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Volumn 25, Issue 10, 2005, Pages 2557-2565

Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the releasable vesicle pool size in chromaffin cells

Author keywords

Chromaffin cell; Exocytosis; LY294002; Phosphatidylinositol 4 phosphate 5 kinase; Phosphatidylinositol 4,5 bisphospate; Plasmalemmal microdomains

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; CATECHOLAMINE; FLUORESCENT DYE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; SYNAPTOJANIN;

EID: 14944339213     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.3761-04.2005     Document Type: Article
Times cited : (194)

References (49)
  • 1
    • 0041475820 scopus 로고    scopus 로고
    • ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5) bisphosphate required for regulated exocytosis
    • Aikawa Y, Martin TFJ (2003) ARF6 regulates a plasma membrane pool of phosphatidylinositol(4,5)bisphosphate required for regulated exocytosis. J Cell Biol 162:647-659.
    • (2003) J Cell Biol , vol.162 , pp. 647-659
    • Aikawa, Y.1    Martin, T.F.J.2
  • 2
    • 2642555388 scopus 로고    scopus 로고
    • Dibasic amino acid residues at the carboxy-terminal end of kinase homology domain participate in the plasma membrane localization and function of phosphatidylinositol 5-kinase γ
    • Arioka M, Nakashima S, Shibasaki Y, Kitamoto K (2004) Dibasic amino acid residues at the carboxy-terminal end of kinase homology domain participate in the plasma membrane localization and function of phosphatidylinositol 5-kinase γ. Biochem Biophys Res Commun 319:456-463.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 456-463
    • Arioka, M.1    Nakashima, S.2    Shibasaki, Y.3    Kitamoto, K.4
  • 3
    • 0032849774 scopus 로고    scopus 로고
    • An efficient method for infection of adrenal chromaffin cells using the Semliki Forest virus gene expression system
    • Ashery U, Betz A, Xu T, Brose N, Rettig J (1999) An efficient method for infection of adrenal chromaffin cells using the Semliki Forest virus gene expression system. Eur J Cell Biol 78:525-532.
    • (1999) Eur J Cell Biol , vol.78 , pp. 525-532
    • Ashery, U.1    Betz, A.2    Xu, T.3    Brose, N.4    Rettig, J.5
  • 5
    • 0344653108 scopus 로고    scopus 로고
    • Activation of phospholipase Cγ by phosphatidylinositol 3,4,5-trisphosphate
    • Bae YS, Cantley LG, Chen CS, Kim SR, Kwon KS, Rhee SG (1998) Activation of phospholipase Cγ by phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 273:4465-4469.
    • (1998) J Biol Chem , vol.273 , pp. 4465-4469
    • Bae, Y.S.1    Cantley, L.G.2    Chen, C.S.3    Kim, S.R.4    Kwon, K.S.5    Rhee, S.G.6
  • 6
    • 0842291506 scopus 로고    scopus 로고
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • 2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat Struct Mol Biol 11:36-44.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 8
    • 0035881755 scopus 로고    scopus 로고
    • New EMBO members' review: Actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts
    • Caroni P (2001) New EMBO members' review: actin cytoskeleton regulation through modulation of PI(4,5)P(2) rafts. EMBO J 20:4332-4336.
    • (2001) EMBO J , vol.20 , pp. 4332-4336
    • Caroni, P.1
  • 9
    • 0031778357 scopus 로고    scopus 로고
    • Possible involvement of phosphatidylinositol 3-kinase in regulated exocytosis: Studies in chromaffin cells with inhibitor LY294002
    • Chasserot-Golaz S, Hubert P, Thierse D, Dirrig S, Vlahos CJ, Aunis D, Bader M-F (1998) Possible involvement of phosphatidylinositol 3-kinase in regulated exocytosis: studies in chromaffin cells with inhibitor LY294002. J Neurochem 70:2347-2355.
    • (1998) J Neurochem , vol.70 , pp. 2347-2355
    • Chasserot-Golaz, S.1    Hubert, P.2    Thierse, D.3    Dirrig, S.4    Vlahos, C.J.5    Aunis, D.6    Bader, M.-F.7
  • 11
    • 0042490720 scopus 로고    scopus 로고
    • Synapsin I-associated phosphatidylinositol 3-kinase mediates synaptic vesicle delivery to the readily releasable pool
    • Cousin MA, Malladi CS, Tan TC, Raymond CR, Smillie KJ, Robinson PJ (2003) Synapsin I-associated phosphatidylinositol 3-kinase mediates synaptic vesicle delivery to the readily releasable pool. J Biol Chem 278:29065-29071.
    • (2003) J Biol Chem , vol.278 , pp. 29065-29071
    • Cousin, M.A.1    Malladi, C.S.2    Tan, T.C.3    Raymond, C.R.4    Smillie, K.J.5    Robinson, P.J.6
  • 12
    • 0035074215 scopus 로고    scopus 로고
    • Phosphoinositides in membrane traffic at the synapse. Phosphoinositides in membrane traffic at the synapse
    • Cremona O, De Camilli P (2001). Phosphoinositides in membrane traffic at the synapse. Phosphoinositides in membrane traffic at the synapse. J Cell Sci 1041-1052.
    • (2001) J Cell Sci , pp. 1041-1052
    • Cremona, O.1    De Camilli, P.2
  • 13
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351:95-105.
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 14
    • 0029876888 scopus 로고    scopus 로고
    • Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases
    • Downing GJ, Kim S, Nakanishi S, Catt KJ, Balla T (1996) Characterization of a soluble adrenal phosphatidylinositol 4-kinase reveals wortmannin sensitivity of type III phosphatidylinositol kinases. Biochemistry 35:3587-3594.
    • (1996) Biochemistry , vol.35 , pp. 3587-3594
    • Downing, G.J.1    Kim, S.2    Nakanishi, S.3    Catt, K.J.4    Balla, T.5
  • 15
    • 0025330471 scopus 로고
    • Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP
    • Eberhard DA, Cooper CL, Low MG, Holz RW (1990) Evidence that the inositol phospholipids are necessary for exocytosis. Loss of inositol phospholipids and inhibition of secretion in permeabilized cells caused by a bacterial phospholipase C and removal of ATP. Biochem J 268:15-25.
    • (1990) Biochem J , vol.268 , pp. 15-25
    • Eberhard, D.A.1    Cooper, C.L.2    Low, M.G.3    Holz, R.W.4
  • 16
    • 0027765507 scopus 로고
    • Phosphatidylinositol transfer protein required for ATP-dependent priming of calcium activated secretion
    • Hay JC, Martin TF (1993) Phosphatidylinositol transfer protein required for ATP-dependent priming of calcium activated secretion. Nature 366:572-575.
    • (1993) Nature , vol.366 , pp. 572-575
    • Hay, J.C.1    Martin, T.F.2
  • 18
    • 0024603065 scopus 로고
    • MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis
    • Holz RW, Bittner MA, Peppers SC, Senter RA, Eberhard DA (1989) MgATP-independent and MgATP-dependent exocytosis. Evidence that MgATP primes adrenal chromaffin cells to undergo exocytosis. J Biol Chem 264:5412-5419.
    • (1989) J Biol Chem , vol.264 , pp. 5412-5419
    • Holz, R.W.1    Bittner, M.A.2    Peppers, S.C.3    Senter, R.A.4    Eberhard, D.A.5
  • 19
    • 0034625410 scopus 로고    scopus 로고
    • A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis
    • Holz RW, Hlubek MD, Sorensen SD, Fisher SK, Balla T, Ozaki S, Prestwich GD, Stuenkel EL, Bittner MA (2000) A pleckstrin homology domain specific for phosphatidylinositol 4,5-bisphosphate (PtdIns-4,5-P2) and fused to green fluorescent protein identifies plasma membrane PtdIns-4,5-P2 as being important in exocytosis. J Biol Chem 275:17878-17885.
    • (2000) J Biol Chem , vol.275 , pp. 17878-17885
    • Holz, R.W.1    Hlubek, M.D.2    Sorensen, S.D.3    Fisher, S.K.4    Balla, T.5    Ozaki, S.6    Prestwich, G.D.7    Stuenkel, E.L.8    Bittner, M.A.9
  • 21
    • 0032860589 scopus 로고    scopus 로고
    • Inhibition of quantal release from motor nerve by wortmannin
    • Hong SJ, Chang CC (1999) Inhibition of quantal release from motor nerve by wortmannin. Br J Pharmacol 128:142-148.
    • (1999) Br J Pharmacol , vol.128 , pp. 142-148
    • Hong, S.J.1    Chang, C.C.2
  • 22
    • 0038825177 scopus 로고    scopus 로고
    • ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ
    • Krauss M, Kinua M, Wenk MR, De Camilli P, Takei K, Haucke V (2003) ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ. J Cell Biol 162:113-124.
    • (2003) J Cell Biol , vol.162 , pp. 113-124
    • Krauss, M.1    Kinua, M.2    Wenk, M.R.3    De Camilli, P.4    Takei, K.5    Haucke, V.6
  • 24
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • 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.
    • (2001) EMBO J , vol.20 , pp. 2202-2213
    • Lang, T.1    Bruns, D.2    Wenzel, D.3    Riedel, D.4    Holroyd, P.5    Thiele, C.6    Jahn, R.7
  • 25
    • 0037135984 scopus 로고    scopus 로고
    • SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs
    • Lang T, Margittai M, Holzler H, Jahn R (2002) SNAREs in native plasma membranes are active and readily form core complexes with endogenous and exogenous SNAREs. J Cell Biol 158:751-760.
    • (2002) J Cell Biol , vol.158 , pp. 751-760
    • Lang, T.1    Margittai, M.2    Holzler, H.3    Jahn, R.4
  • 26
    • 0034717707 scopus 로고    scopus 로고
    • GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism
    • Laux T, Fukami K, Thelen M, Golub T, Frey D, Caroni P (2000) GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. J Cell Biol 149:1455-1472.
    • (2000) J Cell Biol , vol.149 , pp. 1455-1472
    • Laux, T.1    Fukami, K.2    Thelen, M.3    Golub, T.4    Frey, D.5    Caroni, P.6
  • 27
    • 0032478796 scopus 로고    scopus 로고
    • Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis
    • Loyet KM, Kowalchyk JA, Chaudhary A, Chen J, Prestwich GD, Martin TF (1998) Specific binding of phosphatidylinositol 4,5-bisphosphate to calcium-dependent activator protein for secretion (CAPS), a potential phosphoinositide effector protein for regulated exocytosis. J Biol Chem 273:8337-8343.
    • (1998) J Biol Chem , vol.273 , pp. 8337-8343
    • Loyet, K.M.1    Kowalchyk, J.A.2    Chaudhary, A.3    Chen, J.4    Prestwich, G.D.5    Martin, T.F.6
  • 28
    • 0035424240 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulation of surface membrane traffic
    • Martin TF (2001) PI(4,5)P(2) regulation of surface membrane traffic. Curr Opin Cell Biol 13:493-499.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 493-499
    • Martin, T.F.1
  • 30
    • 0036848611 scopus 로고    scopus 로고
    • Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment
    • Nagy G, Matti U, Nehring RB, Binz T, Rettig J, Neher E, Sorensen JB (2002) Protein kinase C-dependent phosphorylation of synaptosome-associated protein of 25 kDa at Ser187 potentiates vesicle recruitment. J Neurosci 22:9278-9286.
    • (2002) J Neurosci , vol.22 , pp. 9278-9286
    • Nagy, G.1    Matti, U.2    Nehring, R.B.3    Binz, T.4    Rettig, J.5    Neher, E.6    Sorensen, J.B.7
  • 31
    • 1242306711 scopus 로고    scopus 로고
    • Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25
    • Nagy G, Reim K, Matti U, Brose N, Binz T, Rettig I, Neher E, Sorensen JB (2004) Regulation of releasable vesicle pool sizes by protein kinase A-dependent phosphorylation of SNAP-25. Neuron 41:417-429.
    • (2004) Neuron , vol.41 , pp. 417-429
    • Nagy, G.1    Reim, K.2    Matti, U.3    Brose, N.4    Binz, T.5    Rettig, I.6    Neher, E.7    Sorensen, J.B.8
  • 32
    • 0031465172 scopus 로고    scopus 로고
    • Mints, Munc18-interacting proteins in synaptic vesicle exocytosis
    • Okamoto M, Sudhof TC (1997) Mints, Munc18-interacting proteins in synaptic vesicle exocytosis. J Biol Chem 272:31459-31464.
    • (1997) J Biol Chem , vol.272 , pp. 31459-31464
    • Okamoto, M.1    Sudhof, T.C.2
  • 34
    • 0037174660 scopus 로고    scopus 로고
    • Emerging roles of presynaptic proteins in calcium triggered exocytosis
    • Rettig J, Neher E (2002) Emerging roles of presynaptic proteins in calcium triggered exocytosis. Science 298:781-785.
    • (2002) Science , vol.298 , pp. 781-785
    • Rettig, J.1    Neher, E.2
  • 35
    • 0037115043 scopus 로고    scopus 로고
    • Effects of 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one on synaptic vesicle cycling at the frog neuromuscular junction
    • Rizzoli SO, Betz WJ (2002) Effects of 2-(4-morpholinyl)-8-phenyl-4H-1- benzopyran-4-one on synaptic vesicle cycling at the frog neuromuscular junction. J Neurosci 22:10680-10689.
    • (2002) J Neurosci , vol.22 , pp. 10680-10689
    • Rizzoli, S.O.1    Betz, W.J.2
  • 36
    • 0037157830 scopus 로고    scopus 로고
    • A phosphatidylinositol (4,5)-bisphosphate binding site within μ2-adaptin regulates clathrin-mediated endocytosis
    • Rohde G, Wenzel D, Haucke V (2002) A phosphatidylinositol (4,5)-bisphosphate binding site within μ2-adaptin regulates clathrin-mediated endocytosis. J Cell Biol 158:209-214.
    • (2002) J Cell Biol , vol.158 , pp. 209-214
    • Rohde, G.1    Wenzel, D.2    Haucke, V.3
  • 37
    • 0029825831 scopus 로고    scopus 로고
    • Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin
    • Schiavo G, Gu QM, Prestwich GD, Sollner TH, Rothman JE (1996) Calcium-dependent switching of the specificity of phosphoinositide binding to synaptotagmin. Proc Natl Acad Sci USA 93:13327-13332.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 13327-13332
    • Schiavo, G.1    Gu, Q.M.2    Prestwich, G.D.3    Sollner, T.H.4    Rothman, J.E.5
  • 39
    • 0031747119 scopus 로고    scopus 로고
    • A role for a wortmannin-sensitive phosphatidylinositol-4-kinase in the endocytosis of muscarinic cholinergic receptors
    • Sorensen SD, Linseman DA, McEwen EL, Heacock AM, Fisher SK (1998) A role for a wortmannin-sensitive phosphatidylinositol-4-kinase in the endocytosis of muscarinic cholinergic receptors. Mol Pharmacol 53:827-836.
    • (1998) Mol Pharmacol , vol.53 , pp. 827-836
    • Sorensen, S.D.1    Linseman, D.A.2    McEwen, E.L.3    Heacock, A.M.4    Fisher, S.K.5
  • 40
    • 0032510323 scopus 로고    scopus 로고
    • Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells
    • Stauffer TP, Ahn S, Meyer T (1998) Receptor-induced transient reduction in plasma membrane PtdIns(4,5)P2 concentration monitored in living cells. Curr Biol 8:343-346.
    • (1998) Curr Biol , vol.8 , pp. 343-346
    • Stauffer, T.P.1    Ahn, S.2    Meyer, T.3
  • 41
    • 0034659468 scopus 로고    scopus 로고
    • Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures
    • Tall EG, Spector I, Pentyala SN, Bitter I, Rebecchi MJ (2000) Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures. Curr Biol 10:743-746.
    • (2000) Curr Biol , vol.10 , pp. 743-746
    • Tall, E.G.1    Spector, I.2    Pentyala, S.N.3    Bitter, I.4    Rebecchi, M.J.5
  • 42
    • 0036736021 scopus 로고    scopus 로고
    • 2 hydrolysis inhibits cortical actin dynamics: Regulation at a global but not at a micrometer scale
    • 2 hydrolysis inhibits cortical actin dynamics: regulation at a global but not at a micrometer scale. Mol Biol Cell 13:3257-3267.
    • (2002) Mol Biol Cell , vol.13 , pp. 3257-3267
    • Van Rheenen, J.1    Jalink, K.2
  • 43
    • 0032547744 scopus 로고    scopus 로고
    • Visualization of phosphoinositides that bind pleckstrin homology domains: Calcium- and agonist-induced dynamic changes and relationship to myo-[3H] inositol-labeled phosphoinositide pools
    • Várnai P, Balla T (1998) Visualization of phosphoinositides that bind pleckstrin homology domains: calcium- and agonist-induced dynamic changes and relationship to myo-[3H] inositol-labeled phosphoinositide pools. J Cell Biol 143:501-510.
    • (1998) J Cell Biol , vol.143 , pp. 501-510
    • Várnai, P.1    Balla, T.2
  • 45
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos CJ, Matter WF, Hui KY, Brown RF (1994) A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J Biol Chem 269:5241-5248.
    • (1994) J Biol Chem , vol.269 , pp. 5241-5248
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 46
    • 0033622509 scopus 로고    scopus 로고
    • Dissection of three calcium-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices
    • Voets T (2000) Dissection of three calcium-dependent steps leading to secretion in chromaffin cells from mouse adrenal slices. Neuron 28:537-545.
    • (2000) Neuron , vol.28 , pp. 537-545
    • Voets, T.1
  • 47
    • 0035949679 scopus 로고    scopus 로고
    • Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I
    • Voets T, Moser T, Lund PE, Chow RH, Geppert M, Sudhof TC, Neher E (2001) Intracellular calcium dependence of large dense-core vesicle exocytosis in the absence of synaptotagmin I. Proc Natl Acad Sci USA 98:11680-11685.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11680-11685
    • Voets, T.1    Moser, T.2    Lund, P.E.3    Chow, R.H.4    Geppert, M.5    Sudhof, T.C.6    Neher, E.7
  • 49
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu T, Binz T, Niemann H, Neher E (1998) Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nat Neurosci 1:192-200.
    • (1998) Nat Neurosci , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4


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