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Volumn 11, Issue 7, 2010, Pages 958-971

S100A10-mediated translocation of annexin-A2 to SNARE proteins in adrenergic chromaffin cells undergoing exocytosis

Author keywords

Annexin A2; Chromaffin cells; Exocytosis; PIP2 clusters; S100A10; SNARE proteins; VAMP2

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM BINDING PROTEIN S100A10; LIPOCORTIN 2; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; SNARE PROTEIN; SYNAPTOBREVIN 2; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TETANUS TOXIN; UNCLASSIFIED DRUG;

EID: 77954711973     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2010.01065.x     Document Type: Article
Times cited : (54)

References (76)
  • 1
    • 0028324464 scopus 로고
    • Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P, Pollard HB. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim Biophys Acta 1994, 1197:63-93.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 2
    • 0031055568 scopus 로고    scopus 로고
    • Distinct annexin subfamilies in plants and protists diverged prior to animal annexins and from a common ancestor
    • Morgan RO, Pilar Fernandez M. Distinct annexin subfamilies in plants and protists diverged prior to animal annexins and from a common ancestor. J Mol Evol 1997, 44:178-188.
    • (1997) J Mol Evol , vol.44 , pp. 178-188
    • Morgan, R.O.1    Pilar Fernandez, M.2
  • 3
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: from structure to function
    • Gerke V, Moss SE. Annexins: from structure to function. Physiol Rev 2002, 82:331-371.
    • (2002) Physiol Rev , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 5
    • 20344369564 scopus 로고    scopus 로고
    • Annexins: linking Ca2+ signalling to membrane dynamics
    • Gerke V, Creutz CE, Moss SE. Annexins: linking Ca2+ signalling to membrane dynamics. Nat Rev Mol Cell Biol 2005, 6:449-461.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 449-461
    • Gerke, V.1    Creutz, C.E.2    Moss, S.E.3
  • 6
    • 0025117429 scopus 로고
    • Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry
    • Nakata T, Sobue K, Hirokawa N. Conformational change and localization of calpactin I complex involved in exocytosis as revealed by quick-freeze, deep-etch electron microscopy and immunocytochemistry. J Cell Biol 1990, 110:13-25.
    • (1990) J Cell Biol , vol.110 , pp. 13-25
    • Nakata, T.1    Sobue, K.2    Hirokawa, N.3
  • 7
    • 0028365214 scopus 로고
    • Quick-freeze, deep-etch visualization of exocytosis in anterior pituitary secretory cells: localization and possible roles of actin and annexin II
    • Senda T, Okabe T, Matsuda M, Fujita H. Quick-freeze, deep-etch visualization of exocytosis in anterior pituitary secretory cells: localization and possible roles of actin and annexin II. Cell Tissue Res 1994, 277:51-60.
    • (1994) Cell Tissue Res , vol.277 , pp. 51-60
    • Senda, T.1    Okabe, T.2    Matsuda, M.3    Fujita, H.4
  • 8
    • 0026063254 scopus 로고
    • The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C
    • Sarafian T, Pradel LA, Henry JP, Aunis D, Bader MF. The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C. J Cell Biol 1991, 114:1135-1147.
    • (1991) J Cell Biol , vol.114 , pp. 1135-1147
    • Sarafian, T.1    Pradel, L.A.2    Henry, J.P.3    Aunis, D.4    Bader, M.F.5
  • 9
    • 0024390672 scopus 로고
    • A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells
    • Ali SM, Geisow MJ, Burgoyne RD. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature 1989, 340:313-315.
    • (1989) Nature , vol.340 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 10
    • 14844328667 scopus 로고    scopus 로고
    • Annexin 2 promotes the formation of lipid microdomains required for calcium-regulated exocytosis of dense-core vesicles
    • Chasserot-Golaz S, Vitale N, Umbrecht-Jenck E, Knight D, Gerke V, Bader MF. Annexin 2 promotes the formation of lipid microdomains required for calcium-regulated exocytosis of dense-core vesicles. Mol Biol Cell 2005, 16:1108-1119.
    • (2005) Mol Biol Cell , vol.16 , pp. 1108-1119
    • Chasserot-Golaz, S.1    Vitale, N.2    Umbrecht-Jenck, E.3    Knight, D.4    Gerke, V.5    Bader, M.F.6
  • 12
  • 13
    • 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. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J 2001, 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
  • 14
    • 1542319211 scopus 로고    scopus 로고
    • Site of docking and fusion of insulin secretory granules in live MIN6 beta cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy
    • Ohara-Imaizumi M, Nishiwaki C, Kikuta T, Kumakura K, Nakamichi Y, Nagamatsu S. Site of docking and fusion of insulin secretory granules in live MIN6 beta cells analyzed by TAT-conjugated anti-syntaxin 1 antibody and total internal reflection fluorescence microscopy. J Biol Chem 2004, 279:8403-8408.
    • (2004) J Biol Chem , vol.279 , pp. 8403-8408
    • Ohara-Imaizumi, M.1    Nishiwaki, C.2    Kikuta, T.3    Kumakura, K.4    Nakamichi, Y.5    Nagamatsu, S.6
  • 15
    • 33646202286 scopus 로고    scopus 로고
    • The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane
    • Sieber JJ, Willig KI, Heintzmann R, Hell SW, Lang T. The SNARE motif is essential for the formation of syntaxin clusters in the plasma membrane. Biophys J 2006, 90:2843-2851.
    • (2006) Biophys J , vol.90 , pp. 2843-2851
    • Sieber, J.J.1    Willig, K.I.2    Heintzmann, R.3    Hell, S.W.4    Lang, T.5
  • 16
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: functions and pathology
    • Schafer BW, Heizmann CW. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem Sci 1996, 21:134-140.
    • (1996) Trends Biochem Sci , vol.21 , pp. 134-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 17
    • 0024062670 scopus 로고
    • P36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix
    • Johnsson N, Marriott G, Weber K. p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO J 1988, 7:2435-2442.
    • (1988) EMBO J , vol.7 , pp. 2435-2442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 20
    • 33846968447 scopus 로고    scopus 로고
    • P11 (S100A10)-an inducible adaptor protein that modulates neuronal functions
    • Svenningsson P, Greengard P. p11 (S100A10)-an inducible adaptor protein that modulates neuronal functions. Curr Opin Pharmacol 2007, 7:27-32.
    • (2007) Curr Opin Pharmacol , vol.7 , pp. 27-32
    • Svenningsson, P.1    Greengard, P.2
  • 21
    • 6344241866 scopus 로고    scopus 로고
    • An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface
    • Deora AB, Kreitzer G, Jacovina AT, Hajjar KA. An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface. J Biol Chem 2004, 279:43411-43418.
    • (2004) J Biol Chem , vol.279 , pp. 43411-43418
    • Deora, A.B.1    Kreitzer, G.2    Jacovina, A.T.3    Hajjar, K.A.4
  • 22
    • 0034995073 scopus 로고    scopus 로고
    • S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles
    • Donato R. S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int J Biochem Cell Biol 2001, 33:637-668.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 637-668
    • Donato, R.1
  • 23
    • 0030013509 scopus 로고    scopus 로고
    • Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells
    • Chasserot-Golaz S, Vitale N, Sagot I, Delouche B, Dirrig S, Pradel LA, Henry JP, Aunis D, Bader MF. Annexin II in exocytosis: catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells. J Cell Biol 1996, 133:1217-1236.
    • (1996) J Cell Biol , vol.133 , pp. 1217-1236
    • Chasserot-Golaz, S.1    Vitale, N.2    Sagot, I.3    Delouche, B.4    Dirrig, S.5    Pradel, L.A.6    Henry, J.P.7    Aunis, D.8    Bader, M.F.9
  • 24
    • 0030996010 scopus 로고    scopus 로고
    • Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner
    • Liu L, Tao JQ, Zimmerman UJ. Annexin II binds to the membrane of A549 cells in a calcium-dependent and calcium-independent manner. Cell Signal 1997, 9:299-304.
    • (1997) Cell Signal , vol.9 , pp. 299-304
    • Liu, L.1    Tao, J.Q.2    Zimmerman, U.J.3
  • 25
    • 0347753248 scopus 로고    scopus 로고
    • AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture
    • Benaud C, Gentil BJ, Assard N, Court M, Garin J, Delphin C, Baudier J. AHNAK interaction with the annexin 2/S100A10 complex regulates cell membrane cytoarchitecture. J Cell Biol 2004, 164:133-144.
    • (2004) J Cell Biol , vol.164 , pp. 133-144
    • Benaud, C.1    Gentil, B.J.2    Assard, N.3    Court, M.4    Garin, J.5    Delphin, C.6    Baudier, J.7
  • 26
    • 0023549924 scopus 로고
    • Morphology and secretory activity of digitonin- and alpha-toxin-permeabilized chromaffin cells
    • Grant NJ, Aunis D, Bader MF. Morphology and secretory activity of digitonin- and alpha-toxin-permeabilized chromaffin cells. Neuroscience 1987, 23:1143-1155.
    • (1987) Neuroscience , vol.23 , pp. 1143-1155
    • Grant, N.J.1    Aunis, D.2    Bader, M.F.3
  • 27
    • 0027409301 scopus 로고
    • Multiple calcium-dependent processes related to secretion in bovine chromaffin cells
    • Neher E, Zucker RS. Multiple calcium-dependent processes related to secretion in bovine chromaffin cells. Neuron 1993, 10:21-30.
    • (1993) Neuron , vol.10 , pp. 21-30
    • Neher, E.1    Zucker, R.S.2
  • 28
    • 33744782044 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the S100 protein family
    • Santamaria-Kisiel L, Rintala-Dempsey AC, Shaw GS. Calcium-dependent and -independent interactions of the S100 protein family. Biochem J 2006, 396:201-214.
    • (2006) Biochem J , vol.396 , pp. 201-214
    • Santamaria-Kisiel, L.1    Rintala-Dempsey, A.C.2    Shaw, G.S.3
  • 31
    • 0028861707 scopus 로고
    • Vesicle-associated membrane protein (VAMP)/synapto-brevin-2 is associated with dense core secretory granules in PC12 neuroendocrine cells
    • Papini E, Rossetto O, Cutler DF. Vesicle-associated membrane protein (VAMP)/synapto-brevin-2 is associated with dense core secretory granules in PC12 neuroendocrine cells. J Biol Chem 1995, 270:1332-1336.
    • (1995) J Biol Chem , vol.270 , pp. 1332-1336
    • Papini, E.1    Rossetto, O.2    Cutler, D.F.3
  • 32
    • 0022243842 scopus 로고
    • Immunohistochemical and biochemical study on the development of the noradrenaline- and adrenaline-storing cells of the adrenal medulla of the rat
    • Verhofstad AA, Coupland RE, Parker TR, Goldstein M. Immunohistochemical and biochemical study on the development of the noradrenaline- and adrenaline-storing cells of the adrenal medulla of the rat. Cell Tissue Res 1985, 242:233-243.
    • (1985) Cell Tissue Res , vol.242 , pp. 233-243
    • Verhofstad, A.A.1    Coupland, R.E.2    Parker, T.R.3    Goldstein, M.4
  • 34
    • 0028072443 scopus 로고
    • Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells
    • Hohne-Zell B, Ecker A, Weller U, Gratzl M. Synaptobrevin cleavage by the tetanus toxin light chain is linked to the inhibition of exocytosis in chromaffin cells. FEBS Lett 1994, 355:131-134.
    • (1994) FEBS Lett , vol.355 , pp. 131-134
    • Hohne-Zell, B.1    Ecker, A.2    Weller, U.3    Gratzl, M.4
  • 35
    • 0038180967 scopus 로고    scopus 로고
    • Observing cell surface signaling domains using electron microscopy
    • Prior IA, Parton RG, Hancock JF. Observing cell surface signaling domains using electron microscopy. Sci STKE 2003, 177:PL9.
    • (2003) Sci STKE , vol.177
    • Prior, I.A.1    Parton, R.G.2    Hancock, J.F.3
  • 36
    • 0034728966 scopus 로고    scopus 로고
    • Observing FcepsilonRI signaling from the inside of the mast cell membrane
    • Wilson BS, Pfeiffer JR, Oliver JM. Observing FcepsilonRI signaling from the inside of the mast cell membrane. J Cell Biol 2000, 149:1131-1142.
    • (2000) J Cell Biol , vol.149 , pp. 1131-1142
    • Wilson, B.S.1    Pfeiffer, J.R.2    Oliver, J.M.3
  • 37
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT
    • Wilson BS, Pfeiffer JR, Surviladze Z, Gaudet EA, Oliver JM. High resolution mapping of mast cell membranes reveals primary and secondary domains of Fc(epsilon)RI and LAT. J Cell Biol 2001, 154:645-658.
    • (2001) J Cell Biol , vol.154 , pp. 645-658
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 39
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol 2003, 160:165-170.
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 40
    • 0034464348 scopus 로고    scopus 로고
    • Statistical evaluation of colocalization patterns in immunogold labeling experiments
    • Philimonenko AA, Janacek J, Hozak P. Statistical evaluation of colocalization patterns in immunogold labeling experiments. J Struct Biol 2000, 132:201-210.
    • (2000) J Struct Biol , vol.132 , pp. 201-210
    • Philimonenko, A.A.1    Janacek, J.2    Hozak, P.3
  • 41
    • 0037445938 scopus 로고    scopus 로고
    • Imaging metabolism of phosphatidylinositol 4,5-bisphosphate in T-cell GM1-enriched domains containing Ras proteins
    • Parmryd I, Adler J, Patel R, Magee AI. Imaging metabolism of phosphatidylinositol 4,5-bisphosphate in T-cell GM1-enriched domains containing Ras proteins. Exp Cell Res 2003, 285:27-38.
    • (2003) Exp Cell Res , vol.285 , pp. 27-38
    • Parmryd, I.1    Adler, J.2    Patel, R.3    Magee, A.I.4
  • 42
    • 20444486130 scopus 로고    scopus 로고
    • The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters
    • Aoyagi K, Sugaya T, Umeda M, Yamamoto S, Terakawa S, Takahashi M. The activation of exocytotic sites by the formation of phosphatidylinositol 4,5-bisphosphate microdomains at syntaxin clusters. J Biol Chem 2005, 280:17346-17352.
    • (2005) J Biol Chem , vol.280 , pp. 17346-17352
    • Aoyagi, K.1    Sugaya, T.2    Umeda, M.3    Yamamoto, S.4    Terakawa, S.5    Takahashi, M.6
  • 43
    • 1842484428 scopus 로고    scopus 로고
    • Lipid rafts and the regulation of exocytosis
    • Salaun C, James DJ, Chamberlain LH. Lipid rafts and the regulation of exocytosis. Traffic 2004, 5:255-264.
    • (2004) Traffic , vol.5 , pp. 255-264
    • Salaun, C.1    James, D.J.2    Chamberlain, L.H.3
  • 44
    • 48249119533 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion
    • James DJ, Khodthong C, Kowalchyk JA, Martin TF. Phosphatidylinositol 4,5-bisphosphate regulates SNARE-dependent membrane fusion. J Cell Biol 2008, 182:355-366.
    • (2008) J Cell Biol , vol.182 , pp. 355-366
    • James, D.J.1    Khodthong, C.2    Kowalchyk, J.A.3    Martin, T.F.4
  • 45
    • 3242877433 scopus 로고    scopus 로고
    • Annexins-unique membrane binding proteins with diverse functions
    • Rescher U, Gerke V. Annexins-unique membrane binding proteins with diverse functions. J Cell Sci 2004, 117:2631-2639.
    • (2004) J Cell Sci , vol.117 , pp. 2631-2639
    • Rescher, U.1    Gerke, V.2
  • 46
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis
    • Chamberlain LH, Burgoyne RD, Gould GW. SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc Natl Acad Sci U S A 2001, 98:5619-5624.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 47
    • 36349028713 scopus 로고    scopus 로고
    • S100A10/p11: family, friends and functions
    • Rescher U, Gerke V. S100A10/p11: family, friends and functions. Pflugers Arch 2008, 455:275-282.
    • (2008) Pflugers Arch , vol.455 , pp. 275-282
    • Rescher, U.1    Gerke, V.2
  • 48
  • 49
    • 0037009441 scopus 로고    scopus 로고
    • P11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1
    • Girard C, Tinel N, Terrenoire C, Romey G, Lazdunski M, Borsotto M. p11, an annexin II subunit, an auxiliary protein associated with the background K+ channel, TASK-1. EMBO J 2002, 21:4439-4448.
    • (2002) EMBO J , vol.21 , pp. 4439-4448
    • Girard, C.1    Tinel, N.2    Terrenoire, C.3    Romey, G.4    Lazdunski, M.5    Borsotto, M.6
  • 51
    • 0037456539 scopus 로고    scopus 로고
    • Two distinct mechanisms target membrane proteins to the axonal surface
    • Sampo B, Kaech S, Kunz S, Banker G. Two distinct mechanisms target membrane proteins to the axonal surface. Neuron 2003, 37:611-624.
    • (2003) Neuron , vol.37 , pp. 611-624
    • Sampo, B.1    Kaech, S.2    Kunz, S.3    Banker, G.4
  • 52
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites
    • Thiel C, Osborn M, Gerke V. The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J Cell Sci 1992, 103:733-742.
    • (1992) J Cell Sci , vol.103 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 53
    • 0030814032 scopus 로고    scopus 로고
    • P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2
    • Wu T, Angus CW, Yao XL, Logun C, Shelhamer JH. P11, a unique member of the S100 family of calcium-binding proteins, interacts with and inhibits the activity of the 85-kDa cytosolic phospholipase A2. J Biol Chem 1997, 272:17145-17153.
    • (1997) J Biol Chem , vol.272 , pp. 17145-17153
    • Wu, T.1    Angus, C.W.2    Yao, X.L.3    Logun, C.4    Shelhamer, J.H.5
  • 54
    • 1642317015 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2-p11 interaction controls arachidonic acid release as a function of epithelial cell confluence
    • Bailleux A, Wendum D, Audubert F, Jouniaux AM, Koumanov K, Trugnan G, Masliah J. Cytosolic phospholipase A2-p11 interaction controls arachidonic acid release as a function of epithelial cell confluence. Biochem J 2004, 378:307-315.
    • (2004) Biochem J , vol.378 , pp. 307-315
    • Bailleux, A.1    Wendum, D.2    Audubert, F.3    Jouniaux, A.M.4    Koumanov, K.5    Trugnan, G.6    Masliah, J.7
  • 57
    • 0037024545 scopus 로고    scopus 로고
    • Localization of phosphatidylinositol 4,5-P(2) important in exocytosis and a quantitative analysis of chromaffin granule motion adjacent to the plasma membrane
    • Holz RW, Axelrod D. Localization of phosphatidylinositol 4,5-P(2) important in exocytosis and a quantitative analysis of chromaffin granule motion adjacent to the plasma membrane. Ann N Y Acad Sci 2002, 971:232-243.
    • (2002) Ann N Y Acad Sci , vol.971 , pp. 232-243
    • Holz, R.W.1    Axelrod, D.2
  • 58
    • 14944339213 scopus 로고    scopus 로고
    • Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the releasable vesicle pool size in chromaffin cells
    • Milosevic I, Sorensen JB, Lang T, Krauss M, Nagy G, Haucke V, Jahn R, Neher E. Plasmalemmal phosphatidylinositol-4,5-bisphosphate level regulates the releasable vesicle pool size in chromaffin cells. J Neurosci 2005, 25:2557-2565.
    • (2005) J Neurosci , vol.25 , pp. 2557-2565
    • Milosevic, I.1    Sorensen, J.B.2    Lang, T.3    Krauss, M.4    Nagy, G.5    Haucke, V.6    Jahn, R.7    Neher, E.8
  • 60
    • 3242887228 scopus 로고    scopus 로고
    • Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes
    • Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V. Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes. J Cell Sci 2004, 117:3473-3480.
    • (2004) J Cell Sci , vol.117 , pp. 3473-3480
    • Rescher, U.1    Ruhe, D.2    Ludwig, C.3    Zobiack, N.4    Gerke, V.5
  • 61
    • 4544231736 scopus 로고    scopus 로고
    • The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy
    • Menke M, Ross M, Gerke V, Steinem C. The molecular arrangement of membrane-bound annexin A2-S100A10 tetramer as revealed by scanning force microscopy. Chembiochem 2004, 5:1003-1006.
    • (2004) Chembiochem , vol.5 , pp. 1003-1006
    • Menke, M.1    Ross, M.2    Gerke, V.3    Steinem, C.4
  • 63
    • 30044431601 scopus 로고    scopus 로고
    • Phosphoinositide specificity of and mechanism of lipid domain formation by annexin A2-p11 heterotetramer.
    • Gokhale NA, Abraham A, Digman MA, Gratton E, Cho W. Phosphoinositide specificity of and mechanism of lipid domain formation by annexin A2-p11 heterotetramer. J Biol Chem 2005, 280:42831-42840.
    • (2005) J Biol Chem , vol.280 , pp. 42831-42840
    • Gokhale, N.A.1    Abraham, A.2    Digman, M.A.3    Gratton, E.4    Cho, W.5
  • 64
    • 33845406931 scopus 로고    scopus 로고
    • Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2
    • Rintala-Dempsey AC, Santamaria-Kisiel L, Liao Y, Lajoie G, Shaw GS. Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2. Biochemistry 2006, 45:14695-14705.
    • (2006) Biochemistry , vol.45 , pp. 14695-14705
    • Rintala-Dempsey, A.C.1    Santamaria-Kisiel, L.2    Liao, Y.3    Lajoie, G.4    Shaw, G.S.5
  • 65
    • 0027471403 scopus 로고
    • The gene encoding the calcium binding protein calcyclin is expressed at sites of exocytosis in the mouse
    • Timmons PM, Chan CT, Rigby PW, Poirier F. The gene encoding the calcium binding protein calcyclin is expressed at sites of exocytosis in the mouse. J Cell Sci 1993, 104:187-196.
    • (1993) J Cell Sci , vol.104 , pp. 187-196
    • Timmons, P.M.1    Chan, C.T.2    Rigby, P.W.3    Poirier, F.4
  • 66
    • 2342531157 scopus 로고    scopus 로고
    • Metastasis-associated S100A4 (Mts1) protein is expressed in subpopulations of sensory and autonomic neurons and in Schwann cells of the adult rat
    • Sandelin M, Zabihi S, Liu L, Wicher G, Kozlova EN. Metastasis-associated S100A4 (Mts1) protein is expressed in subpopulations of sensory and autonomic neurons and in Schwann cells of the adult rat. J Comp Neurol 2004, 473:233-243.
    • (2004) J Comp Neurol , vol.473 , pp. 233-243
    • Sandelin, M.1    Zabihi, S.2    Liu, L.3    Wicher, G.4    Kozlova, E.N.5
  • 67
    • 0027089642 scopus 로고
    • Noradrenergic, but not adrenergic chromaffin cells in the adrenal gland express neuromodulin (GAP-43)
    • Grant NJ, Konig F, Deloulme JC, Aunis D, Langley K. Noradrenergic, but not adrenergic chromaffin cells in the adrenal gland express neuromodulin (GAP-43). Eur J Neurosci 1992, 4:1257-1263.
    • (1992) Eur J Neurosci , vol.4 , pp. 1257-1263
    • Grant, N.J.1    Konig, F.2    Deloulme, J.C.3    Aunis, D.4    Langley, K.5
  • 68
    • 0025687548 scopus 로고
    • Changes in PC12 cell morphology induced by transfection with 42C cDNA, coding for a member of the S-100 protein family
    • Masiakowski P, Shooter EM. Changes in PC12 cell morphology induced by transfection with 42C cDNA, coding for a member of the S-100 protein family. J Neurosci Res 1990, 27:264-269.
    • (1990) J Neurosci Res , vol.27 , pp. 264-269
    • Masiakowski, P.1    Shooter, E.M.2
  • 69
    • 0020024227 scopus 로고
    • Calcium-dependent regulation of chromaffin granule movement, membrane contact, and fusion during exocytosis
    • Pollard HB, Creutz CE, Fowler V, Scott J, Pazoles CJ. Calcium-dependent regulation of chromaffin granule movement, membrane contact, and fusion during exocytosis. Cold Spring Harb Symp Quant Biol 1982, 46:819-834.
    • (1982) Cold Spring Harb Symp Quant Biol , vol.46 , pp. 819-834
    • Pollard, H.B.1    Creutz, C.E.2    Fowler, V.3    Scott, J.4    Pazoles, C.J.5
  • 70
    • 0021847682 scopus 로고
    • Reorganization of alpha-fodrin induced by stimulation in secretory cells
    • Perrin D, Aunis D. Reorganization of alpha-fodrin induced by stimulation in secretory cells. Nature 1985, 315:589-592.
    • (1985) Nature , vol.315 , pp. 589-592
    • Perrin, D.1    Aunis, D.2
  • 71
    • 0019847651 scopus 로고
    • Immunocytochemical study of microtubules in chromaffin cells in culture and evidence that tubulin is not an integral protein of the chromaffin granule membrane
    • Bader M-F, Ciesielski-Treska J, Thierse D, Hesketh JE, Aunis D. Immunocytochemical study of microtubules in chromaffin cells in culture and evidence that tubulin is not an integral protein of the chromaffin granule membrane. J. Neurochem. 1981, 37:917-933.
    • (1981) J. Neurochem. , vol.37 , pp. 917-933
    • Bader, M.-.F.1    Ciesielski-Treska, J.2    Thierse, D.3    Hesketh, J.E.4    Aunis, D.5
  • 72
    • 0022979266 scopus 로고
    • Characterization of hormone and protein release from alpha-toxin-permeabilized chromaffin cells in primary culture
    • Bader M-F, Thierse D, Aunis D, Ahnert-Hilger G, Gratzl M. Characterization of hormone and protein release from alpha-toxin-permeabilized chromaffin cells in primary culture. J.Biol. Chem 1986, 261:5777-5783.
    • (1986) J.Biol. Chem , vol.261 , pp. 5777-5783
    • Bader, M.-.F.1    Thierse, D.2    Aunis, D.3    Ahnert-Hilger, G.4    Gratzl, M.5
  • 73
    • 0034642174 scopus 로고    scopus 로고
    • N-terminal domain of annexin 2 regulates Ca(2+)-dependent membrane aggregation by the core domain: a site directed mutagenesis study
    • Ayala-Sanmartin J, Gouache P, Henry JP. N-terminal domain of annexin 2 regulates Ca(2+)-dependent membrane aggregation by the core domain: a site directed mutagenesis study. Biochemistry 2000, 39:15190-15198.
    • (2000) Biochemistry , vol.39 , pp. 15190-15198
    • Ayala-Sanmartin, J.1    Gouache, P.2    Henry, J.P.3
  • 74
    • 0034662499 scopus 로고    scopus 로고
    • Ca2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin
    • Quetglas S, Leveque C, Miquelis R, Sato K, Seagar M. Ca2+-dependent regulation of synaptic SNARE complex assembly via a calmodulin- and phospholipid-binding domain of synaptobrevin. Proc Natl Acad Sci U S A 2000, 97:9695-9700.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 9695-9700
    • Quetglas, S.1    Leveque, C.2    Miquelis, R.3    Sato, K.4    Seagar, M.5
  • 76
    • 27744484465 scopus 로고    scopus 로고
    • Characterizing the topography of membrane receptors and signaling molecules from spatial patterns obtained using nanometer-scale electron-dense probes and electron microscopy
    • Zhang J, Leiderman K, Pfeiffer JR, Wilson BS, Oliver JM, Steinberg SL. Characterizing the topography of membrane receptors and signaling molecules from spatial patterns obtained using nanometer-scale electron-dense probes and electron microscopy. Micron 2006, 37:14-34.
    • (2006) Micron , vol.37 , pp. 14-34
    • Zhang, J.1    Leiderman, K.2    Pfeiffer, J.R.3    Wilson, B.S.4    Oliver, J.M.5    Steinberg, S.L.6


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