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Volumn 430, Issue 3, 2010, Pages 453-460

Evidence for an interaction between Golli and STIM1 in store-operated calcium entry

Author keywords

Calcium; Endoplasmic reticulum (ER); Golli; Myelin basic protein (MBP); Stromal interaction molecule 1 (STIM1)

Indexed keywords

COMPLEXATION; MOLECULES; PROTEINS;

EID: 77956667529     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20100650     Document Type: Article
Times cited : (60)

References (41)
  • 2
    • 15544368216 scopus 로고    scopus 로고
    • Store-operated calcium channels
    • Parekh, A. B. and Putney, Jr, J. W. (2005) Store-operated calcium channels. Physiol. Rev. 85, 757-810
    • (2005) Physiol. Rev. , vol.85 , pp. 757-810
    • Parekh, A.B.1    Putney Jr., J.W.2
  • 3
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh, A. B. and Penner, R. (1997) Store depletion and calcium influx. Physiol. Rev. 77, 901-930
    • (1997) Physiol. Rev. , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 10
  • 12
    • 33748569838 scopus 로고    scopus 로고
    • 2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane
    • DOI 10.1083/jcb.200604014
    • Wu, M. M., Buchanan, J., Luik, R. M. and Lewis, R. S. (2006) Ca2+ store depletion causes STIM1 to accumulate in ER regions closely associated with the plasma membrane. J. Cell Biol. 174, 803-813 (Pubitemid 44373730)
    • (2006) Journal of Cell Biology , vol.174 , Issue.6 , pp. 803-813
    • Wu, M.M.1    Buchanan, J.2    Luik, R.M.3    Lewis, R.S.4
  • 13
    • 33748548406 scopus 로고    scopus 로고
    • 2+ entry: Local activation of CRAC channels by STIM1 at ER-plasma membrane junctions
    • 2+ entry: local activation of CRAC channels by STIM1 at ER-plasma membrane junctions. J. Cell Biol. 174, 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
  • 14
    • 55549083129 scopus 로고    scopus 로고
    • The CRAC channel consists of a tetramer formed by Stim-induced dimerization of Orai dimers
    • Penna, A., Demuro, A., Yeromin, A. V., Zhang, S. L., Safrina, O., Parker, I. and Cahalan, M. D. (2008) The CRAC channel consists of a tetramer formed by Stim-induced dimerization of Orai dimers. Nature 456, 116-120
    • (2008) Nature , vol.456 , pp. 116-120
    • Penna, A.1    Demuro, A.2    Yeromin, A.V.3    Zhang, S.L.4    Safrina, O.5    Parker, I.6    Cahalan, M.D.7
  • 18
    • 67349237167 scopus 로고    scopus 로고
    • A minimal regulatory domain in the C terminus of STIM1 binds to and activates ORAI1 CRAC channels
    • Kawasaki, T., Lange, I. and Feske, S. (2009) A minimal regulatory domain in the C terminus of STIM1 binds to and activates ORAI1 CRAC channels. Biochem. Biophys. Res. Commun. 385, 49-54
    • (2009) Biochem. Biophys. Res. Commun. , vol.385 , pp. 49-54
    • Kawasaki, T.1    Lange, I.2    Feske, S.3
  • 20
    • 66749085475 scopus 로고    scopus 로고
    • A cytosolic homomerization and a modulatory domain within STIM1 C-terminus determine coupling to ORAI1 channels
    • Muik, M., Fahrner, M., Derler, I., Schindl, R., Bergsmann, J., Frischauf, I., Groschner, K. and Romanin, C. (2009) A cytosolic homomerization and a modulatory domain within STIM1 C-terminus determine coupling to ORAI1 channels. J. Biol. Chem. 284, 8421-8426
    • (2009) J. Biol. Chem. , vol.284 , pp. 8421-8426
    • Muik, M.1    Fahrner, M.2    Derler, I.3    Schindl, R.4    Bergsmann, J.5    Frischauf, I.6    Groschner, K.7    Romanin, C.8
  • 21
    • 35748956408 scopus 로고    scopus 로고
    • Visualization and manipulation of plasma membrane-endoplasmic reticulum contact sites indicates the presence of additional molecular components within the STIM1-Orai1 Complex
    • Varnai, P., Toth, B., Toth, D. J., Hunyady, L. and Balla, T. (2007) Visualization and manipulation of plasma membrane-endoplasmic reticulum contact sites indicates the presence of additional molecular components within the STIM1-Orai1 Complex. J. Biol. Chem. 282, 29678-29690
    • (2007) J. Biol. Chem. , vol.282 , pp. 29678-29690
    • Varnai, P.1    Toth, B.2    Toth, D.J.3    Hunyady, L.4    Balla, T.5
  • 22
    • 3042567344 scopus 로고    scopus 로고
    • The golli-myelin basic protein negatively regulates signal transduction in T lymphocytes
    • Feng, J. M., Fernandes, A. O., Campagnoni, C. W., Hu, Y. H. and Campagnoni, A. T. (2004) The golli-myelin basic protein negatively regulates signal transduction in T lymphocytes. J. Neuroimmunol. 152, 57-66
    • (2004) J. Neuroimmunol. , vol.152 , pp. 57-66
    • Feng, J.M.1    Fernandes, A.O.2    Campagnoni, C.W.3    Hu, Y.H.4    Campagnoni, A.T.5
  • 23
    • 0027418817 scopus 로고
    • Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain
    • Campagnoni, A. T., Pribyl, T. M., Campagnoni, C. W., Kampf, K., Amur-Umarjee, S., Landry, C. F., Handley, V. W., Newman, S. L., Garbay, B. and Kitamura, K. (1993) Structure and developmental regulation of Golli-mbp, a 105-kilobase gene that encompasses the myelin basic protein gene and is expressed in cells in the oligodendrocyte lineage in the brain. J. Biol. Chem. 268, 4930-4938
    • (1993) J. Biol. Chem. , vol.268 , pp. 4930-4938
    • Campagnoni, A.T.1    Pribyl, T.M.2    Campagnoni, C.W.3    Kampf, K.4    Amur-Umarjee, S.5    Landry, C.F.6    Handley, V.W.7    Newman, S.L.8    Garbay, B.9    Kitamura, K.10
  • 25
    • 36248949702 scopus 로고    scopus 로고
    • Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells
    • Paez, P. M., Spreuer, V., Handley, V., Feng, J. M., Campagnoni, C. and Campagnoni, A. T. (2007) Increased expression of golli myelin basic proteins enhances calcium influx into oligodendroglial cells. J. Neurosci. 27, 12690-12699
    • (2007) J. Neurosci. , vol.27 , pp. 12690-12699
    • Paez, P.M.1    Spreuer, V.2    Handley, V.3    Feng, J.M.4    Campagnoni, C.5    Campagnoni, A.T.6
  • 28
    • 34447520503 scopus 로고    scopus 로고
    • Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III β
    • Haynes, L. P., Sherwood, M. W., Dolman, N. J. and Burgoyne, R. D. (2007) Specificity, promiscuity and localization of ARF protein interactions with NCS-1 and phosphatidylinositol-4 kinase-III β. Traffic 8, 1080-1092
    • (2007) Traffic , vol.8 , pp. 1080-1092
    • Haynes, L.P.1    Sherwood, M.W.2    Dolman, N.J.3    Burgoyne, R.D.4
  • 31
    • 38749132516 scopus 로고    scopus 로고
    • A gain-of-function mutant of Munc18-1 stimulates secretory granule recruitment and exocytosis and reveals a direct interaction of Munc18-1 with Rab3
    • Graham, M. E., Handley, M. T., Barclay, J. W., Ciufo, L. F., Barrow, S. L., Morgan, A. and Burgoyne, R. D. (2008) A gain-of-function mutant of Munc18-1 stimulates secretory granule recruitment and exocytosis and reveals a direct interaction of Munc18-1 with Rab3. Biochem. J. 409, 407-416
    • (2008) Biochem. J. , vol.409 , pp. 407-416
    • Graham, M.E.1    Handley, M.T.2    Barclay, J.W.3    Ciufo, L.F.4    Barrow, S.L.5    Morgan, A.6    Burgoyne, R.D.7
  • 32
    • 56049105171 scopus 로고    scopus 로고
    • A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins
    • Boyd, A., Ciufo, L. F., Barclay, J. W., Graham, M. E., Haynes, L. P., Doherty, M. K., Riesen, M., Burgoyne, R. D. and Morgan, A. (2008) A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins. Genetics 180, 165-178
    • (2008) Genetics , vol.180 , pp. 165-178
    • Boyd, A.1    Ciufo, L.F.2    Barclay, J.W.3    Graham, M.E.4    Haynes, L.P.5    Doherty, M.K.6    Riesen, M.7    Burgoyne, R.D.8    Morgan, A.9
  • 33
    • 70350738339 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis of inducible protein interactions: Effects of factors affecting protein folding on fluorescent protein fragment association
    • Robida, A. M. and Kerppola, T. K. (2009) Bimolecular fluorescence complementation analysis of inducible protein interactions: effects of factors affecting protein folding on fluorescent protein fragment association. J. Mol. Biol. 394, 391-409
    • (2009) J. Mol. Biol. , vol.394 , pp. 391-409
    • Robida, A.M.1    Kerppola, T.K.2
  • 35
    • 47949132511 scopus 로고    scopus 로고
    • Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation
    • Luik, R. M., Wang, B., Prakriya, M., Wu, M. M. and Lewis, R. S. (2008) Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation. Nature 454, 538-542
    • (2008) Nature , vol.454 , pp. 538-542
    • Luik, R.M.1    Wang, B.2    Prakriya, M.3    Wu, M.M.4    Lewis, R.S.5
  • 36
    • 0029657908 scopus 로고    scopus 로고
    • 2+ signals underlying waves and graded responses in HeLa cells
    • 2+ signals underlying waves and graded responses in HeLa cells. Curr. Biol. 6, 855-865
    • (1996) Curr. Biol. , vol.6 , pp. 855-865
    • Bootman, M.D.1    Berridge, M.J.2
  • 37
    • 0346422451 scopus 로고    scopus 로고
    • Calcium binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphophate-mediated calcium signalling
    • Haynes, L. P., Tepikin, A. V. and Burgoyne, R. D. (2004) Calcium binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphophate- mediated calcium signalling. J. Biol. Chem. 279, 547-555
    • (2004) J. Biol. Chem. , vol.279 , pp. 547-555
    • Haynes, L.P.1    Tepikin, A.V.2    Burgoyne, R.D.3
  • 38
    • 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. (2006) Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 443, 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
  • 39
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola, T. K. (2006) Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 7, 449-456
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 449-456
    • Kerppola, T.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.