메뉴 건너뛰기




Volumn 15, Issue 4, 2004, Pages 635-646

VAMP2-dependent exocytosis regulates plasma membrane insertion of TRPC3 channels and contributes to agonist-stimulated Ca2+ influx

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SOLUBLE N ETHYLMALEIMIDE SENSITIVE FACTOR ATTACHMENT PROTEIN; BREFELDIN A; CARBACHOL; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; ION CHANNEL; PROTEIN; RECEPTOR PROTEIN; SNARE PROTEIN; SYNAPTOBREVIN; SYNAPTOBREVIN 2; TETANUS TOXIN; THAPSIGARGIN; TRANSIENT RECEPTOR PROTEIN 3; UNCLASSIFIED DRUG;

EID: 4344685732     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.07.010     Document Type: Article
Times cited : (179)

References (40)
  • 1
    • 0033759875 scopus 로고    scopus 로고
    • Evidence for a vesicle-mediated maintenance of store-operated calcium channels in a human embryonic kidney cell line
    • Alderton J.M., Ahmed S.A., Smith L.A., Steinhardt R.A. Evidence for a vesicle-mediated maintenance of store-operated calcium channels in a human embryonic kidney cell line. Cell Calcium. 28:2000;161-169
    • (2000) Cell Calcium , vol.28 , pp. 161-169
    • Alderton, J.M.1    Ahmed, S.A.2    Smith, L.A.3    Steinhardt, R.A.4
  • 2
    • 0037187771 scopus 로고    scopus 로고
    • Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current
    • Bahner M., Frechter S., Da Silva N., Minke B., Paulsen R., Huber A. Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current. Neuron. 34:2002;83-93
    • (2002) Neuron , vol.34 , pp. 83-93
    • Bahner, M.1    Frechter, S.2    Da Silva, N.3    Minke, B.4    Paulsen, R.5    Huber, A.6
  • 3
    • 0347503522 scopus 로고    scopus 로고
    • CRAC can be dissociated from regulated exocytosis in rat basophilic leukaemia (RBL-1) cells
    • CRAC can be dissociated from regulated exocytosis in rat basophilic leukaemia (RBL-1) cells. J. Physiol. 553:2003;37-93
    • (2003) J. Physiol. , vol.553 , pp. 37-93
    • Bakowski, D.1    Burgoyne, R.D.2    Parekh, A.B.3
  • 5
    • 0035844216 scopus 로고    scopus 로고
    • Role of the phospholipase C-inositol 1,4,5-trisphosphate pathway in calcium release-activated calcium current and capacitative calcium entry
    • Broad L.M., Braun F.J., Lievremont J.P., Bird G.S., Kurosaki T., Putney J.W. Jr. Role of the phospholipase C-inositol 1,4,5-trisphosphate pathway in calcium release-activated calcium current and capacitative calcium entry. J. Biol. Chem. 276:2001;15945-15952
    • (2001) J. Biol. Chem. , vol.276 , pp. 15945-15952
    • Broad, L.M.1    Braun, F.J.2    Lievremont, J.P.3    Bird, G.S.4    Kurosaki, T.5    Putney Jr., J.W.6
  • 7
    • 1342304080 scopus 로고    scopus 로고
    • Exocytotic insertion of TRPC6 channel into the plasma membrane upon Gq-protein-coupled receptor activation
    • Cayouette S., Lussier M.P., Mathieu E.L., Bousquet S.M., Boulay G. Exocytotic insertion of TRPC6 channel into the plasma membrane upon Gq-protein-coupled receptor activation. J. Biol. Chem. 279:2004;7241-7246
    • (2004) J. Biol. Chem. , vol.279 , pp. 7241-7246
    • Cayouette, S.1    Lussier, M.P.2    Mathieu, E.L.3    Bousquet, S.M.4    Boulay, G.5
  • 8
    • 0038650888 scopus 로고    scopus 로고
    • Dynamics of phosphoinositides in membrane retrieval and insertion
    • Czech M.P. Dynamics of phosphoinositides in membrane retrieval and insertion. Annual Rev. Physiol. 65:2003;791-815
    • (2003) Annual Rev. Physiol. , vol.65 , pp. 791-815
    • Czech, M.P.1
  • 9
    • 0041708061 scopus 로고    scopus 로고
    • TRPC5 is a regulator of hippocampal neurite length and growth cone morphology
    • Greka A., Navarro B., Oancea E., Duggan A., Clapham D.E. TRPC5 is a regulator of hippocampal neurite length and growth cone morphology. Nat. Neurosci. 6:2003;837-845
    • (2003) Nat. Neurosci. , vol.6 , pp. 837-845
    • Greka, A.1    Navarro, B.2    Oancea, E.3    Duggan, A.4    Clapham, D.E.5
  • 10
    • 0038383463 scopus 로고    scopus 로고
    • The dynamic organization of postsynaptic proteins: Translocating molecules regulate synaptic function
    • Inoue A., Okabe S. The dynamic organization of postsynaptic proteins. translocating molecules regulate synaptic function Curr. Opin. Neurobiol. 13:2003;332-340
    • (2003) Curr. Opin. Neurobiol. , vol.13 , pp. 332-340
    • Inoue, A.1    Okabe, S.2
  • 11
    • 0033162068 scopus 로고    scopus 로고
    • Translocation of a calcium-permeable cation channel induced by insulin-like growth factor
    • Kanzaki M. Translocation of a calcium-permeable cation channel induced by insulin-like growth factor. Nat. Cell Biol. 1:1999;165-170
    • (1999) Nat. Cell Biol. , vol.1 , pp. 165-170
    • Kanzaki, M.1
  • 12
    • 0036795577 scopus 로고    scopus 로고
    • SNARE interactions in membrane trafficking: A perspective from mammalian central synapses
    • Kavalali E.T. SNARE interactions in membrane trafficking. a perspective from mammalian central synapses Bioessays. 24:2002;926-936
    • (2002) Bioessays , vol.24 , pp. 926-936
    • Kavalali, E.T.1
  • 14
    • 0033200089 scopus 로고    scopus 로고
    • Activation of a TRPC3-dependent cation current through the neurotrophin BDNF
    • Li H.S., Xu X.Z., Montell C. Activation of a TRPC3-dependent cation current through the neurotrophin BDNF. Neuron. 24:1999;261-273
    • (1999) Neuron , vol.24 , pp. 261-273
    • Li, H.S.1    Xu, X.Z.2    Montell, C.3
  • 15
    • 0030763651 scopus 로고    scopus 로고
    • SNARE proteins, why so many, why so few?
    • Linial M. SNARE proteins, why so many, why so few? J. Neurochem. 69:1997;1781-1792
    • (1997) J. Neurochem. , vol.69 , pp. 1781-1792
    • Linial, M.1
  • 16
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains J
    • Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S., Ambudkar I.S. Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains J. Biol. Chem. 275:2000;11934-11942
    • (2000) Biol. Chem. , vol.275 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 17
    • 0035834716 scopus 로고    scopus 로고
    • 2+ influx without disruption of Trp3-inositol trisphosphate receptor association
    • 2+ influx without disruption of Trp3-inositol trisphosphate receptor association. J. Biol. Chem. 276:2001;42401-42408
    • (2001) J. Biol. Chem. , vol.276 , pp. 42401-42408
    • Lockwich, T.1    Singh, B.B.2    Liu, X.3    Ambudkar, I.S.4
  • 18
    • 0036080482 scopus 로고    scopus 로고
    • TRP channel proteins and signal transduction
    • Minke B., Cook B. TRP channel proteins and signal transduction. Physiol. Rev. 82:2002;429-472
    • (2002) Physiol. Rev. , vol.82 , pp. 429-472
    • Minke, B.1    Cook, B.2
  • 19
    • 0035838673 scopus 로고    scopus 로고
    • Physiology, phylogeny, and functions of the TRP superfamily of cation channels
    • Montell C. Physiology, phylogeny, and functions of the TRP superfamily of cation channels. Science's STKE. 90:2001;RE1
    • (2001) Science's STKE , vol.90 , pp. 1
    • Montell, C.1
  • 20
    • 2942614748 scopus 로고    scopus 로고
    • Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity
    • Published online April 5, 2004.
    • Morenilla-Palao C., Planells-Cases R., Garcia-Sanz N., Ferrer-Montiel A. Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity. J. Biol. Chem. 279:2004;25665-25672. Published online April 5, 2004.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25665-25672
    • Morenilla-Palao, C.1    Planells-Cases, R.2    Garcia-Sanz, N.3    Ferrer-Montiel, A.4
  • 21
    • 0028972114 scopus 로고
    • Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles
    • Nielsen S., Marples D., Birn H., Mohtashami M., Dalby N.O., Trimble M., Knepper M. Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with Aquaporin-. 2(water channels. J. Clin. Invest. 96):1995;1834-1844
    • (1995) Colocalization with Aquaporin , vol.2 , Issue.WATER CHANNELS. J. CLIN. INVEST. 96 , pp. 1834-1844
    • Nielsen, S.1    Marples, D.2    Birn, H.3    Mohtashami, M.4    Dalby, N.O.5    Trimble, M.6    Knepper, M.7
  • 22
    • 0030810066 scopus 로고    scopus 로고
    • Store depletion and calcium influx
    • Parekh A.B., Penner R. Store depletion and calcium influx. Physiol. Rev. 77:1997;901-930
    • (1997) Physiol. Rev. , vol.77 , pp. 901-930
    • Parekh, A.B.1    Penner, R.2
  • 26
    • 0037235442 scopus 로고    scopus 로고
    • Constitutive cycling: A general mechanism to regulate cell surface proteins
    • Royle S.J., Murrell-Lagnado R.D. Constitutive cycling. a general mechanism to regulate cell surface proteins Bioessays. 25:2003;39-46
    • (2003) Bioessays , vol.25 , pp. 39-46
    • Royle, S.J.1    Murrell-Lagnado, R.D.2
  • 27
    • 0030048838 scopus 로고    scopus 로고
    • Calcium-dependent interaction of N-type calcium channels with synaptic core complex
    • Sheng Z.H., Rettig J., Cook T., Catterall W.A. Calcium-dependent interaction of N-type calcium channels with synaptic core complex. Nature. 379:1996;451-454
    • (1996) Nature , vol.379 , pp. 451-454
    • Sheng, Z.H.1    Rettig, J.2    Cook, T.3    Catterall, W.A.4
  • 28
    • 0036142516 scopus 로고    scopus 로고
    • Distribution of high voltage-actiavted calcium channels in cultured y-amonibutyric acidergic neurons from mouse cerebral cortex
    • Timmermann D.B., Westenbroek R.E., Schousboe A., Catterall W.A. Distribution of high voltage-actiavted calcium channels in cultured y-amonibutyric acidergic neurons from mouse cerebral cortex. J. Neurosci. Res. 67:2002;48-61
    • (2002) J. Neurosci. Res. , vol.67 , pp. 48-61
    • Timmermann, D.B.1    Westenbroek, R.E.2    Schousboe, A.3    Catterall, W.A.4
  • 31
    • 0037484292 scopus 로고    scopus 로고
    • Expression level of the canonical transient receptor potential 3 (TRPC3) channel determines its mechanism of activation
    • Vazquez G., Wedel B.J., Trebak M., Bird G., Putney J.W. Jr. Expression level of the canonical transient receptor potential 3 (TRPC3) channel determines its mechanism of activation. J. Biol. Chem. 278:2003;21649-21654
    • (2003) J. Biol. Chem. , vol.278 , pp. 21649-21654
    • Vazquez, G.1    Wedel, B.J.2    Trebak, M.3    Bird, G.4    Putney Jr., J.W.5
  • 33
    • 4344604697 scopus 로고    scopus 로고
    • Intracellular organization of insulin signaling and GLUT4 translocation
    • Watson R.T., Pessin J.E. Intracellular organization of insulin signaling and GLUT4 translocation. Mol. Endocrinol. 16:2002;1060-1068
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1060-1068
    • Watson, R.T.1    Pessin, J.E.2
  • 34
    • 0037477379 scopus 로고    scopus 로고
    • A Calmodulin/IP3 receptor binding region targets TRPC3 to the plasma membrane in a calmodulin/IP3 receptor-independent process
    • Wedel B.J., Vazquez G., McKay R.R., Bird G.S., Putney J.W. Jr. A Calmodulin/IP3 receptor binding region targets TRPC3 to the plasma membrane in a calmodulin/IP3 receptor-independent process. J. Biol. Chem. 278:2003;25758-25765
    • (2003) J. Biol. Chem. , vol.278 , pp. 25758-25765
    • Wedel, B.J.1    Vazquez, G.2    McKay, R.R.3    Bird, G.S.4    Putney Jr., J.W.5
  • 36
    • 0043033098 scopus 로고    scopus 로고
    • A C. elegans sperm TRP protein required for sperm-egg interactions during fertilization
    • Xu X.Z., Sternberg P.W. A C. elegans sperm TRP protein required for sperm-egg interactions during fertilization. Cell. 114:2003;285-297
    • (2003) Cell , vol.114 , pp. 285-297
    • Xu, X.Z.1    Sternberg, P.W.2
  • 37
    • 0035845566 scopus 로고    scopus 로고
    • Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isofrom
    • Xu X.Z., Moebius F., Gill D.L., Montell C. Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isofrom. Proc. Natl. Acad. Sci. USA. 98:2001;10692-110697
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10692-110697
    • Xu, X.Z.1    Moebius, F.2    Gill, D.L.3    Montell, C.4
  • 38
    • 0033588320 scopus 로고    scopus 로고
    • 2+ current in Xenopus oocytes requires SNAP-25 but not a diffusible messenger
    • 2+ current in Xenopus oocytes requires SNAP-25 but not a diffusible messenger. Cell. 98:1999;475-485
    • (1999) Cell , vol.98 , pp. 475-485
    • Yao, Y.1    Ferrer-Montiel, A.V.2    Montal, M.3    Tsien, R.Y.4
  • 40
    • 0031594711 scopus 로고    scopus 로고
    • 2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK) 293 cells. Evidence for a non-capacitative Ca. 2+
    • 2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK) 293 cells. Evidence for a non-capacitative Ca. 2+(entry. J. Biol. Chem. 273):1998;133-142
    • (1998) J. Biol. Chem. , vol.273 , pp. 133-142
    • Zhu, X.1    Jiang, M.2    Birnbaumer, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.