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Volumn 42, Issue 2, 2007, Pages 157-162

The long and arduous road to CRAC

Author keywords

Calcium channel; Calcium signaling; CRAC; CRACM1; Orai1; SOC; STIM1; Store operated calcium entry; Transient receptor potential superfamily; TRPM

Indexed keywords

CALCIUM CHANNEL; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL M1; CATION CHANNEL; GENE PRODUCT; PROTEIN ORAI1; STORE OPERATED CALCIUM CHANNEL; STROMAL INTERACTION MOLECULE 1 PROTEIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; TRANSIENT RECEPTOR POTENTIAL CHANNEL M2; TRANSIENT RECEPTOR POTENTIAL CHANNEL M4; TRANSIENT RECEPTOR POTENTIAL CHANNEL M7; UNCLASSIFIED DRUG;

EID: 34447099542     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2007.03.008     Document Type: Article
Times cited : (47)

References (66)
  • 1
    • 0022575011 scopus 로고
    • A model for receptor-regulated calcium entry
    • Putney Jr. J.W. A model for receptor-regulated calcium entry. Cell Calcium 7 (1986) 1-12
    • (1986) Cell Calcium , vol.7 , pp. 1-12
    • Putney Jr., J.W.1
  • 2
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • Hoth M., and Penner R. Depletion of intracellular calcium stores activates a calcium current in mast cells. Nature 355 (1992) 353-356
    • (1992) Nature , vol.355 , pp. 353-356
    • Hoth, M.1    Penner, R.2
  • 3
    • 0035064074 scopus 로고    scopus 로고
    • Calcium signaling mechanisms in T lymphocytes
    • Lewis R.S. Calcium signaling mechanisms in T lymphocytes. Annu. Rev. Immunol. 19 (2001) 497-521
    • (2001) Annu. Rev. Immunol. , vol.19 , pp. 497-521
    • Lewis, R.S.1
  • 4
    • 0033604543 scopus 로고    scopus 로고
    • Signalling through the high-affinity IgE receptor Fc epsilonRI
    • Turner H., and Kinet J.P. Signalling through the high-affinity IgE receptor Fc epsilonRI. Nature 402 (1999) B24-B30
    • (1999) Nature , vol.402
    • Turner, H.1    Kinet, J.P.2
  • 11
    • 0037012649 scopus 로고    scopus 로고
    • TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization
    • Launay P., Fleig A., Perraud A.L., Scharenberg A.M., Penner R., and Kinet J.P. TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization. Cell 109 (2002) 397-407
    • (2002) Cell , vol.109 , pp. 397-407
    • Launay, P.1    Fleig, A.2    Perraud, A.L.3    Scharenberg, A.M.4    Penner, R.5    Kinet, J.P.6
  • 12
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction
    • Montell C., and Rubin G.M. Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction. Neuron 2 (1989) 1313-1323
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 13
    • 0026583241 scopus 로고
    • The trp gene is essential for a light-activated Ca2+ channel in Drosophila photoreceptors
    • Hardie R.C., and Minke B. The trp gene is essential for a light-activated Ca2+ channel in Drosophila photoreceptors. Neuron 8 (1992) 643-651
    • (1992) Neuron , vol.8 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 14
    • 0030815874 scopus 로고    scopus 로고
    • New light on TRP and TRPL
    • Montell C. New light on TRP and TRPL. Mol. Pharmacol. 52 (1997) 755-763
    • (1997) Mol. Pharmacol. , vol.52 , pp. 755-763
    • Montell, C.1
  • 15
    • 0035810243 scopus 로고    scopus 로고
    • CaT1 manifests the pore properties of the calcium-release-activated calcium channel
    • Yue L., Peng J.B., Hediger M.A., and Clapham D.E. CaT1 manifests the pore properties of the calcium-release-activated calcium channel. Nature 410 (2001) 705-709
    • (2001) Nature , vol.410 , pp. 705-709
    • Yue, L.1    Peng, J.B.2    Hediger, M.A.3    Clapham, D.E.4
  • 22
    • 0034618134 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP(+)) is an essential regulator of T-lymphocyte Ca(2+)-signaling
    • Berg I., Potter B.V., Mayr G.W., and Guse A.H. Nicotinic acid adenine dinucleotide phosphate (NAADP(+)) is an essential regulator of T-lymphocyte Ca(2+)-signaling. J. Cell Biol. 150 (2000) 581-588
    • (2000) J. Cell Biol. , vol.150 , pp. 581-588
    • Berg, I.1    Potter, B.V.2    Mayr, G.W.3    Guse, A.H.4
  • 23
    • 33845602018 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes
    • Beck A., Kolisek M., Bagley L.A., Fleig A., and Penner R. Nicotinic acid adenine dinucleotide phosphate and cyclic ADP-ribose regulate TRPM2 channels in T lymphocytes. FASEB J. 20 (2006) 962-964
    • (2006) FASEB J. , vol.20 , pp. 962-964
    • Beck, A.1    Kolisek, M.2    Bagley, L.A.3    Fleig, A.4    Penner, R.5
  • 26
    • 0030941654 scopus 로고    scopus 로고
    • Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase A
    • Cote G.P., Luo X., Murphy M.B., and Egelhoff T.T. Mapping of the novel protein kinase catalytic domain of Dictyostelium myosin II heavy chain kinase A. J. Biol. Chem. 272 (1997) 6846-6849
    • (1997) J. Biol. Chem. , vol.272 , pp. 6846-6849
    • Cote, G.P.1    Luo, X.2    Murphy, M.B.3    Egelhoff, T.T.4
  • 27
    • 0033611493 scopus 로고    scopus 로고
    • Alpha-kinases: a new class of protein kinases with a novel catalytic domain
    • Ryazanov A.G., Pavur K.S., and Dorovkov M.V. Alpha-kinases: a new class of protein kinases with a novel catalytic domain. Curr. Biol. 9 (1999) R43-R45
    • (1999) Curr. Biol. , vol.9
    • Ryazanov, A.G.1    Pavur, K.S.2    Dorovkov, M.V.3
  • 28
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: analysis of the family and comparison with conventional protein kinases
    • Drennan D., and Ryazanov A.G. Alpha-kinases: analysis of the family and comparison with conventional protein kinases. Prog. Biophys. Mol. Biol. 85 (2004) 1-32
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 1-32
    • Drennan, D.1    Ryazanov, A.G.2
  • 29
    • 0027746958 scopus 로고
    • Nonselective cation channels in exocrine gland cells
    • Thorn P., and Petersen O.H. Nonselective cation channels in exocrine gland cells. EXS 66 (1993) 185-200
    • (1993) EXS , vol.66 , pp. 185-200
    • Thorn, P.1    Petersen, O.H.2
  • 30
    • 0027741870 scopus 로고
    • Nonselective cation channels
    • Siemen D. Nonselective cation channels. EXS 66 (1993) 3-25
    • (1993) EXS , vol.66 , pp. 3-25
    • Siemen, D.1
  • 39
    • 33747643506 scopus 로고    scopus 로고
    • Large store-operated calcium selective currents due to co-expression of Orai1 or Orai2 with the intracellular calcium sensor, Stim1
    • Mercer J.C., Dehaven W.I., Smyth J.T., Wedel B., Boyles R.R., Bird G.S., and Putney Jr. J.W. Large store-operated calcium selective currents due to co-expression of Orai1 or Orai2 with the intracellular calcium sensor, Stim1. J. Biol. Chem. 281 (2006) 24979-24990
    • (2006) J. Biol. Chem. , vol.281 , pp. 24979-24990
    • Mercer, J.C.1    Dehaven, W.I.2    Smyth, J.T.3    Wedel, B.4    Boyles, R.R.5    Bird, G.S.6    Putney Jr., J.W.7
  • 42
    • 33748655172 scopus 로고    scopus 로고
    • Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai
    • Yeromin A.V., Zhang S.L., Jiang W., Yu Y., Safrina O., and Cahalan M.D. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 443 (2006) 226-229
    • (2006) Nature , vol.443 , pp. 226-229
    • Yeromin, A.V.1    Zhang, S.L.2    Jiang, W.3    Yu, Y.4    Safrina, O.5    Cahalan, M.D.6
  • 45
    • 18844404413 scopus 로고    scopus 로고
    • Capacitative calcium entry: sensing the calcium stores
    • Putney Jr. J.W. Capacitative calcium entry: sensing the calcium stores. J. Cell Biol. 169 (2005) 381-382
    • (2005) J. Cell Biol. , vol.169 , pp. 381-382
    • Putney Jr., J.W.1
  • 46
    • 27144515996 scopus 로고    scopus 로고
    • STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane
    • Zhang S.L., Yu Y., Roos J., Kozak J.A., Deerinck T.J., Ellisman M.H., Stauderman K.A., and Cahalan M.D. STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature 437 (2005) 902-905
    • (2005) Nature , vol.437 , pp. 902-905
    • Zhang, S.L.1    Yu, Y.2    Roos, J.3    Kozak, J.A.4    Deerinck, T.J.5    Ellisman, M.H.6    Stauderman, K.A.7    Cahalan, M.D.8
  • 47
    • 33748548406 scopus 로고    scopus 로고
    • The elementary unit of store-operated Ca2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions
    • Luik R.M., Wu M.M., Buchanan J., and Lewis R.S. The elementary unit of store-operated Ca2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions. J. Cell Biol. 174 (2006) 815-825
    • (2006) J. Cell Biol. , vol.174 , pp. 815-825
    • Luik, R.M.1    Wu, M.M.2    Buchanan, J.3    Lewis, R.S.4
  • 49
    • 34247247126 scopus 로고    scopus 로고
    • A hexahistidine-Zn2+-dye label reveals STIM1 surface exposure
    • Hauser C.T., and Tsien R.Y. A hexahistidine-Zn2+-dye label reveals STIM1 surface exposure. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3693-3697
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 3693-3697
    • Hauser, C.T.1    Tsien, R.Y.2
  • 52
    • 33748791716 scopus 로고    scopus 로고
    • Interaction of STIM1 with endogenously expressed human canonical TRP1 upon depletion of intracellular Ca2+ stores
    • Lopez J.J., Salido G.M., Pariente J.A., and Rosado J.A. Interaction of STIM1 with endogenously expressed human canonical TRP1 upon depletion of intracellular Ca2+ stores. J. Biol. Chem. 281 (2006) 28254-28264
    • (2006) J. Biol. Chem. , vol.281 , pp. 28254-28264
    • Lopez, J.J.1    Salido, G.M.2    Pariente, J.A.3    Rosado, J.A.4
  • 53
    • 0027338204 scopus 로고
    • Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx
    • Randriamampita C., and Tsien R.Y. Emptying of intracellular Ca2+ stores releases a novel small messenger that stimulates Ca2+ influx. Nature 364 (1993) 809-814
    • (1993) Nature , vol.364 , pp. 809-814
    • Randriamampita, C.1    Tsien, R.Y.2
  • 54
    • 0033587804 scopus 로고    scopus 로고
    • Store-operated Ca2+ entry: evidence for a secretion-like coupling model
    • Patterson R.L., van Rossum D.B., and Gill D.L. Store-operated Ca2+ entry: evidence for a secretion-like coupling model. Cell 98 (1999) 487-499
    • (1999) Cell , vol.98 , pp. 487-499
    • Patterson, R.L.1    van Rossum, D.B.2    Gill, D.L.3
  • 55
    • 0034677783 scopus 로고    scopus 로고
    • A role for the actin cytoskeleton in the initiation and maintenance of store-mediated calcium entry in human platelets. Evidence for conformational coupling
    • Rosado J.A., Jenner S., and Sage S.O. A role for the actin cytoskeleton in the initiation and maintenance of store-mediated calcium entry in human platelets. Evidence for conformational coupling. J. Biol. Chem. 275 (2000) 7527-7533
    • (2000) J. Biol. Chem. , vol.275 , pp. 7527-7533
    • Rosado, J.A.1    Jenner, S.2    Sage, S.O.3
  • 56
    • 0029148125 scopus 로고
    • Primaquine, an inhibitor of vesicular transport, blocks the calcium-release-activated current in rat megakaryocytes
    • Somasundaram B., Norman J.C., and Mahaut-Smith M.P. Primaquine, an inhibitor of vesicular transport, blocks the calcium-release-activated current in rat megakaryocytes. Biochem. J. 309 Pt 3 (1995) 725-729
    • (1995) Biochem. J. , vol.309 , Issue.PART 3 , pp. 725-729
    • Somasundaram, B.1    Norman, J.C.2    Mahaut-Smith, M.P.3
  • 58
    • 33747592823 scopus 로고    scopus 로고
    • Graded regulation of the Kv2.1 potassium channel by variable phosphorylation
    • Park K.S., Mohapatra D.P., Misonou H., and Trimmer J.S. Graded regulation of the Kv2.1 potassium channel by variable phosphorylation. Science 313 (2006) 976-979
    • (2006) Science , vol.313 , pp. 976-979
    • Park, K.S.1    Mohapatra, D.P.2    Misonou, H.3    Trimmer, J.S.4
  • 59
    • 0029914088 scopus 로고    scopus 로고
    • Evidence for a phorbol ester-insensitive phosphorylation step in capacitative calcium entry in rat thymic lymphocytes
    • Marriott I., and Mason M.J. Evidence for a phorbol ester-insensitive phosphorylation step in capacitative calcium entry in rat thymic lymphocytes. J. Biol. Chem. 271 (1996) 26732-26738
    • (1996) J. Biol. Chem. , vol.271 , pp. 26732-26738
    • Marriott, I.1    Mason, M.J.2
  • 60
    • 0029006156 scopus 로고
    • Slow calcium-dependent inactivation of depletion-activated calcium current. Store-dependent and -independent mechanisms
    • Zweifach A., and Lewis R.S. Slow calcium-dependent inactivation of depletion-activated calcium current. Store-dependent and -independent mechanisms. J. Biol. Chem. 270 (1995) 14445-14451
    • (1995) J. Biol. Chem. , vol.270 , pp. 14445-14451
    • Zweifach, A.1    Lewis, R.S.2
  • 61
    • 0029096601 scopus 로고
    • Depletion-activated calcium current is inhibited by protein kinase in RBL-2H3 cells
    • Parekh A.B., and Penner R. Depletion-activated calcium current is inhibited by protein kinase in RBL-2H3 cells. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 7907-7911
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7907-7911
    • Parekh, A.B.1    Penner, R.2
  • 62
    • 0027370065 scopus 로고
    • Transient inhibition by chemotactic peptide of a store-operated Ca2+ entry pathway in human neutrophils
    • Montero M., Garcia-Sancho J., and Alvarez J. Transient inhibition by chemotactic peptide of a store-operated Ca2+ entry pathway in human neutrophils. J. Biol. Chem. 268 (1993) 13055-13061
    • (1993) J. Biol. Chem. , vol.268 , pp. 13055-13061
    • Montero, M.1    Garcia-Sancho, J.2    Alvarez, J.3
  • 64
    • 0033855079 scopus 로고    scopus 로고
    • Characterization and regulation of rat microglial Ca(2+) release-activated Ca(2+) (CRAC) channel by protein kinases
    • Hahn J., Jung W., Kim N., Uhm D.Y., and Chung S. Characterization and regulation of rat microglial Ca(2+) release-activated Ca(2+) (CRAC) channel by protein kinases. Glia 31 (2000) 118-124
    • (2000) Glia , vol.31 , pp. 118-124
    • Hahn, J.1    Jung, W.2    Kim, N.3    Uhm, D.Y.4    Chung, S.5
  • 65
    • 28144463211 scopus 로고    scopus 로고
    • Inhibition by calyculin A and okadaic acid of the Ca(2+) release-activated Ca(2+) entry pathway in rat basophilic leukemia cells: evidence for regulation by type 1/2A serine/threonine phosphatase activity
    • Evans N.E., Forth M.K., Simpson A.K., and Mason M.J. Inhibition by calyculin A and okadaic acid of the Ca(2+) release-activated Ca(2+) entry pathway in rat basophilic leukemia cells: evidence for regulation by type 1/2A serine/threonine phosphatase activity. Biochim. Biophys. Acta 1718 (2005) 32-43
    • (2005) Biochim. Biophys. Acta , vol.1718 , pp. 32-43
    • Evans, N.E.1    Forth, M.K.2    Simpson, A.K.3    Mason, M.J.4
  • 66
    • 0028067169 scopus 로고
    • Phosphorylation down-regulates the store-operated Ca2+ entry pathway of human neutrophils
    • Montero M., Garcia-Sancho J., and Alvarez J. Phosphorylation down-regulates the store-operated Ca2+ entry pathway of human neutrophils. J. Biol. Chem. 269 (1994) 3963-3967
    • (1994) J. Biol. Chem. , vol.269 , pp. 3963-3967
    • Montero, M.1    Garcia-Sancho, J.2    Alvarez, J.3


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