzuki, Y.1    Demoliere, C.2    Kitamura, D.3    Takeshita, H.4    Deuschle, U.5    Watanabe, T.6
  • 23
    • 0034455302 scopus 로고    scopus 로고
    • Thyroid hormone regulation of phospholamban phosphorylation in the rat heart
    • Ojamaa K., Kenessey A., and Klein I. Thyroid hormone regulation of phospholamban phosphorylation in the rat heart. Endocrinology 141 (2000) 2139-2144
    • (2000) Endocrinology , vol.141 , pp. 2139-2144
    • Ojamaa, K.1    Kenessey, A.2    Klein, I.3
  • 24
    • 0034614471 scopus 로고    scopus 로고
    • Characterization and quantitation of phospholamban and its phosphorylation state using antibodies
    • Mayer E.J., Huckle W., Johnson R.G.J., and McKenna E. Characterization and quantitation of phospholamban and its phosphorylation state using antibodies. Biochem. Biophys. Res. Commun. 267 (2000) 40-48
    • (2000) Biochem. Biophys. Res. Commun. , vol.267 , pp. 40-48
    • Mayer, E.J.1    Huckle, W.2    Johnson, R.G.J.3    McKenna, E.4
  • 25
    • 0034686045 scopus 로고    scopus 로고
    • 2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP
    • 2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP. J. Biol. Chem. 275 (2000) 15034-15038
    • (2000) J. Biol. Chem. , vol.275 , pp. 15034-15038
    • Asahi, M.1    McKenna, E.2    Kurzydlowski, K.3    Tada, M.4    MacLennan, D.H.5
  • 27
    • 0040078063 scopus 로고    scopus 로고
    • Identification of truncated form of mouse HAX-1s gene (HAX-1xs) and characterization of its expression in small intestine and thymus of mice after burn injury
    • Cho K., Adamson L., Park J.H., Zipkin R., and Greenhalgh D. Identification of truncated form of mouse HAX-1s gene (HAX-1xs) and characterization of its expression in small intestine and thymus of mice after burn injury. Shock 18 (2002) 223-229
    • (2002) Shock , vol.18 , pp. 223-229
    • Cho, K.1    Adamson, L.2    Park, J.H.3    Zipkin, R.4    Greenhalgh, D.5
  • 28
    • 0034636015 scopus 로고    scopus 로고
    • The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton
    • Gallagher A.R., Cedzich A., Gretz N., Somlo S., and Witzgall R. The polycystic kidney disease protein PKD2 interacts with Hax-1, a protein associated with the actin cytoskeleton. Proc. Natl Acad. Sci. USA 97 (2000) 4017-4022
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4017-4022
    • Gallagher, A.R.1    Cedzich, A.2    Gretz, N.3    Somlo, S.4    Witzgall, R.5
  • 29
    • 0034958129 scopus 로고    scopus 로고
    • Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible component of the B-cell receptor signalling pathway
    • Dufva M., Olsson M., and Rymo L. Epstein-Barr virus nuclear antigen 5 interacts with HAX-1, a possible component of the B-cell receptor signalling pathway. J. Gen. Virol. 82 (2001) 1581-1587
    • (2001) J. Gen. Virol. , vol.82 , pp. 1581-1587
    • Dufva, M.1    Olsson, M.2    Rymo, L.3
  • 30
    • 0036140439 scopus 로고    scopus 로고
    • K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function
    • Sharp T.V., Wang H.W., Koumi A., Hollyman D., Endo Y., Ye H., et al. K15 protein of Kaposi's sarcoma-associated herpesvirus is latently expressed and binds to HAX-1, a protein with antiapoptotic function. J. Virol. 76 (2002) 802-816
    • (2002) J. Virol. , vol.76 , pp. 802-816
    • Sharp, T.V.1    Wang, H.W.2    Koumi, A.3    Hollyman, D.4    Endo, Y.5    Ye, H.6
  • 31
    • 85047687537 scopus 로고    scopus 로고
    • Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human
    • Haghighi K., Kolokathis F., Pater L., Lynch R.A., Asahi M., Gramolini A.O., et al. Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human. J. Clin. Invest. 111 (2003) 869-876
    • (2003) J. Clin. Invest. , vol.111 , pp. 869-876
    • Haghighi, K.1    Kolokathis, F.2    Pater, L.3    Lynch, R.A.4    Asahi, M.5    Gramolini, A.O.6
  • 32
    • 10544246896 scopus 로고    scopus 로고
    • Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts
    • Chu G., Luo W., Slack J.P., Tilgmann C., Sweet W.E., Spindler M., et al. Compensatory mechanisms associated with the hyperdynamic function of phospholamban-deficient mouse hearts. Circulat. Res. 79 (1996) 1064-1076
    • (1996) Circulat. Res. , vol.79 , pp. 1064-1076
    • Chu, G.1    Luo, W.2    Slack, J.P.3    Tilgmann, C.4    Sweet, W.E.5    Spindler, M.6
  • 33
    • 33144470004 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of sarcolipin in phospholamban null mice impairs myocyte function that is restored by phosphorylation
    • Gramolini A.O., Trivieri M.G., Oudit G.Y., Kislinger T., Li W., Patel M.M., et al. Cardiac-specific overexpression of sarcolipin in phospholamban null mice impairs myocyte function that is restored by phosphorylation. Proc. Natl Acad. Sci. USA 103 (2006) 2446-2451
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 2446-2451
    • Gramolini, A.O.1    Trivieri, M.G.2    Oudit, G.Y.3    Kislinger, T.4    Li, W.5    Patel, M.M.6
  • 35
    • 27144529047 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr interacts with antiapoptotic mitochondrial protein HAX-1
    • Yedavalli V.S., Shih H.M., Chiang Y.P., Lu C.Y., Chang L.Y., Chen M.Y., et al. Human immunodeficiency virus type 1 Vpr interacts with antiapoptotic mitochondrial protein HAX-1. J. Virol. 79 (2005) 13735-13746
    • (2005) J. Virol. , vol.79 , pp. 13735-13746
    • Yedavalli, V.S.1    Shih, H.M.2    Chiang, Y.P.3    Lu, C.Y.4    Chang, L.Y.5    Chen, M.Y.6
  • 36
    • 33747396191 scopus 로고    scopus 로고
    • Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition
    • Han Y., Chen Y.-S., Liu Z., Bodyak N., Rigor D., Bisping E., et al. Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition. Circulat. Res. 99 (2006) 415-423
    • (2006) Circulat. Res. , vol.99 , pp. 415-423
    • Han, Y.1    Chen, Y.-S.2    Liu, Z.3    Bodyak, N.4    Rigor, D.5    Bisping, E.6
  • 37
    • 20044388511 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum
    • Kaliman P., Catalucci D., Lam J.T., Kondo R., Gutierrez J.C., Reddy S., et al. Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum. J. Biol. Chem. 280 (2005) 8016-8021
    • (2005) J. Biol. Chem. , vol.280 , pp. 8016-8021
    • Kaliman, P.1    Catalucci, D.2    Lam, J.T.3    Kondo, R.4    Gutierrez, J.C.5    Reddy, S.6
  • 39
    • 0001121822 scopus 로고    scopus 로고
    • Sites on the cytoplasmic region of phospholamban involved in interaction with the calcium-activated ATPase of the sarcoplasmic reticulum
    • Levine B.A., Patchell V.B., Sharma P., Gao Y., Bigelow D.J., Yao Q., et al. Sites on the cytoplasmic region of phospholamban involved in interaction with the calcium-activated ATPase of the sarcoplasmic reticulum. Eur. J. Biochem. 264 (1999) 905-913
    • (1999) Eur. J. Biochem. , vol.264 , pp. 905-913
    • Levine, B.A.1    Patchell, V.B.2    Sharma, P.3    Gao, Y.4    Bigelow, D.J.5    Yao, Q.6
  • 40
    • 0036179554 scopus 로고    scopus 로고
    • Reconstitution of the cytoplasmic interaction between phospholamban and Ca(2+)-ATPase of cardiac sarcoplasmic reticulum
    • Kimura Y., and Inui M. Reconstitution of the cytoplasmic interaction between phospholamban and Ca(2+)-ATPase of cardiac sarcoplasmic reticulum. Mol. Pharmacol. 61 (2002) 667-673
    • (2002) Mol. Pharmacol. , vol.61 , pp. 667-673
    • Kimura, Y.1    Inui, M.2
  • 41
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., and Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21 (1996) 267-271
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 42
    • 0037242712 scopus 로고    scopus 로고
    • Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) forms complexes with a cellular anti-apoptosis protein Bcl-2 or its EBV counterpart BHRF1 through HS1-associated protein X-1
    • Matsuda G., Nakajima K., Kawaguchi Y., Yamanashi Y., and Hirai K. Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) forms complexes with a cellular anti-apoptosis protein Bcl-2 or its EBV counterpart BHRF1 through HS1-associated protein X-1. Microbiol. Immunol. 47 (2003) 91-99
    • (2003) Microbiol. Immunol. , vol.47 , pp. 91-99
    • Matsuda, G.1    Nakajima, K.2    Kawaguchi, Y.3    Yamanashi, Y.4    Hirai, K.5
  • 43
    • 10344234244 scopus 로고    scopus 로고
    • Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1
    • Radhika V., Onesime D., Ha J.H., and Dhanasekaran N. Galpha13 stimulates cell migration through cortactin-interacting protein Hax-1. J. Biol. Chem. 279 (2004) 49406-49413
    • (2004) J. Biol. Chem. , vol.279 , pp. 49406-49413
    • Radhika, V.1    Onesime, D.2    Ha, J.H.3    Dhanasekaran, N.4
  • 44
    • 3543047295 scopus 로고    scopus 로고
    • Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells
    • Ortiz D.F., Moseley J., Calderon G., Swift A.L., Li S., and Arias I.M. Identification of HAX-1 as a protein that binds bile salt export protein and regulates its abundance in the apical membrane of Madin-Darby canine kidney cells. J. Biol. Chem. 279 (2004) 32761-32770
    • (2004) J. Biol. Chem. , vol.279 , pp. 32761-32770
    • Ortiz, D.F.1    Moseley, J.2    Calderon, G.3    Swift, A.L.4    Li, S.5    Arias, I.M.6
  • 45
    • 33845970253 scopus 로고    scopus 로고
    • The pleiotropic human prohibitin 2: mitochondrial functions and estrogen receptor-dependent nuclear translocation
    • (Epub ahead of print)
    • Kasashima K., Ohta E., Kagawa Y., and Endo H. The pleiotropic human prohibitin 2: mitochondrial functions and estrogen receptor-dependent nuclear translocation. J. Biol Chem. (2006) (Epub ahead of print)
    • (2006) J. Biol Chem.
    • Kasashima, K.1    Ohta, E.2    Kagawa, Y.3    Endo, H.4
  • 46
    • 33749243490 scopus 로고    scopus 로고
    • Intracellular IL-1{alpha}-binding proteins contribute to biological functions of endogenous IL-1{alpha} in systemic sclerosis fibroblasts
    • Kawaguchi Y., Nishimagi E., Tochimoto A., Kawamoto M., Katsumata Y., Soejima M., et al. Intracellular IL-1{alpha}-binding proteins contribute to biological functions of endogenous IL-1{alpha} in systemic sclerosis fibroblasts. Proc. Natl Acad. Sci. USA 103 (2006) 14501-14506
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14501-14506
    • Kawaguchi, Y.1    Nishimagi, E.2    Tochimoto, A.3    Kawamoto, M.4    Katsumata, Y.5    Soejima, M.6
  • 47
    • 33750724136 scopus 로고    scopus 로고
    • Characterization of KIAA0513, a novel signaling molecule that interacts with modulators of neuroplasticity, apoptosis, and the cytoskeleton
    • (Epub ahead of print)
    • Lauriat T.L., Dracheva S., Kremerskothen J., Duning K., Haroutunian V., Buxbaum J.D., et al. Characterization of KIAA0513, a novel signaling molecule that interacts with modulators of neuroplasticity, apoptosis, and the cytoskeleton. Brain Res. (2006) (Epub ahead of print)
    • (2006) Brain Res.
    • Lauriat, T.L.1    Dracheva, S.2    Kremerskothen, J.3    Duning, K.4    Haroutunian, V.5    Buxbaum, J.D.6
  • 48
    • 0038806356 scopus 로고    scopus 로고
    • HAX-1, identified by differential display reverse transcription polymerase chain reaction, is overexpressed in lesional psoriasis
    • Mirmohammadsadegh A., Tartler U., Michel G., Baer A., Walz M., Wolf R., et al. HAX-1, identified by differential display reverse transcription polymerase chain reaction, is overexpressed in lesional psoriasis. J. Invest. Dermatol. 120 (2003) 1045-1051
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 1045-1051
    • Mirmohammadsadegh, A.1    Tartler, U.2    Michel, G.3    Baer, A.4    Walz, M.5    Wolf, R.6
  • 50
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S., Tanaka S., Takayama S., Schibler M.J., Fenton W., and Reed J.C. Investigation of the subcellular distribution of the bcl-2 oncoprotein: residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53 (1993) 4701-4714
    • (1993) Cancer Res. , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 51
    • 0034604033 scopus 로고    scopus 로고
    • Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2
    • Hacki J., Egger L., Monney L., Conus S., Rosse T., Fellay I., and Borner C. Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2. Oncogene 19 (2000) 2286-2295
    • (2000) Oncogene , vol.19 , pp. 2286-2295
    • Hacki, J.1    Egger, L.2    Monney, L.3    Conus, S.4    Rosse, T.5    Fellay, I.6    Borner, C.7
  • 52
    • 0035211935 scopus 로고    scopus 로고
    • Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis
    • Rudner J., Lepple-Wienhues A., Budach W., Berschauer J., Friedrich B., Wesselborg S., et al. Wild-type, mitochondrial and ER-restricted Bcl-2 inhibit DNA damage-induced apoptosis but do not affect death receptor-induced apoptosis. J. Cell. Sci. 114 (2001) 4161-4172
    • (2001) J. Cell. Sci. , vol.114 , pp. 4161-4172
    • Rudner, J.1    Lepple-Wienhues, A.2    Budach, W.3    Berschauer, J.4    Friedrich, B.5    Wesselborg, S.6
  • 53
    • 0034610995 scopus 로고    scopus 로고
    • Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells
    • Pinton P., Ferrari D., Magalhaes P., Schulze-Osthoff K., Di Virgilio F., Pozzan T., and Rizzuto R. Reduced loading of intracellular Ca(2+) stores and downregulation of capacitative Ca(2+) influx in Bcl-2-overexpressing cells. J. Cell. Biol. 148 (2000) 857-862
    • (2000) J. Cell. Biol. , vol.148 , pp. 857-862
    • Pinton, P.1    Ferrari, D.2    Magalhaes, P.3    Schulze-Osthoff, K.4    Di Virgilio, F.5    Pozzan, T.6    Rizzuto, R.7
  • 60
    • 0035968264 scopus 로고    scopus 로고
    • Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure
    • Haghighi K., Schmidt A.G., Hoit B.D., Brittsan A.G., Yatani A., Lester J.W., et al. Superinhibition of sarcoplasmic reticulum function by phospholamban induces cardiac contractile failure. J. Biol. Chem. 276 (2001) 24145-24152
    • (2001) J. Biol. Chem. , vol.276 , pp. 24145-24152
    • Haghighi, K.1    Schmidt, A.G.2    Hoit, B.D.3    Brittsan, A.G.4    Yatani, A.5    Lester, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.