메뉴 건너뛰기




Volumn 110, Issue 2, 2009, Pages 520-529

Dominant role of lipid rafts L-type calcium channel in activity-dependent potentiation of large dense-core vesicle exocytosis

Author keywords

Activity dependent potentiation; Amperometry; Chromaffin cells; Lipid rafts; Vesicle; Voltage gated calcium channel

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CALCIUM CHANNEL BLOCKING AGENT; CALCIUM CHANNEL L TYPE; CALCIUM CHANNEL Q TYPE; CALCIUM ION; G PROTEIN COUPLED RECEPTOR; MARCKS PROTEIN; NIFEDIPINE; OMEGA AGATOXIN IVA; OMEGA CONOTOXIN GVIA; OMEGA CONOTOXIN MVIIC; PROTEIN KINASE C EPSILON; PURINERGIC P2X RECEPTOR; VOLTAGE GATED CALCIUM CHANNEL;

EID: 67649515448     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2009.06148.x     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 20444486130 scopus 로고    scopus 로고
    • The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters
    • DOI 10.1074/jbc.M413307200
    • Aoyagi K., Sugaya T., Umeda M., Yamamoto S., Terakawa S. Takahashi M. (2005) The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters. J. Biol. Chem. 280, 17346 17352. (Pubitemid 41389204)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.17 , pp. 17346-17352
    • Aoyagi, K.1    Sugaya, T.2    Umeda, M.3    Yamamoto, S.4    Terakawa, S.5    Takahashi, M.6
  • 2
    • 0037083896 scopus 로고    scopus 로고
    • Cross-talk unfolded: MARCKS proteins
    • DOI 10.1042/0264-6021:3620001
    • Arbuzova A., Schmitz A. A. Vergeres G. (2002) Cross-talk unfolded: MARCKS proteins. Biochem. J. 362, 1 12. (Pubitemid 34174456)
    • (2002) Biochemical Journal , vol.362 , Issue.1 , pp. 1-12
    • Arbuzova, A.1    Schmitz, A.A.P.2    Vergeres, G.3
  • 3
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown D. A. Rose J. K. (1992) Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533 544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 4
    • 25644436461 scopus 로고    scopus 로고
    • Essential role for the PKC target MARCKS in maintaining dendritic spine morphology
    • DOI 10.1016/j.neuron.2005.08.027, PII S0896627305007026
    • Calabrese B. Halpain S. (2005) Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Neuron 48, 77 90. (Pubitemid 41384167)
    • (2005) Neuron , vol.48 , Issue.1 , pp. 77-90
    • Calabrese, B.1    Halpain, S.2
  • 6
    • 0036304982 scopus 로고    scopus 로고
    • 2+ sensor that triggers exocytosis?
    • DOI 10.1038/nrm855
    • Chapman E. R. (2002) Synaptotagmin: a Ca(2+) sensor that triggers exocytosis? Nat. Rev. Mol. Cell Biol. 3, 498 508. (Pubitemid 34733431)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.7 , pp. 498-508
    • Chapman, E.R.1
  • 7
    • 0029794544 scopus 로고    scopus 로고
    • Dihydropyridine-sensitive and -insensitive voltage-operated calcium channels participate in the control of glucose-induced insulin release from human pancreatic β cells
    • Davalli A. M., Biancardi E., Pollo A., Socci C., Pontiroli A. E., Pozza G., Clementi F., Sher E. Carbone E. (1996) Dihydropyridine-sensitive and -insensitive voltage-operated calcium channels participate in the control of glucose-induced insulin release from human pancreatic beta cells. J. Endocrinol. 150, 195 203. (Pubitemid 26295614)
    • (1996) Journal of Endocrinology , vol.150 , Issue.2 , pp. 195-203
    • Davalli, A.M.1    Biancardi, E.2    Pollo, A.3    Socci, C.4    Pontiroli, A.E.5    Pozza, G.6    Clementi, F.7    Sher, E.8    Carbone, E.9
  • 8
    • 34447117683 scopus 로고    scopus 로고
    • Regulation of SNARE fusion machinery by fatty acids
    • DOI 10.1007/s00018-007-6557-5
    • Davletov B., Connell E. Darios F. (2007) Regulation of SNARE fusion machinery by fatty acids. Cell. Mol. Life Sci. 64, 1597 1608. (Pubitemid 47036938)
    • (2007) Cellular and Molecular Life Sciences , vol.64 , Issue.13 , pp. 1597-1608
    • Davletov, B.1    Connell, E.2    Darios, F.3
  • 9
    • 33749836234 scopus 로고    scopus 로고
    • Phosphoinositides in cell regulation and membrane dynamics
    • DOI 10.1038/nature05185, PII NATURE05185
    • Di Paolo G. De Camilli P. (2006) Phosphoinositides in cell regulation and membrane dynamics. Nature 443, 651 657. (Pubitemid 44564702)
    • (2006) Nature , vol.443 , Issue.7112 , pp. 651-657
    • Di Paolo, G.1    De Camilli, P.2
  • 10
    • 0028848411 scopus 로고
    • Role of calcium channel subtypes in calcium transients in hippocampal CA3 neurons
    • Elliott E. M., Malouf A. T. Catterall W. A. (1995) Role of calcium channel subtypes in calcium transients in hippocampal CA3 neurons. J. Neurosci. 15, 6433 6444.
    • (1995) J. Neurosci. , vol.15 , pp. 6433-6444
    • Elliott, E.M.1    Malouf, A.T.2    Catterall, W.A.3
  • 12
    • 0037039169 scopus 로고    scopus 로고
    • Subcellular distribution of high-voltage-activated calcium channel subtypes in rat globus pallidus neurons
    • Hanson J. E. Smith Y. (2002) Subcellular distribution of high-voltage-activated calcium channel subtypes in rat globus pallidus neurons. J. Comp. Neurol. 442, 89 98.
    • (2002) J. Comp. Neurol. , vol.442 , pp. 89-98
    • Hanson, J.E.1    Smith, Y.2
  • 13
    • 0027171638 scopus 로고
    • Protein kinase C phosphorylates Ser152, Ser156 and Ser163 but not Ser160 of MARCKS in rat brain
    • Heemskerk F. M., Chen H. C. Huang F. L. (1993) Protein kinase C phosphorylates Ser152, Ser156 and Ser163 but not Ser160 of MARCKS in rat brain. Biochem. Biophys. Res. Commun. 190, 236 241.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 236-241
    • Heemskerk, F.M.1    Chen, H.C.2    Huang, F.L.3
  • 14
    • 0035031224 scopus 로고    scopus 로고
    • Coupling of L-type voltage-sensitive calcium channels to P2X(2) purinoceptors in PC-12 cells
    • Hur E. M., Park T. J. Kim K. T. (2001) Coupling of L-type voltage-sensitive calcium channels to P2X(2) purinoceptors in PC-12 cells. Am. J. Physiol. Cell Physiol. 280, C1121 C1129.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Hur, E.M.1    Park, T.J.2    Kim, K.T.3
  • 15
    • 1242316984 scopus 로고    scopus 로고
    • Sensitization of epidermal growth factor-induced signaling by bradykinin is mediated by c-Src: Implications for a role of lipid microdomains
    • DOI 10.1074/jbc.M311687200
    • Hur E. M., Park Y. S., Lee B. D., Jang I. H., Kim H. S., Kim T. D., Suh P. G., Ryu S. H. Kim K. T. (2004) Sensitization of epidermal growth factor-induced signaling by bradykinin is mediated by c-Src. Implications for a role of lipid microdomains. J. Biol. Chem. 279, 5852 5860. (Pubitemid 38220617)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5852-5860
    • Hur, E.-M.1    Park, Y.-S.2    Lee, B.D.3    Jang, I.H.4    Kim, H.S.5    Kim, T.-D.6    Suh, P.-G.7    Ryu, S.H.8    Kim, K.-T.9
  • 16
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • DOI 10.1146/annurev.biochem.68.1.863
    • Jahn R. Sudhof T. C. (1999) Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863 911. (Pubitemid 29449211)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 17
    • 0033543237 scopus 로고    scopus 로고
    • Phospholipase C-delta1 is activated by capacitative calcium entry that follows phospholipase C-beta activation upon bradykinin stimulation
    • Kim Y. H., Park T. J., Lee Y. H., Baek K. J., Suh P. G., Ryu S. H. Kim K. T. (1999) Phospholipase C-delta1 is activated by capacitative calcium entry that follows phospholipase C-beta activation upon bradykinin stimulation. J. Biol. Chem. 274, 26127 26134.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26127-26134
    • Kim, Y.H.1    Park, T.J.2    Lee, Y.H.3    Baek, K.J.4    Suh, P.G.5    Ryu, S.H.6    Kim, K.T.7
  • 18
    • 37249068200 scopus 로고    scopus 로고
    • SNARE proteins and 'membrane rafts'
    • DOI 10.1113/jphysiol.2007.134346
    • Lang T. (2007) SNARE proteins and 'membrane rafts'. J. Physiol. 585, 693 698. (Pubitemid 350278707)
    • (2007) Journal of Physiology , vol.585 , Issue.3 , pp. 693-698
    • Lang, T.1
  • 19
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • DOI 10.1093/emboj/20.9.2202
    • Lang T., Bruns D., Wenzel D., Riedel D., Holroyd P., Thiele C. Jahn R. (2001) SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J. 20, 2202 2213. (Pubitemid 32410590)
    • (2001) EMBO Journal , vol.20 , Issue.9 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5    Thiele, C.6    Jahn, R.7
  • 22
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • DOI 10.1126/science.1142614
    • Martens S., Kozlov M. M. McMahon H. T. (2007) How synaptotagmin promotes membrane fusion. Science 316, 1205 1208. (Pubitemid 46877485)
    • (2007) Science , vol.316 , Issue.5828 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 23
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • DOI 10.1038/nature04398
    • McLaughlin S. Murray D. (2005) Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438, 605 611. (Pubitemid 41740564)
    • (2005) Nature , vol.438 , Issue.7068 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 25
    • 24044538530 scopus 로고    scopus 로고
    • Analysis of exocytotic events recorded by amperometry
    • DOI 10.1038/nmeth782
    • Mosharov E. V. Sulzer D. (2005) Analysis of exocytotic events recorded by amperometry. Nat. Methods 2, 651 658. (Pubitemid 41223090)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 651-658
    • Mosharov, E.V.1    Sulzer, D.2
  • 26
    • 32644434472 scopus 로고    scopus 로고
    • Activity-dependent potentiation of large dense-core vesicle release modulated by mitogen-activated protein kinase/extracellularly regulated kinase signaling
    • Park Y. S., Jun D. J., Hur E. M., Lee S. K., Suh B. S. Kim K. T. (2006a) Activity-dependent potentiation of large dense-core vesicle release modulated by mitogen-activated protein kinase/extracellularly regulated kinase signaling. Endocrinology 147, 1349 1356.
    • (2006) Endocrinology , vol.147 , pp. 1349-1356
    • Park, Y.S.1    Jun, D.J.2    Hur, E.M.3    Lee, S.K.4    Suh, B.S.5    Kim, K.T.6
  • 27
    • 33748266082 scopus 로고    scopus 로고
    • Involvement of protein kinase C-ε in activity-dependent potentiation of large dense-core vesicle exocytosis in chromaffin cells
    • DOI 10.1523/JNEUROSCI.2828-06.2006
    • Park Y. S., Hur E. M., Choi B. H., Kwak E., Jun D. J., Park S. J. Kim K. T. (2006b) Involvement of protein kinase C-epsilon in activity-dependent potentiation of large dense-core vesicle exocytosis in chromaffin cells. J. Neurosci. 26, 8999 9005. (Pubitemid 44319389)
    • (2006) Journal of Neuroscience , vol.26 , Issue.35 , pp. 8999-9005
    • Park, Y.-S.1    Hur, E.-M.2    Choi, B.-H.3    Kwak, E.4    Jun, D.-J.5    Park, S.-J.6    Kim, K.-T.7
  • 28
    • 53249119328 scopus 로고    scopus 로고
    • Non-genomic glucocorticoid effects on activity-dependent potentiation of catecholamine release in chromaffin cells
    • Park Y. S., Choi Y. H., Park C. H. Kim K. T. (2008) Non-genomic glucocorticoid effects on activity-dependent potentiation of catecholamine release in chromaffin cells. Endocrinology 149, 4921 4927.
    • (2008) Endocrinology , vol.149 , pp. 4921-4927
    • Park, Y.S.1    Choi, Y.H.2    Park, C.H.3    Kim, K.T.4
  • 29
    • 33749529365 scopus 로고    scopus 로고
    • Ternary SNARE complexes are enriched in lipid rafts during mast cell exocytosis
    • DOI 10.1111/j.1600-0854.2006.00490.x
    • Puri N. Roche P. A. (2006) Ternary SNARE complexes are enriched in lipid rafts during mast cell exocytosis. Traffic 7, 1482 1494. (Pubitemid 44524521)
    • (2006) Traffic , vol.7 , Issue.11 , pp. 1482-1494
    • Puri, N.1    Roche, P.A.2
  • 30
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • DOI 10.1111/j.1600-0854.2004.0162.x
    • Salaun C., James D. J. Chamberlain L. H. (2004) Lipid rafts and the regulation of exocytosis. Traffic 5, 255 264. (Pubitemid 38455749)
    • (2004) Traffic , vol.5 , Issue.4 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 31
    • 21244500528 scopus 로고    scopus 로고
    • Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells
    • DOI 10.1074/jbc.M501923200
    • Salaun C., Gould G. W. Chamberlain L. H. (2005) Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells. J. Biol. Chem. 280, 19449 19453. (Pubitemid 41379464)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.20 , pp. 19449-19453
    • Salaun, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 32
    • 20444428727 scopus 로고    scopus 로고
    • Presynaptic calcium and control of vesicle fusion
    • DOI 10.1016/j.conb.2005.05.006, PII S0959438805000711
    • Schneggenburger R. Neher E. (2005) Presynaptic calcium and control of vesicle fusion. Curr. Opin. Neurobiol. 15, 266 274. (Pubitemid 40806437)
    • (2005) Current Opinion in Neurobiology , vol.15 , Issue.3 SPEC. ISS. , pp. 266-274
    • Schneggenburger, R.1    Neher, E.2
  • 34
    • 0035943628 scopus 로고    scopus 로고
    • Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components
    • Spizz G. Blackshear P. J. (2001) Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components. J. Biol. Chem. 276, 32264 32273.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32264-32273
    • Spizz, G.1    Blackshear, P.J.2
  • 35
    • 0029831440 scopus 로고    scopus 로고
    • Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine- rich protein kinase C substrate protein in intact cells
    • DOI 10.1074/jbc.271.38.23424
    • Swierczynski S. L. Blackshear P. J. (1996) Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells. J. Biol. Chem. 271, 23424 23430. (Pubitemid 26314791)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.38 , pp. 23424-23430
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 37
    • 0032528631 scopus 로고    scopus 로고
    • 2+ channel subtypes on rat spinal motor neurons, interneurons, and nerve terminals
    • 2+ channel subtypes on rat spinal motor neurons, interneurons, and nerve terminals. J. Neurosci. 18, 6319 6330. (Pubitemid 28373237)
    • (1998) Journal of Neuroscience , vol.18 , Issue.16 , pp. 6319-6330
    • Westenbroek, R.E.1    Hoskins, L.2    Catterall, W.A.3
  • 38
    • 34250857340 scopus 로고    scopus 로고
    • Regulation of Membrane Fusion in Synaptic Excitation-Secretion Coupling: Speed and Accuracy Matter
    • DOI 10.1016/j.neuron.2007.06.013, PII S0896627307004400
    • Wojcik S. M. Brose N. (2007) Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter. Neuron 55, 11 24. (Pubitemid 46990816)
    • (2007) Neuron , vol.55 , Issue.1 , pp. 11-24
    • Wojcik, S.M.1    Brose, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.