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Volumn 5, Issue 241, 2012, Pages

The membrane-bound enzyme CD38 exists in two opposing orientations

Author keywords

[No Author keywords available]

Indexed keywords

CD38 ANTIGEN; CYCLIC ADENOSINE DIPHOSPHATE RIBOSE;

EID: 84866366579     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2002700     Document Type: Article
Times cited : (129)

References (51)
  • 1
    • 0025265030 scopus 로고
    • Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation
    • D. G. Jackson, J. I. Bell, Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. J. Immunol. 144, 2811-2815 (1990).
    • (1990) J. Immunol. , vol.144 , pp. 2811-2815
    • Jackson, D.G.1    Bell, J.I.2
  • 2
    • 0040226744 scopus 로고
    • Discrete stages of human intrathymic differentiation: Analysis of normal thymocytes and leukemic lymphoblasts of T-cell lineage
    • E. L. Reinherz, P. C. Kung, G. Goldstein, R. H. Levey, S. F. Schlossman, Discrete stages of human intrathymic differentiation: Analysis of normal thymocytes and leukemic lymphoblasts of T-cell lineage. Proc. Natl. Acad. Sci. U.S.A. 77, 1588-1592 (1980).
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1588-1592
    • Reinherz, E.L.1    Kung, P.C.2    Goldstein, G.3    Levey, R.H.4    Schlossman, S.F.5
  • 5
    • 14844354701 scopus 로고
    • +into a calcium-mobilizing metabolite
    • + into a calcium-mobilizing metabolite. Cell Regul. 2, 203-209 (1991).
    • (1991) Cell Regul. , vol.2 , pp. 203-209
    • Lee, H.C.1    Aarhus, R.2
  • 6
    • 0026468136 scopus 로고
    • Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38
    • D. J. States, T. F. Walseth, H. C. Lee, Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem. Sci. 17, 495 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 495
    • States, D.J.1    Walseth, T.F.2    Lee, H.C.3
  • 8
    • 0027892021 scopus 로고
    • Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases
    • H. Kim, E. L. Jacobson, M. K. Jacobson, Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science 261, 1330-1333 (1993).
    • (1993) Science , vol.261 , pp. 1330-1333
    • Kim, H.1    Jacobson, E.L.2    Jacobson, M.K.3
  • 10
    • 0027501559 scopus 로고
    • Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP
    • S. Takasawa, A. Tohgo, N. Noguchi, T. Koguma, K. Nata, T. Sugimoto, H. Yonekura, H. Okamoto, Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J. Biol. Chem. 268, 26052-26054 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26052-26054
    • Takasawa, S.1    Tohgo, A.2    Noguchi, N.3    Koguma, T.4    Nata, K.5    Sugimoto, T.6    Yonekura, H.7    Okamoto, H.8
  • 11
    • 0029616337 scopus 로고
    • ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP
    • R. Aarhus, R. M. Graeff, D. M. Dickey, T. F. Walseth, H. C. Lee, ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. J. Biol. Chem. 270, 30327-30333 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 30327-30333
    • Aarhus, R.1    Graeff, R.M.2    Dickey, D.M.3    Walseth, T.F.4    Lee, H.C.5
  • 12
    • 1942485783 scopus 로고    scopus 로고
    • 2+ stores: A perspective from cyclic ADP-ribose and NAADP
    • 2+ stores: A perspective from cyclic ADP-ribose and NAADP. Curr. Mol. Med. 4, 227-237 (2004).
    • (2004) Curr. Mol. Med. , vol.4 , pp. 227-237
    • Lee, H.C.1
  • 14
  • 20
    • 0034647497 scopus 로고    scopus 로고
    • Identification of the enzymatic active site of CD38 by site-directed mutagenesis
    • C. Munshi, R. Aarhus, R. Graeff, T. F. Walseth, D. Levitt, H. C. Lee, Identification of the enzymatic active site of CD38 by site-directed mutagenesis. J. Biol. Chem. 275, 21566-21571 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 21566-21571
    • Munshi, C.1    Aarhus, R.2    Graeff, R.3    Walseth, T.F.4    Levitt, D.5    Lee, H.C.6
  • 21
    • 0031429651 scopus 로고    scopus 로고
    • Large-scale production of human CD38 in yeast by fermentation
    • C. B. Munshi, K. B. Fryxell, H. C. Lee, W. D. Branton, Large-scale production of human CD38 in yeast by fermentation. Methods Enzymol. 280, 318-330 (1997).
    • (1997) Methods Enzymol. , vol.280 , pp. 318-330
    • Munshi, C.B.1    Fryxell, K.B.2    Lee, H.C.3    Branton, W.D.4
  • 23
    • 33845936792 scopus 로고    scopus 로고
    • Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis
    • Q. Liu, I. A. Kriksunov, R. Graeff, C. Munshi, H. C. Lee, Q. Hao, Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis. J. Biol. Chem. 281, 32861-32869 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 32861-32869
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Munshi, C.4    Lee, H.C.5    Hao, Q.6
  • 24
    • 53849148622 scopus 로고    scopus 로고
    • Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38
    • Q. Liu, I. A. Kriksunov, H. Jiang, R. Graeff, H. Lin, H. C. Lee, Q. Hao, Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38. Chem. Biol. 15, 1068-1078 (2008).
    • (2008) Chem. Biol. , vol.15 , pp. 1068-1078
    • Liu, Q.1    Kriksunov, I.A.2    Jiang, H.3    Graeff, R.4    Lin, H.5    Lee, H.C.6    Hao, Q.7
  • 26
    • 0037147137 scopus 로고    scopus 로고
    • Evidence for a causal role of CD38 expression in granulocytic differentiation of human HL-60 cells
    • C. B. Munshi, R. Graeff, H. C. Lee, Evidence for a causal role of CD38 expression in granulocytic differentiation of human HL-60 cells. J. Biol. Chem. 277, 49453-49458 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49453-49458
    • Munshi, C.B.1    Graeff, R.2    Lee, H.C.3
  • 27
    • 34548740853 scopus 로고    scopus 로고
    • The role of platelet/endothelial cell adhesion molecule 1 (CD31) and CD38 antigens in marrow microenvironmental retention of acute myelogenous leukemia cells
    • N. Gallay, L. Anani, A. Lopez, P. Colombat, C. Binet, J. Domenech, B. B. Weksler, F. Malavasi, O. Herault, The role of platelet/endothelial cell adhesion molecule 1 (CD31) and CD38 antigens in marrow microenvironmental retention of acute myelogenous leukemia cells. Cancer Res. 67, 8624-8632 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 8624-8632
    • Gallay, N.1    Anani, L.2    Lopez, A.3    Colombat, P.4    Binet, C.5    Domenech, J.6    Weksler, B.B.7    Malavasi, F.8    Herault, O.9
  • 28
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • M. Higy, T. Junne, M. Spiess, Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry 43, 12716-12722 (2004).
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 29
    • 34250663574 scopus 로고    scopus 로고
    • The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology
    • H. Lorenz, D. W. Hailey, C. Wunder, J. Lippincott-Schwartz, The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology. Nat. Protoc. 1, 276-279 (2006).
    • (2006) Nat. Protoc. , vol.1 , pp. 276-279
    • Lorenz, H.1    Hailey, D.W.2    Wunder, C.3    Lippincott-Schwartz, J.4
  • 30
    • 0842344106 scopus 로고    scopus 로고
    • Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators
    • G. T. Hanson, R. Aggeler, D. Oglesbee, M. Cannon, R. A. Capaldi, R. Y. Tsien, S. J. Remington, Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators. J. Biol. Chem. 279, 13044-13053 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 13044-13053
    • Hanson, G.T.1    Aggeler, R.2    Oglesbee, D.3    Cannon, M.4    Capaldi, R.A.5    Tsien, R.Y.6    Remington, S.J.7
  • 31
    • 79959365485 scopus 로고    scopus 로고
    • Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose
    • Y. J. Zhao, H. M. Zhang, C. M. C. Lam, Q. Hao, H. C. Lee, Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose. J. Biol. Chem. 286, 22170-22177 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 22170-22177
    • Zhao, Y.J.1    Zhang, H.M.2    Lam, C.M.C.3    Hao, Q.4    Lee, H.C.5
  • 33
    • 33947623627 scopus 로고    scopus 로고
    • Structure and enzymatic functions of human CD38
    • H. C. Lee, Structure and enzymatic functions of human CD38. Mol. Med. 12, 317-323 (2006).
    • (2006) Mol. Med. , vol.12 , pp. 317-323
    • Lee, H.C.1
  • 34
    • 67650653239 scopus 로고    scopus 로고
    • Mice lacking the ADP ribosyl cyclase CD38 exhibit attenuated renal vasoconstriction to angiotensin II, endothelin-1, and norepinephrine
    • T. L. Thai, W. J. Arendshorst, Mice lacking the ADP ribosyl cyclase CD38 exhibit attenuated renal vasoconstriction to angiotensin II, endothelin-1, and norepinephrine. Am. J. Physiol. Renal Physiol. 297, F169-F176 (2009).
    • (2009) Am. J. Physiol. Renal Physiol. , vol.297
    • Thai, T.L.1    Arendshorst, W.J.2
  • 35
    • 14944349319 scopus 로고    scopus 로고
    • Autocrine and paracrine calcium signaling by the CD38/NAD+/cyclic ADP-ribose system
    • A. De Flora, E. Zocchi, L. Guida, L. Franco, S. Bruzzone, Autocrine and paracrine calcium signaling by the CD38/NAD+/cyclic ADP-ribose system. Ann. N. Y. Acad. Sci. 1028, 176-191 (2004).
    • (2004) Ann. N. Y. Acad. Sci. , vol.1028 , pp. 176-191
    • De Flora, A.1    Zocchi, E.2    Guida, L.3    Franco, L.4    Bruzzone, S.5
  • 36
    • 0344610780 scopus 로고    scopus 로고
    • Subcellular and extracellular trafficking of NAD and cyclic ADP-ribose: A new way for regulating intracellular calcium homeostasis
    • H. C. Lee, Ed. Kluwer Academic Publishers, Dordrecht
    • A. De Flora, L. Guida, L. Franco, S. Bruzzone, E. Zocchi, Subcellular and extracellular trafficking of NAD and cyclic ADP-ribose: A new way for regulating intracellular calcium homeostasis, in Cyclic ADP-Ribose and NAADP. Structures, Metabolism and Functions, H. C. Lee, Ed. (Kluwer Academic Publishers, Dordrecht, 2002).
    • (2002) Cyclic ADP-Ribose and NAADP. Structures, Metabolism and Functions
    • De Flora, A.1    Guida, L.2    Franco, L.3    Bruzzone, S.4    Zocchi, E.5
  • 40
    • 0032113448 scopus 로고    scopus 로고
    • Regulation of Protein topology by trans-acting factors at the endoplasmic reticulum
    • R. S. Hegde, S. Voigt, V. R. Lingappa, Regulation of Protein topology by trans-acting factors at the endoplasmic reticulum. Mol. Cell 2, 85-91 (1998).
    • (1998) Mol. Cell , vol.2 , pp. 85-91
    • Hegde, R.S.1    Voigt, S.2    Lingappa, V.R.3
  • 41
    • 16344395798 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons
    • R. S. Stewart, D. A. Harris, A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons. J. Biol. Chem. 280, 15855-15864 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 15855-15864
    • Stewart, R.S.1    Harris, D.A.2
  • 42
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • R. S. Stewart, D. A. Harris, Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J. Biol. Chem. 278, 45960-45968 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 43
    • 38049184626 scopus 로고    scopus 로고
    • Melanocortin-2 receptor accessory protein MRAP forms antiparallel homodimers
    • J. A. Sebag, P. M. Hinkle, Melanocortin-2 receptor accessory protein MRAP forms antiparallel homodimers. Proc. Natl. Acad. Sci. U.S.A. 104, 20244-20249 (2007).
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 20244-20249
    • Sebag, J.A.1    Hinkle, P.M.2
  • 44
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology
    • G. von Heijne, The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5, 3021-3027 (1986).
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Von Heijne, G.1
  • 47
    • 0034637449 scopus 로고    scopus 로고
    • Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus
    • K. M. Khoo, M. K. Han, J. B. Park, S.W. Chae, U. H. Kim, H. C. Lee, B. H. Bay, C. F. Chang, Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus. J. Biol. Chem. 275, 24807-24817 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24807-24817
    • Khoo, K.M.1    Han, M.K.2    Park, J.B.3    Chae, S.W.4    Kim, U.H.5    Lee, H.C.6    Bay, B.H.7    Chang, C.F.8
  • 48
    • 34547216748 scopus 로고    scopus 로고
    • A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum
    • H. L. Ploegh, A lipid-based model for the creation of an escape hatch from the endoplasmic reticulum. Nature 448, 435-438 (2007).
    • (2007) Nature , vol.448 , pp. 435-438
    • Ploegh, H.L.1
  • 49
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type i membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • D. Blom, C. Hirsch, P. Stern, D. Tortorella, H. L. Ploegh, A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised. EMBO J. 23, 650-658 (2004).
    • (2004) EMBO J. , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 50
    • 58749100282 scopus 로고    scopus 로고
    • Immunoblotting and immunodetection
    • J. S. Bonifacino, M. Dasso, J. Lippincott-Schwartz, J. B. Harford, K. M. Yamada, Eds. Wiley, New York
    • S. R. Gallagher, S. E. Winston, S. A. Fuller, J. G. R. Hurrell, Immunoblotting and immunodetection, in Current Protocols in Cell Biology, J. S. Bonifacino, M. Dasso, J. Lippincott-Schwartz, J. B. Harford, K. M. Yamada, Eds. (Wiley, New York, 1998), pp. 6.2.1-6.2.20.
    • (1998) Current Protocols in Cell Biology
    • Gallagher, S.R.1    Winston, S.E.2    Fuller, S.A.3    Hurrell, J.G.R.4
  • 51
    • 0037081860 scopus 로고    scopus 로고
    • A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity
    • R. Graeff, H. C. Lee, A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity. Biochem. J. 361, 379-384 (2002).
    • (2002) Biochem. J. , vol.361 , pp. 379-384
    • Graeff, R.1    Lee, H.C.2


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