메뉴 건너뛰기




Volumn 165, Issue 3, 2000, Pages 1220-1227

Transient translocation of the B cell receptor and Src homology 2 domain-containing inositol phosphatase to lipid rafts: Evidence toward a role in calcium regulation

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CALCIUM; INOSITOL PHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0034254193     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.165.3.1220     Document Type: Article
Times cited : (130)

References (55)
  • 1
    • 0030831199 scopus 로고    scopus 로고
    • The complexity of signaling pathways activated by the BCR
    • DeFranco, A. L. 1997. The complexity of signaling pathways activated by the BCR. Curr. Opin. Immunol. 9:296.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 296
    • DeFranco, A.L.1
  • 2
    • 0030795735 scopus 로고    scopus 로고
    • Molecular mechanisms in B cell antigen receptor signaling
    • Kurosaki, T. 1997. Molecular mechanisms in B cell antigen receptor signaling. Curr. Opin. Immunol. 9:309.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 309
    • Kurosaki, T.1
  • 3
    • 0030890949 scopus 로고    scopus 로고
    • Initiation and processing of signals from the B cell antigen receptor
    • Reth, M., and J. Wienands. 1997. Initiation and processing of signals from the B cell antigen receptor. Annu. Rev. Immunol. 15:453.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 453
    • Reth, M.1    Wienands, J.2
  • 4
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature 387:589.
    • (1997) Nature , vol.387 , pp. 589
    • Simons, K.1    Ikonen, E.2
  • 5
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D. A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell. Dev. Biol. 14:111.
    • (1998) Annu. Rev. Cell. Dev. Biol. , vol.14 , pp. 111
    • Brown, D.A.1    London, E.2
  • 6
    • 0031692336 scopus 로고    scopus 로고
    • The caveolae membrane system
    • Anderson, R. G. 1998. The caveolae membrane system. Annu. Rev. Biochem. 67:199.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 199
    • Anderson, R.G.1
  • 7
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and S. Mayor, 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798.
    • (1998) Nature , vol.394 , pp. 798
    • Varma, R.1    Mayor, S.2
  • 8
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by crosslinking
    • Friedrichson, T., and T. V. Kurzchalia. 1998. Microdomains of GPI-anchored proteins in living cells revealed by crosslinking. Nature 394:802.
    • (1998) Nature , vol.394 , pp. 802
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 9
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder, R. J., S. N. Ahmed, Y. Zhu, E. London, and D. A. Brown. 1998. Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J. Biol. Chem. 273:1150.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1150
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 10
    • 0032527642 scopus 로고    scopus 로고
    • Structure and origin of ordered lipid domains in biological membranes
    • Brown, D. A., and E. London. 1998. Structure and origin of ordered lipid domains in biological membranes. J. Membr. Biol. 164:103.
    • (1998) J. Membr. Biol. , vol.164 , pp. 103
    • Brown, D.A.1    London, E.2
  • 11
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A. M., D. J. Dietzen, J. Kwong, D. C. Link, and D. M. Lublin. 1994. Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353.
    • (1994) J. Cell Biol. , vol.126 , pp. 353
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 12
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins, S. M., N. A. Quintrell, and J. M. Bishop. 1995. Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15:3507.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 13
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan, G., M. Parenti, and A. I. Magee. 1995. The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20:181.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 14
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, B., T. Brennan, Q. Li, C. McCormack, and B. Seed. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity 8:723.
    • (1998) Immunity , vol.8 , pp. 723
    • Xavier, B.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 15
    • 0032142953 scopus 로고    scopus 로고
    • LAT palmitoylation: Its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation
    • Zhang, W., R. P. Trible, and L. E. Samelson. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9:239.
    • (1998) Immunity , vol.9 , pp. 239
    • Zhang, W.1    Trible, R.P.2    Samelson, L.E.3
  • 16
    • 0033993454 scopus 로고    scopus 로고
    • Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes
    • Kabouridis, P. S., J. Janzen, A. L. Magee, and S. C. Ley. 2000. Cholesterol depletion disrupts lipid rafts and modulates the activity of multiple signaling pathways in T lymphocytes. Eur. J. Immunol. 30:954.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 954
    • Kabouridis, P.S.1    Janzen, J.2    Magee, A.L.3    Ley, S.C.4
  • 17
    • 0029858008 scopus 로고    scopus 로고
    • Lovastatin inhibits T-cell antigen receptor signaling independent of its effects on ras
    • Goldman, F., R. J. Hohl, J. Crabtree, K. Lewis-Tibesar, and G. Koretzky. 1996. Lovastatin inhibits T-cell antigen receptor signaling independent of its effects on ras. Blood 88:4611.
    • (1996) Blood , vol.88 , pp. 4611
    • Goldman, F.1    Hohl, R.J.2    Crabtree, J.3    Lewis-Tibesar, K.4    Koretzky, G.5
  • 19
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field, K. A., D. Holowka, and B. Baird. 1997. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:4276.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 21
    • 0031962079 scopus 로고    scopus 로고
    • Rapid redistribution of CD20 to a low-density detergent-insoluble membrane compartment
    • Deans, J. P., S. R. Robbins, M. J. Polyak, and J. A. Savage. 1998. Rapid redistribution of CD20 to a low-density detergent-insoluble membrane compartment. J. Biol. Chem. 273:344.
    • (1998) J. Biol. Chem. , vol.273 , pp. 344
    • Deans, J.P.1    Robbins, S.R.2    Polyak, M.J.3    Savage, J.A.4
  • 22
    • 0033431772 scopus 로고    scopus 로고
    • A role for lipid rafts in B cell antigen receptor signaling and antigen targeting
    • Cheng, P. C., M. L. Dykstra, R. N. Mitchell, and S. K. Pierce. 1999. A role for lipid rafts in B cell antigen receptor signaling and antigen targeting. J. Exp. Med. 190:1549.
    • (1999) J. Exp. Med. , vol.190 , pp. 1549
    • Cheng, P.C.1    Dykstra, M.L.2    Mitchell, R.N.3    Pierce, S.K.4
  • 23
    • 0005517434 scopus 로고
    • Role of the Bp35 cell surface polypeptide in human B-cell activation
    • Clark, E. A., G. Shu, and J. A. Ledbetter. 1985. Role of the Bp35 cell surface polypeptide in human B-cell activation. Proc. Natl. Acad. Sci. USA 82:1766.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1766
    • Clark, E.A.1    Shu, G.2    Ledbetter, J.A.3
  • 24
    • 0039493929 scopus 로고    scopus 로고
    • Targeting of a G α subunit (Gil α) and c-Src tyrosine kinase to caveolae membranes: Clarifying the role of N-myristoylation
    • Song, K. S., M. Sargiacomo, F. Galbiati, M. Parenti, and M. P. Lisanti. 1997. Targeting of a G α subunit (Gil α) and c-Src tyrosine kinase to caveolae membranes: clarifying the role of N-myristoylation. Cell Mol. Biol. 43:293.
    • (1997) Cell Mol. Biol. , vol.43 , pp. 293
    • Song, K.S.1    Sargiacomo, M.2    Galbiati, F.3    Parenti, M.4    Lisanti, M.P.5
  • 25
    • 0029091389 scopus 로고
    • The ligand-induced membrane IgM association with the cytoskeletal matrix of B cells is not mediated through the Ig αβ heterodimer
    • Hartwig, J. H., L. S. Jugloff, N. J. De Groot, S. A. Grupp, and J. Jongstra-Bilen. 1995. The ligand-induced membrane IgM association with the cytoskeletal matrix of B cells is not mediated through the Ig αβ heterodimer. J. Immunol. 155: 3769.
    • (1995) J. Immunol. , vol.155 , pp. 3769
    • Hartwig, J.H.1    Jugloff, L.S.2    De Groot, N.J.3    Grupp, S.A.4    Jongstra-Bilen, J.5
  • 26
    • 0031202421 scopus 로고    scopus 로고
    • Cross-linking of the IgM receptor induces rapid translocation of IgM-associated Ig α, Lyn, and Syk tyrosine kinases to the membrane skeleton
    • Jugloff, L. S., and J. Jongstra-Bilen. 1997. Cross-linking of the IgM receptor induces rapid translocation of IgM-associated Ig α, Lyn, and Syk tyrosine kinases to the membrane skeleton. J. Immunol. 159:1096.
    • (1997) J. Immunol. , vol.159 , pp. 1096
    • Jugloff, L.S.1    Jongstra-Bilen, J.2
  • 27
    • 0029051899 scopus 로고
    • Multisubunit receptors in the immune system and their association with the cytoskeleton: In search of functional significance
    • Caplan, S., and M. Baniyash. 1995. Multisubunit receptors in the immune system and their association with the cytoskeleton: in search of functional significance. Immunol. Res. 14:98.
    • (1995) Immunol. Res. , vol.14 , pp. 98
    • Caplan, S.1    Baniyash, M.2
  • 28
    • 0033082977 scopus 로고    scopus 로고
    • Antigen-stimulated dissociation of BCR mIg from Ig-α/Ig-β: Implications for receptor desensitization
    • Vilen, B. J., T. Nakamura, and J. C. Cambier. 1999. Antigen-stimulated dissociation of BCR mIg from Ig-α/Ig-β: implications for receptor desensitization. Immunity 10:239.
    • (1999) Immunity , vol.10 , pp. 239
    • Vilen, B.J.1    Nakamura, T.2    Cambier, J.C.3
  • 29
    • 0030453582 scopus 로고    scopus 로고
    • lck associated with glycolipid-enriched membrane domains
    • lck associated with glycolipid-enriched membrane domains. J. Cell Biol. 135:1515.
    • (1996) J. Cell Biol. , vol.135 , pp. 1515
    • Rodgers, W.1    Rose, J.K.2
  • 30
    • 0026568357 scopus 로고
    • Interaction of CD4:lck with the T cell receptor/CD3 complex induces early signaling events in the absence of CD45 tyrosine phosphatase
    • Deans, J. P., S. B. Kanner, R. M. Torres, and J. A. Ledbetter. 1992. Interaction of CD4:lck with the T cell receptor/CD3 complex induces early signaling events in the absence of CD45 tyrosine phosphatase. Eur. J. Immunol. 22:661.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 661
    • Deans, J.P.1    Kanner, S.B.2    Torres, R.M.3    Ledbetter, J.A.4
  • 31
    • 0033558102 scopus 로고    scopus 로고
    • The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes
    • D'Oro, U., and J. D. Ashwell. 1999. The CD45 tyrosine phosphatase is an inhibitor of Lck activity in thymocytes. J. Immunol. 162:1879.
    • (1999) J. Immunol. , vol.162 , pp. 1879
    • D'Oro, U.1    Ashwell, J.D.2
  • 32
    • 0029779003 scopus 로고    scopus 로고
    • Mutational analysis of Lck in CD45-negative T cells: Dominant role of tyrosine 394 phosphorylation in kinase activity
    • D'Oro, U., K. Sakaguchi, E. Appella, and J. D. Ashwell. 1996. Mutational analysis of Lck in CD45-negative T cells: dominant role of tyrosine 394 phosphorylation in kinase activity. Mol. Cell Biol. 16:4996.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 4996
    • D'Oro, U.1    Sakaguchi, K.2    Appella, E.3    Ashwell, J.D.4
  • 34
    • 0023718731 scopus 로고
    • Drug solubilizers to aid pharmacologists: Amorphous cyclodextrin derivatives
    • Pitha, J., T. Irie, P. B. Sklar, and J. S. Nye. 1988. Drug solubilizers to aid pharmacologists: amorphous cyclodextrin derivatives. Life Sci. 43:493.
    • (1988) Life Sci. , vol.43 , pp. 493
    • Pitha, J.1    Irie, T.2    Sklar, P.B.3    Nye, J.S.4
  • 35
    • 0024806367 scopus 로고
    • Differential effects of α-, β- and γ-cyclodextrins on human erythrocytes
    • Ohtani, Y., T. Irie, K. Uekama, K. Fukunaga, and J. Pitha. 1989. Differential effects of α-, β- and γ-cyclodextrins on human erythrocytes. Eur. J. Biochem. 186:17.
    • (1989) Eur. J. Biochem. , vol.186 , pp. 17
    • Ohtani, Y.1    Irie, T.2    Uekama, K.3    Fukunaga, K.4    Pitha, J.5
  • 37
  • 38
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • Ilangumaran, S., and D. C. Hoessli. 1998. Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane. Biochem. J. 335:433.
    • (1998) Biochem. J. , vol.335 , pp. 433
    • Ilangumaran, S.1    Hoessli, D.C.2
  • 39
    • 0033387429 scopus 로고    scopus 로고
    • Activation and tyrosine phosphorylation of protein kinase Cδ in response to B cell antigen receptor stimulation
    • Popoff, I. J., and J. P. Deans. 1999. Activation and tyrosine phosphorylation of protein kinase Cδ in response to B cell antigen receptor stimulation. Mol. Immunol. 36:1005.
    • (1999) Mol. Immunol. , vol.36 , pp. 1005
    • Popoff, I.J.1    Deans, J.P.2
  • 40
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi, T., and R. G. Anderson. 1998. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J. Biol. Chem. 273: 21099.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099
    • Furuchi, T.1    Anderson, R.G.2
  • 41
    • 0032992072 scopus 로고    scopus 로고
    • Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
    • Zhang, W., B. J. Irvin, R. P. Trible, R. T. Abraham, and L. E. Samelson. 1999. Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line. Int. Immunol. 11:943.
    • (1999) Int. Immunol. , vol.11 , pp. 943
    • Zhang, W.1    Irvin, B.J.2    Trible, R.P.3    Abraham, R.T.4    Samelson, L.E.5
  • 42
    • 0032212728 scopus 로고    scopus 로고
    • LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway
    • Finco, T. S., T. Kadlecek, W. Zhang, L. E. Samelson, and A. Weiss. 1998. LAT is required for TCR-mediated activation of PLCγ1 and the Ras pathway. Immunity 9:617.
    • (1998) Immunity , vol.9 , pp. 617
    • Finco, T.S.1    Kadlecek, T.2    Zhang, W.3    Samelson, L.E.4    Weiss, A.5
  • 43
    • 0032856990 scopus 로고    scopus 로고
    • Localization of LAT in glycolipid-enriched microdomains is required for T cell activation
    • Lin, J., A. Weiss, and T. S. Finco. 1999. Localization of LAT in glycolipid-enriched microdomains is required for T cell activation. J. Biol. Chem. 274: 28861.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28861
    • Lin, J.1    Weiss, A.2    Finco, T.S.3
  • 44
    • 0032938630 scopus 로고    scopus 로고
    • The adaptor protein SLP-65/ BLNK controls the calcium response in activated B cells
    • Wollscheid, B., J. Wienands, and M. Reth. 1999. The adaptor protein SLP-65/ BLNK controls the calcium response in activated B cells. Curr. Top Microbiol. Immunol. 246:283.
    • (1999) Curr. Top Microbiol. Immunol. , vol.246 , pp. 283
    • Wollscheid, B.1    Wienands, J.2    Reth, M.3
  • 46
    • 0032127159 scopus 로고    scopus 로고
    • BLNK: A central linker protein in B cell activation
    • Fu, C., C. W. Turck, T. Kurosaki, and A. C. Chan. 1998. BLNK: a central linker protein in B cell activation. Immunity 9:93.
    • (1998) Immunity , vol.9 , pp. 93
    • Fu, C.1    Turck, C.W.2    Kurosaki, T.3    Chan, A.C.4
  • 47
    • 0033959733 scopus 로고    scopus 로고
    • BLNK: Connecting Syk and Btk to calcium signals
    • Kurosaki, T., and S. Tsukada. 2000. BLNK: connecting Syk and Btk to calcium signals. Immunity 12:1.
    • (2000) Immunity , vol.12 , pp. 1
    • Kurosaki, T.1    Tsukada, S.2
  • 48
    • 0029926545 scopus 로고    scopus 로고
    • Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains
    • Pike, L. J., and L. Casey. 1996. Localization and turnover of phosphatidylinositol 4,5-bisphosphate in caveolin-enriched membrane domains. J. Biol. Chem. 271: 26453.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26453
    • Pike, L.J.1    Casey, L.2
  • 49
    • 0029899011 scopus 로고    scopus 로고
    • Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains
    • Hope, H. R., and L. J. Pike. 1996. Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains. Mol. Biol. Cell 7:843.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 843
    • Hope, H.R.1    Pike, L.J.2
  • 50
    • 0032055485 scopus 로고    scopus 로고
    • SHIP modulates immune receptor responses by regulating membrane association of Btk
    • Bolland, S., R. N. Pearse, T. Kurosaki, and J. V. Ravetch. 1998. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity 8:509.
    • (1998) Immunity , vol.8 , pp. 509
    • Bolland, S.1    Pearse, R.N.2    Kurosaki, T.3    Ravetch, J.V.4
  • 51
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: A target for SHIP-mediated inhibitory signals
    • Scharenberg, A. M., O. El-Hillal, D. A. Fruman, L. O. Beitz, Z. Li, S. Lin, I. Gout, L. C. Cantley, D. J. Rawlings, and J. P. Kinet. 1998. Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 17:1961.
    • (1998) EMBO J. , vol.17 , pp. 1961
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6    Gout, I.7    Cantley, L.C.8    Rawlings, D.J.9    Kinet, J.P.10
  • 53
    • 0029835940 scopus 로고    scopus 로고
    • Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB
    • Ono, M., S. Bolland, P. Tempst, and J. V. Ravetch. 1996. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor FcγRIIB. Nature 383:263.
    • (1996) Nature , vol.383 , pp. 263
    • Ono, M.1    Bolland, S.2    Tempst, P.3    Ravetch, J.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.