Cited by 225Ion Channels and ReceptorsCalcium signaling and nucleotide metabolismIon channel regulation and function

Calcium signalling and cell-fate choice in B cells

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Scharenberg, Andrew M., Humphries, Lisa A., Rawlings, David J.·2007·Nature Reviews Immunology

Abstract

Alterations in the cytosolic concentration of calcium ions (Ca2+) transmit information that is crucial for the development and function of B cells. Cytosolic Ca2+ concentration is determined by a balance of active transport and gradient-driven Ca2+ fluxes, both of which are subject to the influence of multiple receptors and environmental sensing pathways. Recent advances in genomics have allowed for the compilation of an increasingly comprehensive list of Ca2+ transporters and channels expressed by B cells. The increasing understanding of the function and regulation of these proteins has begun to shift the frontier of Ca2+ physiology in B cells from molecular analysis to determining how diverse inputs to cytosolic Ca2+ concentration are integrated in specific immunological contexts.

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  • Anti-IgM antibodies stimulate B cells through the B cell receptor (BCR) thereby activating downstream signaling cascades like PI3K, AKT and MAPK pathways.

    “Anti-IgM antibodies stimulate B cells through the B cell receptor (BCR) thereby activating further downstream signaling cascades like the phosphatidylinositol 3-kinase (PI3K), protein kinase B (AKT) and mitogen-activated protein kinase (MAPK) pathways [51–53].”

    From The oncoprotein TBX3 is controlling severity in experimental arthritis (2019) · cites this paper as [51]

    The Introduction describes BCR engagement activating a signalling complex and identifies PI3K as part of BCR signalling. It does not establish that anti-IgM antibodies activate the claimed AKT and MAPK pathways; MAPK appears only in the title of a cited reference. (LLM, conf=0.86)

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  1. [1]Quintana A, Griesemer D, Schwarz EC, Hoth M. Calcium-dependent activation of T-lymphocytes. Pflugers Arch. 2005;450:1–12. doi: 10.1007/s00424-004-1364-4. [DOI] [PubMed] [Google Scholar] · DOI
  2. [2]Lewis RS. Calcium signaling mechanisms in T lymphocytes. Annu Rev Immunol. 2001;19:497–521. doi: 10.1146/annurev.immunol.19.1.497. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  3. [3]Cahalan MD, Wulff H, Chandy KG. Molecular properties and physiological roles of ion channels in the immune system. J Clin Immunol. 2001;21:235–252. doi: 10.1023/a:1010958907271. [DOI] [PubMed] [Google Scholar] · DOI
  4. [4]Brose N, Betz A, Wegmeyer H. Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals. Curr Opin Neurobiol. 2004;14:328–340. doi: 10.1016/j.conb.2004.05.006. [DOI] [PubMed] [Google Scholar] · DOI
  5. [5]Rhee SG. Regulation of phosphoinositide-specific phospholipase C. Annu Rev Biochem. 2001;70:281–312. doi: 10.1146/annurev.biochem.70.1.281. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI · Paper page
  6. [6]Parekh AB, Penner R. Store depletion and calcium influx. Physiol Rev. 1997;77:901–930. doi: 10.1152/physrev.1997.77.4.901. [DOI] [PubMed] [Google Scholar] · DOI
  7. [7]Lewis RS. The molecular choreography of a store-operated calcium channel. Nature. 2007;446:284–287. doi: 10.1038/nature05637. [DOI] [PubMed] [Google Scholar] · DOI
  8. [8]Cahalan MD, et al. Molecular basis of the CRAC channel. Cell Calcium. 2007 doi: 10.1016/j.ceca.2007.03.002. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  9. [9]Roos J, et al. STIM1, an essential and conserved component of store-operated Ca2+ channel function. J Cell Biol. 2005;169:435–445. doi: 10.1083/jcb.200502019. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  10. [10]Zhang SL, et al. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature. 2005;437:902–905. doi: 10.1038/nature04147. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  11. [11]Liou J, et al. STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx. Curr Biol. 2005;15:1235–1241. doi: 10.1016/j.cub.2005.05.055. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  12. [12]Vig M, et al. CRACM1 multimers form the ion-selective pore of the CRAC channel. Curr Biol. 2006;16:2073–2079. doi: 10.1016/j.cub.2006.08.085. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  13. [13]Yeromin AV, et al. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature. 2006;443:226–229. doi: 10.1038/nature05108. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  14. [14]Prakriya M, et al. Orai1 is an essential pore subunit of the CRAC channel. Nature. 2006;443:230–233. doi: 10.1038/nature05122. [DOI] [PubMed] [Google Scholar] · DOI
  15. [15]Luik RM, Wu MM, Buchanan J, Lewis RS. The elementary unit of store-operated Ca2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions. J Cell Biol. 2006;174:815–825. doi: 10.1083/jcb.200604015. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  16. [16]Wu MM, Buchanan J, Luik RM, Lewis RS. Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane. J Cell Biol. 2006;174:803–813. doi: 10.1083/jcb.200604014. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  17. [17]Bautista DM, Hoth M, Lewis RS. Enhancement of calcium signalling dynamics and stability by delayed modulation of the plasma-membrane calcium-ATPase in human T cells. J Physiol. 2002;541:877–894. doi: 10.1113/jphysiol.2001.016154. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  18. [18]Bautista DM, Lewis RS. Modulation of plasma membrane calcium-ATPase activity by local calcium microdomains near CRAC channels in human T cells. J Physiol. 2004;556:805–817. doi: 10.1113/jphysiol.2003.060004. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  19. [19]Parekh AB, Fleig A, Penner R. The store-operated calcium current I(CRAC): nonlinear activation by InsP3 and dissociation from calcium release. Cell. 1997;89:973–980. doi: 10.1016/s0092-8674(00)80282-2. [DOI] [PubMed] [Google Scholar] · DOI
  20. [20]Takata M, Homma Y, Kurosaki T. Requirement of phospholipase C-gamma 2 activation in surface immunoglobulin M-induced B cell apoptosis. J Exp Med. 1995;182:907–914. doi: 10.1084/jem.182.4.907. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  21. [22]Fu C, Turck CW, Kurosaki T, Chan AC. BLNK: a central linker protein in B cell activation. Immunity. 1998;9:93–103. doi: 10.1016/s1074-7613(00)80591-9. [DOI] [PubMed] [Google Scholar] · DOI
  22. [23]Taguchi T, et al. Deficiency of BLNK hampers PLC-gamma2 phosphorylation and Ca2+ influx induced by the pre-B-cell receptor in human pre-B cells. Immunology. 2004;112:575–582. doi: 10.1111/j.1365-2567.2004.01918.x. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  23. [24]Baba Y, et al. BLNK mediates Syk-dependent Btk activation. Proc Natl Acad Sci U S A. 2001;98:2582–2586. doi: 10.1073/pnas.051626198. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  24. [25]Ishiai M, et al. BLNK required for coupling Syk to PLC gamma 2 and Rac1-JNK in B cells. Immunity. 1999;10:117–125. doi: 10.1016/s1074-7613(00)80012-6. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  25. [27]Hashimoto S, et al. Identification of the SH2 domain binding protein of Bruton's tyrosine kinase as BLNK--functional significance of Btk-SH2 domain in B-cell antigen receptor-coupled calcium signaling. Blood. 1999;94:2357–2364. [PubMed] [Google Scholar]
  26. [28]Pappu R, et al. Requirement for B cell linker protein (BLNK) in B cell development. Science. 1999;286:1949–1954. doi: 10.1126/science.286.5446.1949. [DOI] [PubMed] [Google Scholar] · DOI
  27. [29]Minegishi Y, et al. An essential role for BLNK in human B cell development. Science. 1999;286:1954–1957. doi: 10.1126/science.286.5446.1954. [DOI] [PubMed] [Google Scholar] · DOI
  28. [30]Saito K, Scharenberg AM, Kinet JP. Interaction between the Btk PH domain and phosphatidylinositol-3,4,5-trisphosphate directly regulates Btk. J Biol Chem. 2001;276:16201–16206. doi: 10.1074/jbc.M100873200. [DOI] [PubMed] [Google Scholar] · DOI
  29. [31]Scharenberg AM, et al. 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. 1998;17:1961–1972. doi: 10.1093/emboj/17.7.1961. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  30. [32]Kim SK, et al. Point mutations in the split PLC-gamma1 PH domain modulate phosphoinositide binding. J Biochem Mol Biol. 2004;37:720–725. doi: 10.5483/bmbrep.2004.37.6.720. [DOI] [PubMed] [Google Scholar] · DOI
  31. [33]Saito K, et al. BTK regulates PtdIns-4,5-P2 synthesis: importance for calcium signaling and PI3K activity. Immunity. 2003;19:669–678. doi: 10.1016/s1074-7613(03)00297-8. [DOI] [PubMed] [Google Scholar] · DOI
  32. [34]Fruman DA, et al. Impaired B cell development and proliferation in absence of phosphoinositide 3-kinase p85alpha. Science. 1999;283:393–397. doi: 10.1126/science.283.5400.393. [DOI] [PubMed] [Google Scholar] · DOI
  33. [35]Okkenhaug K, et al. Impaired B and T cell antigen receptor signaling in p110delta PI 3-kinase mutant mice. Science. 2002;297:1031–1034. doi: 10.1126/science.1073560. [DOI] [PubMed] [Google Scholar] · DOI
  34. [36]Humphries LA, et al. Tec kinases mediate sustained calcium influx via site-specific tyrosine phosphorylation of the phospholipase Cgamma Src homology 2-Src homology 3 linker. J Biol Chem. 2004;279:37651–37661. doi: 10.1074/jbc.M311985200. [DOI] [PubMed] [Google Scholar] · DOI
  35. [37]Tsukada S, et al. Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia. Cell. 1993;72:279–290. doi: 10.1016/0092-8674(93)90667-f. [DOI] [PubMed] [Google Scholar] · DOI
  36. [38]Yu PW, et al. Sustained correction of B-cell development and function in a murine model of X-linked agammaglobulinemia (XLA) using retroviral-mediated gene transfer. Blood. 2004;104:1281–1290. doi: 10.1182/blood-2003-09-3044. [DOI] [PubMed] [Google Scholar] · DOI
  37. [39]Rodriguez R, et al. Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling. J Biol Chem. 2001;276:47982–47992. doi: 10.1074/jbc.M107577200. [DOI] [PubMed] [Google Scholar] · DOI
  38. [41]Kerner JD, et al. Impaired expansion of mouse B cell progenitors lacking Btk. Immunity. 1995;3:301–312. doi: 10.1016/1074-7613(95)90115-9. [DOI] [PubMed] [Google Scholar] · DOI
  39. [42]Rawlings DJ, et al. Mutation of unique region of Bruton's tyrosine kinase in immunodeficient XID mice. Science. 1993;261:358–361. doi: 10.1126/science.8332901. [DOI] [PubMed] [Google Scholar] · DOI
  40. [43]Haas KM, Tedder TF. Role of the CD19 and CD21/35 receptor complex in innate immunity, host defense and autoimmunity. Adv Exp Med Biol. 2005;560:125–139. doi: 10.1007/0-387-24180-9_16. [DOI] [PubMed] [Google Scholar] · DOI
  41. [44]Rickert RC. Regulation of B lymphocyte activation by complement C3 and the B cell coreceptor complex. Curr Opin Immunol. 2005;17:237–243. doi: 10.1016/j.coi.2005.03.001. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  42. [45]Carter RH, Barrington RA. Signaling by the CD19/CD21 complex on B cells. Curr Dir Autoimmun. 2004;7:4–32. doi: 10.1159/000075685. [DOI] [PubMed] [Google Scholar] · DOI
  43. [46]Tuveson DA, Carter RH, Soltoff SP, Fearon DT. CD19 of B cells as a surrogate kinase insert region to bind phosphatidylinositol 3-kinase. Science. 1993;260:986–989. doi: 10.1126/science.7684160. [DOI] [PubMed] [Google Scholar] · DOI
  44. [47]Weng WK, Jarvis L, LeBien TW. Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. J Biol Chem. 1994;269:32514–32521. [PubMed] [Google Scholar]
  45. [48]Carter RH, Fearon DT. CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. Science. 1992;256:105–107. [PubMed] [Google Scholar]
  46. [49]Wang Y, Carter RH. CD19 regulates B cell maturation, proliferation, and positive selection in the FDC zone of murine splenic germinal centers. Immunity. 2005;22:749–761. doi: 10.1016/j.immuni.2005.04.012. [DOI] [PubMed] [Google Scholar] · DOI
  47. [50]Phillips NE, Parker DC. Fc-dependent inhibition of mouse B cell activation by whole anti-mu antibodies. J Immunol. 1983;130:602–606. [PubMed] [Google Scholar]
  48. [51]Tony HP, Schimpl A. Stimulation of murine B cells with anti-Ig antibodies: dominance of a negative signal mediated by the Fc receptor. Eur J Immunol. 1980;10:726–729. doi: 10.1002/eji.1830100914. [DOI] [PubMed] [Google Scholar] · DOI
  49. [52]Wilson HA, et al. The B lymphocyte calcium response to anti-Ig is diminished by membrane immunoglobulin cross-linkage to the Fc gamma receptor. J Immunol. 1987;138:1712–1718. [PubMed] [Google Scholar]
  50. [53]Ono M, Bolland S, Tempst P, Ravetch JV. Role of the inositol phosphatase SHIP in negative regulation of the immune system by the receptor Fc(gamma)RIIB. Nature. 1996;383:263–266. doi: 10.1038/383263a0. [DOI] [PubMed] [Google Scholar] · DOI
  51. [54]D'Ambrosio D, et al. Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1. Science. 1995;268:293–297. doi: 10.1126/science.7716523. [DOI] [PubMed] [Google Scholar] · DOI
  52. [55]Bolland S, Pearse RN, Kurosaki T, Ravetch JV. SHIP modulates immune receptor responses by regulating membrane association of Btk. Immunity. 1998;8:509–516. doi: 10.1016/s1074-7613(00)80555-5. [DOI] [PubMed] [Google Scholar] · DOI
  53. [56]Hippen KL, et al. Fc gammaRIIB1 inhibition of BCR-mediated phosphoinositide hydrolysis and Ca2+ mobilization is integrated by CD19 dephosphorylation. Immunity. 1997;7:49–58. doi: 10.1016/s1074-7613(00)80509-9. [DOI] [PubMed] [Google Scholar] · DOI
  54. [57]Fong DC, et al. Mutational analysis reveals multiple distinct sites within Fc gamma receptor IIB that function in inhibitory signaling. J Immunol. 2000;165:4453–4462. doi: 10.4049/jimmunol.165.8.4453. [DOI] [PubMed] [Google Scholar] · DOI
  55. [58]Fong DC, et al. Selective in vivo recruitment of the phosphatidylinositol phosphatase SHIP by phosphorylated Fc gammaRIIB during negative regulation of IgE-dependent mouse mast cell activation. Immunol Lett. 1996;54:83–91. doi: 10.1016/s0165-2478(96)02654-5. [DOI] [PubMed] [Google Scholar] · DOI
  56. [59]Ono M, et al. Deletion of SHIP or SHP-1 reveals two distinct pathways for inhibitory signaling. Cell. 1997;90:293–301. doi: 10.1016/s0092-8674(00)80337-2. [DOI] [PubMed] [Google Scholar] · DOI
  57. [60]Sato S, Tuscano JM, Inaoki M, Tedder TF. CD22 negatively and positively regulates signal transduction through the B lymphocyte antigen receptor. Semin Immunol. 1998;10:287–297. doi: 10.1006/smim.1998.0121. [DOI] [PubMed] [Google Scholar] · DOI
  58. [61]Nitschke L, Carsetti R, Ocker B, Kohler G, Lamers MC. CD22 is a negative regulator of B-cell receptor signalling. Curr Biol. 1997;7:133–143. doi: 10.1016/s0960-9822(06)00057-1. [DOI] [PubMed] [Google Scholar] · DOI
  59. [62]Otipoby KL, et al. CD22 regulates thymus-independent responses and the lifespan of B cells. Nature. 1996;384:634–637. doi: 10.1038/384634a0. [DOI] [PubMed] [Google Scholar] · DOI
  60. [63]Chen J, et al. CD22 attenuates calcium signaling by potentiating plasma membrane calcium-ATPase activity. Nat Immunol. 2004;5:651–657. doi: 10.1038/ni1072. [DOI] [PubMed] [Google Scholar] · DOI
  61. [64]Nitschke L. The role of CD22 and other inhibitory co-receptors in B-cell activation. Curr Opin Immunol. 2005;17:290–297. doi: 10.1016/j.coi.2005.03.005. [DOI] [PubMed] [Google Scholar] · DOI
  62. [65]Poe JC, et al. Severely impaired B lymphocyte proliferation, survival, and induction of the c-Myc:Cullin 1 ubiquitin ligase pathway resulting from CD22 deficiency on the C57BL/6 genetic background. J Immunol. 2004;172:2100–2110. doi: 10.4049/jimmunol.172.4.2100. [DOI] [PubMed] [Google Scholar] · DOI
  63. [66]Danzer CP, Collins BE, Blixt O, Paulson JC, Nitschke L. Transitional and marginal zone B cells have a high proportion of unmasked CD22: implications for BCR signaling. Int Immunol. 2003;15:1137–1147. doi: 10.1093/intimm/dxg114. [DOI] [PubMed] [Google Scholar] · DOI
  64. [67]Samardzic T, et al. CD22 regulates early B cell development in BOB.1/OBF.1-deficient mice. Eur J Immunol. 2002;32:2481–2489. doi: 10.1002/1521-4141(200209)32:9<2481::AID-IMMU2481>3.0.CO;2-C. [DOI] [PubMed] [Google Scholar] · DOI
  65. [68]Asano N. B Lymphocyte signaling established by the CD19/CD22 loop regulates autoimmunity in the tight-skin mouse. Am J Pathol. 2004;165:641–650. doi: 10.1016/S0002-9440(10)63328-7. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  66. [69]O'Keefe TL, Williams GT, Batista FD, Neuberger MS. Deficiency in CD22, a B cellspecific inhibitory receptor, is sufficient to predispose to development of high affinity autoantibodies. J Exp Med. 1999;189:1307–1313. doi: 10.1084/jem.189.8.1307. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  67. [70]Vianna-Jorge R, Suarez-Kurtz G. Potassium channels in T lymphocytes: therapeutic targets for autoimmune disorders? BioDrugs. 2004;18:329–341. doi: 10.2165/00063030-200418050-00005. [DOI] [PubMed] [Google Scholar] · DOI
  68. [71]Chandy KG, et al. K+ channels as targets for specific immunomodulation. Trends Pharmacol Sci. 2004;25:280–289. doi: 10.1016/j.tips.2004.03.010. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  69. [72]Panyi G. Biophysical and pharmacological aspects of K+ channels in T lymphocytes. Eur Biophys J. 2005;34:515–529. doi: 10.1007/s00249-005-0499-3. [DOI] [PubMed] [Google Scholar] · DOI
  70. [73]Panyi G, Varga Z, Gaspar R. Ion channels and lymphocyte activation. Immunol Lett. 2004;92:55–66. doi: 10.1016/j.imlet.2003.11.020. [DOI] [PubMed] [Google Scholar] · DOI
  71. [74]Wulff H, Knaus HG, Pennington M, Chandy KG. K+ channel expression during B cell differentiation: implications for immunomodulation and autoimmunity. J Immunol. 2004;173:776–786. doi: 10.4049/jimmunol.173.2.776. [DOI] [PubMed] [Google Scholar] · DOI
  72. [75]Owsianik G, Talavera K, Voets T, Nilius B. Permeation and Selectivity of TRP Channels. Annu Rev Physiol. 2005;68:685–717. doi: 10.1146/annurev.physiol.68.040204.101406. [DOI] [PubMed] [Google Scholar] · DOI
  73. [76]Launay P, et al. TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization. Cell. 2002;109:397–407. doi: 10.1016/s0092-8674(02)00719-5. [DOI] [PubMed] [Google Scholar] · DOI
  74. [77]Prawitt D, et al. TRPM5 is a transient Ca2+-activated cation channel responding to rapid changes in [Ca2+]i. Proc Natl Acad Sci U S A. 2003;100:15166–15171. doi: 10.1073/pnas.2334624100. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  75. [78]Launay P, et al. TRPM4 regulates calcium oscillations after T cell activation. Science. 2004;306:1374–1377. doi: 10.1126/science.1098845. [DOI] [PubMed] [Google Scholar] · DOI
  76. [79]Vennekens R, et al. Increased IgE-dependent mast cell activation and anaphylactic responses in mice lacking the calcium-activated nonselective cation channel TRPM4. Nat Immunol. 2007;8:312–320. doi: 10.1038/ni1441. [DOI] [PubMed] [Google Scholar] · DOI
  77. [80]Mori Y, et al. Transient receptor potential 1 regulates capacitative Ca(2+) entry and Ca(2+) release from endoplasmic reticulum in B lymphocytes. J Exp Med. 2002;195:673–681. doi: 10.1084/jem.20011758. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  78. [81]Zhu MX, Tang J. TRPC channel interactions with calmodulin and IP3 receptors. Novartis Found Symp. 2004;258:44–58. discussion 58–62, 98–102, 263–266. [PubMed] [Google Scholar]
  79. [82]Tang J, et al. Identification of common binding sites for calmodulin and inositol 1,4,5-trisphosphate receptors on the carboxyl termini of trp channels. J Biol Chem. 2001;276:21303–21310. doi: 10.1074/jbc.M102316200. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  80. [83]Zhang Z, et al. Activation of Trp3 by inositol 1,4,5-trisphosphate receptors through displacement of inhibitory calmodulin from a common binding domain. Proc Natl Acad Sci U S A. 2001;98:3168–3173. doi: 10.1073/pnas.051632698. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  81. [84]Boulay G, et al. Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5-trisphosphate receptor (IP3R) that bind transient receptor potential (TRP): evidence for roles of TRP and IP3R in store depletion-activated Ca(2+) entry. Proc Natl Acad Sci U S A. 1999;96:14955–14960. doi: 10.1073/pnas.96.26.14955. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  82. [85]Huang GN, et al. STIM1 carboxyl-terminus activates native SOC, I(crac) and TRPC1 channels. Nat Cell Biol. 2006;8:1003–1010. doi: 10.1038/ncb1454. [DOI] [PubMed] [Google Scholar] · DOI
  83. [86]Ong HL, et al. Dynamic assembly of TRPC1/STIM1/Orai1 ternary complex is involved in store operated calcium influx: Evidence for similarities in SOC and CRAC channel components. J Biol Chem. 2007;282:9105–9116. doi: 10.1074/jbc.M608942200. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  84. [87]Rosker C, et al. Ca(2+) signaling by TRPC3 involves Na(+) entry and local coupling to the Na(+)/Ca(2+) exchanger. J Biol Chem. 2004;279:13696–13704. doi: 10.1074/jbc.M308108200. [DOI] [PubMed] [Google Scholar] · DOI
  85. [88]Basu S, Srivastava P. Immunological role of neuronal receptor vanilloid receptor 1 expressed on dendritic cells. Proc Natl Acad Sci U S A. 2005;102:5120–5125. doi: 10.1073/pnas.0407780102. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  86. [89]Amantini C, et al. Distinct thymocyte subsets express the vanilloid receptor VR1 that mediates capsaicin-induced apoptotic cell death. Cell Death Differ. 2004;11:1342–1356. doi: 10.1038/sj.cdd.4401506. [DOI] [PubMed] [Google Scholar] · DOI
  87. [90]Nadler MJ, et al. LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability. Nature. 2001;411:590–595. doi: 10.1038/35079092. [DOI] [PubMed] [Google Scholar] · DOI
  88. [91]Perraud AL, et al. ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. Nature. 2001;411:595–599. doi: 10.1038/35079100. [DOI] [PubMed] [Google Scholar] · DOI
  89. [92]Inada H, Iida T, Tominaga M. Different expression patterns of TRP genes in murine B and T lymphocytes. Biochem Biophys Res Commun. 2006;350:762–767. doi: 10.1016/j.bbrc.2006.09.111. [DOI] [PubMed] [Google Scholar] · DOI
  90. [93]Liu X, Zhu P, Freedman BD. Multiple Eicosanoid-Activated Non-Selective Cation Channels Regulate B Lymphocyte Adhesion to Integrin Ligands. Am J Physiol Cell Physiol. 2005;290:c873–c882. doi: 10.1152/ajpcell.00229.2005. [DOI] [PubMed] [Google Scholar] · DOI
  91. [94]Zhu P, Liu X, Labelle EF, Freedman BD. Mechanisms of hypotonicity-induced calcium signaling and integrin activation by arachidonic acid-derived inflammatory mediators in B cells. J Immunol. 2005;175:4981–4989. doi: 10.4049/jimmunol.175.8.4981. [DOI] [PubMed] [Google Scholar] · DOI
  92. [95]Liu QH, et al. Distinct calcium channels regulate responses of primary B lymphocytes to B cell receptor engagement and mechanical stimuli. J Immunol. 2005;174:68–79. doi: 10.4049/jimmunol.174.1.68. [DOI] [PubMed] [Google Scholar] · DOI
  93. [96]Kotturi MF, Jefferies WA. Molecular characterization of L-type calcium channel splice variants expressed in human T lymphocytes. Mol Immunol. 2005;42:1461–1474. doi: 10.1016/j.molimm.2005.01.014. [DOI] [PubMed] [Google Scholar] · DOI
  94. [97]Savignac M, et al. Dihydropyridine receptors are selective markers of Th2 cells and can be targeted to prevent Th2-dependent immunopathological disorders. J Immunol. 2004;172:5206–5212. doi: 10.4049/jimmunol.172.9.5206. [DOI] [PubMed] [Google Scholar] · DOI
  95. [98]Stokes L, Gordon J, Grafton G. Non-voltage-gated L-type Ca2+ channels in human T cells: pharmacology and molecular characterization of the major alpha pore-forming and auxiliary beta-subunits. J Biol Chem. 2004;279:19566–19573. doi: 10.1074/jbc.M401481200. [DOI] [PubMed] [Google Scholar] · DOI
  96. [99]Dolmetsch RE, Lewis RS, Goodnow CC, Healy JI. Differential activation of transcription factors induced by Ca2+ response amplitude and duration. Nature. 1997;386:855–858. doi: 10.1038/386855a0. [DOI] [PubMed] [Google Scholar] · DOI
  97. [100]Healy JI, et al. Different nuclear signals are activated by the B cell receptor during positive versus negative signaling. Immunity. 1997;6:419–428. doi: 10.1016/s1074-7613(00)80285-x. [DOI] [PubMed] [Google Scholar] · DOI
  98. [101]Macian F. NFAT proteins: key regulators of T-cell development and function. Nat Rev Immunol. 2005;5:472–484. doi: 10.1038/nri1632. [DOI] [PubMed] [Google Scholar] · DOI
  99. [102]Liu JO. The yins of T cell activation. Sci STKE 2005. 2005:re1. doi: 10.1126/stke.2652005re1. [DOI] [PubMed] [Google Scholar] · DOI
  100. [103]Hogan PG, Chen L, Nardone J, Rao A. Transcriptional regulation by calcium, calcineurin, and NFAT. Genes Dev. 2003;17:2205–2232. doi: 10.1101/gad.1102703. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  101. [104]Guo B, Su TT, Rawlings DJ. Protein kinase C family functions in B-cell activation. Curr Opin Immunol. 2004;16:367–373. doi: 10.1016/j.coi.2004.03.012. [DOI] [PubMed] [Google Scholar] · DOI
  102. [105]Hanson CJ, Bootman MD, Roderick HL. Cell signalling: IP3 receptors channel calcium into cell death. Curr Biol. 2004;14:R933–R935. doi: 10.1016/j.cub.2004.10.019. [DOI] [PubMed] [Google Scholar] · DOI
  103. [106]Butow RA, Avadhani NG. Mitochondrial signaling: the retrograde response. Mol Cell. 2004;14:1–15. doi: 10.1016/s1097-2765(04)00179-0. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  104. [107]Jaattela M, Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol. 2003;4:416–423. doi: 10.1038/ni0503-416. [DOI] [PubMed] [Google Scholar] · DOI
  105. [108]Perl A, Gergely P, Jr, Puskas F, Banki K. Metabolic switches of T-cell activation and apoptosis. Antioxid Redox Signal. 2002;4:427–443. doi: 10.1089/15230860260196227. [DOI] [PubMed] [Google Scholar] · DOI
  106. [109]Rathmell JC. Apoptosis and B cell tolerance. Curr Dir Autoimmun. 2003;6:38–60. doi: 10.1159/000066855. [DOI] [PubMed] [Google Scholar] · DOI
  107. [110]Bhakta NR, Oh DY, Lewis RS. Calcium oscillations regulate thymocyte motility during positive selection in the three-dimensional thymic environment. Nat Immunol. 2005;6:143–151. doi: 10.1038/ni1161. [DOI] [PubMed] [Google Scholar] · DOI
  108. [111]Aneiros E, Philipp S, Lis A, Freichel M, Cavalie A. Modulation of Ca2+ signaling by Na+/Ca2+ exchangers in mast cells. J Immunol. 2005;174:119–130. doi: 10.4049/jimmunol.174.1.119. [DOI] [PubMed] [Google Scholar] · DOI
  109. [112]Eder P, Poteser M, Romanin C, Groschner K. Na(+) entry and modulation of Na(+)/Ca(2+) exchange as a key mechanism of TRPC signaling. Pflugers Arch. 2005;451:99–104. doi: 10.1007/s00424-005-1434-2. [DOI] [PubMed] [Google Scholar] · DOI
  110. [113]Guerini D, Coletto L, Carafoli E. Exporting calcium from cells. Cell Calcium. 2005;38:281–289. doi: 10.1016/j.ceca.2005.06.032. [DOI] [PubMed] [Google Scholar] · DOI
  111. [114]Strehler EE, Treiman M. Calcium pumps of plasma membrane and cell interior. Curr Mol Med. 2004;4:323–335. doi: 10.2174/1566524043360735. [DOI] [PubMed] [Google Scholar] · DOI
  112. [115]Wuytack F, Raeymaekers L, Missiaen L. Molecular physiology of the SERCA and SPCA pumps. Cell Calcium. 2002;32:279–305. doi: 10.1016/s0143416002001847. [DOI] [PubMed] [Google Scholar] · DOI
  113. [116]Kirichok Y, Krapivinsky G, Clapham DE. The mitochondrial calcium uniporter is a highly selective ion channel. Nature. 2004;427:360–364. doi: 10.1038/nature02246. [DOI] [PubMed] [Google Scholar] · DOI · Paper page
  114. [117]Hoth M, Button DC, Lewis RS. Mitochondrial control of calcium-channel gating: a mechanism for sustained signaling and transcriptional activation in T lymphocytes. Proc Natl Acad Sci U S A. 2000;97:10607–10612. doi: 10.1073/pnas.180143997. [DOI] [PMC free article] [PubMed] [Google Scholar] · DOI
  115. [118]Saris NE, Carafoli E. A historical review of cellular calcium handling, with emphasis on mitochondria. Biochemistry (Mosc) 2005;70:187–194. doi: 10.1007/s10541-005-0100-9. [DOI] [PubMed] [Google Scholar] · DOI
  116. [119]Jacobson J, Duchen MR. Interplay between mitochondria and cellular calcium signalling. Mol Cell Biochem. 2004;256–257:209–218. doi: 10.1023/b:mcbi.0000009869.29827.df. [DOI] [PubMed] [Google Scholar] · DOI
  117. [120]Gunter TE, Yule DI, Gunter KK, Eliseev RA, Salter JD. Calcium and mitochondria. FEBS Lett. 2004;567:96–102. doi: 10.1016/j.febslet.2004.03.071. [DOI] [PubMed] [Google Scholar] · DOI
  118. [121]Patterson RL, Boehning D, Snyder SH. Inositol 1,4,5-trisphosphate receptors as signal integrators. Annu Rev Biochem. 2004;73:437–465. doi: 10.1146/annurev.biochem.73.071403.161303. [DOI] [PubMed] [Google Scholar] · DOI

Cited by

Sorted by citations

Authors
Scharenberg, A. M., Humphries, L. A., & Rawlings, D. J.
Affiliations
Seattle Children's Hospital (US)
Corresponding author
  • Scharenberg, Andrew M.
  • Rawlings, David J.
Venue
Nature Reviews Immunology
Published
2007-10
Volume
7
Issue
10
Pages
778-789
ISSN
  • 1474-1733 (ISSN-L)
  • 1474-1741
OpenAlex
W2011593699
Cited by
225
References
3
Citations by year
2026: 4 · 2025: 6 · 2024: 10 · 2023: 9 · 2022: 15 · 2021: 13 · 2020: 15 · 2019: 10 · 2018: 7 · 2017: 12 · 2016: 15 · 2015: 12 · 2014: 9 · 2013: 6 · 2012: 17
FWCI
1.44
Type
journal article
Language
en
Open access
Locations
  • Nature reviews. Immunology (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Heart, Lung, and Blood Institute (HL07543)
  • National Cancer Institute (R01CA081140, CA 81140)
  • National Institute of General Medical Sciences (R01GM064091, P01GM078195, R01GM064316, GM64316, GM64091)
  • National Institute of Allergy and Infectious Diseases (AI45901, AI044259, R01AI044259, R01AI045901)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD37091, R01HD037091)
Topics
  • Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Calcium signaling and nucleotide metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Keywords
calcium signaling, B cells, intracellular calcium, cell fate determination, calcium transporters, calcium channels, calcium flux, calcium homeostasis, B cell development, B cell function, signal integration
MeSH terms
Animals, B-Lymphocytes, Calcium, Cytosol, Humans, Receptors, Antigen, B-Cell, Inositol 1,4,5-Trisphosphate, Calcium Signaling, Phospholipase C gamma

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