메뉴 건너뛰기




Volumn 24, Issue 8, 1997, Pages 611-618

Protein phosphorylation events in exocytosis and endocytosis

Author keywords

Cell biology; Endocytosis; G proteins; Mechanisms; Neurotransmission; Receptors

Indexed keywords

CLATHRIN; DYNAMIN; MEMBRANE PROTEIN; SYNAPSIN; SYNAPSIN I; SYNAPTOBREVIN;

EID: 0030797977     PISSN: 03051870     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1440-1681.1997.tb02101.x     Document Type: Conference Paper
Times cited : (24)

References (76)
  • 2
    • 0025309605 scopus 로고
    • Pathways to regulated exocytosis in neurons
    • De Camilli P, Jahn R. Pathways to regulated exocytosis in neurons. Annu. Rev. Physiol. 1990; 52: 625-15.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 625-715
    • De Camilli, P.1    Jahn, R.2
  • 3
    • 0027354448 scopus 로고
    • Storage and release of neurotransmitters
    • Kelly RB. Storage and release of neurotransmitters. Cell 1993; 72 (Suppl.): 43-53.
    • (1993) Cell , vol.72 , Issue.SUPPL. , pp. 43-53
    • Kelly, R.B.1
  • 4
    • 0028211773 scopus 로고
    • The coated pit and macropinocytic pathways serve distinct endosome populations
    • Hewlett LJ, Prescott AR, Watts C. The coated pit and macropinocytic pathways serve distinct endosome populations. J. Cell Biol. 1994; 124: 689-703.
    • (1994) J. Cell Biol. , vol.124 , pp. 689-703
    • Hewlett, L.J.1    Prescott, A.R.2    Watts, C.3
  • 5
    • 0029809310 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fission of caveolae directly from plasma membranes
    • Schnitzer JE, Oh P, McIntosh DP. Role of GTP hydrolysis in fission of caveolae directly from plasma membranes. Science 1996; 274: 239-42.
    • (1996) Science , vol.274 , pp. 239-242
    • Schnitzer, J.E.1    Oh, P.2    McIntosh, D.P.3
  • 6
    • 0027333415 scopus 로고
    • Signal-dependent membrane protein trafficking in the endocytic pathway
    • Trowbridge IS, Collawn JF, Hopkins CR. Signal-dependent membrane protein trafficking in the endocytic pathway. Annu. Rev. Cell Biol. 1993; 9: 129-61.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 129-161
    • Trowbridge, I.S.1    Collawn, J.F.2    Hopkins, C.R.3
  • 7
    • 0029752791 scopus 로고    scopus 로고
    • Endocytosis and molecular sorting
    • Mellman I. Endocytosis and molecular sorting. Annu. Rev. Cell Biol. 1996; 12: 575-625.
    • (1996) Annu. Rev. Cell Biol. , vol.12 , pp. 575-625
    • Mellman, I.1
  • 8
    • 0029889579 scopus 로고    scopus 로고
    • Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif
    • Sorkin A, Mazzotti M, Sorkina T, Scotto L, Beguinot L. Epidermal growth factor receptor interaction with clathrin adaptors is mediated by the Tyr974-containing internalization motif. J. Biol. Chem. 1996; 271: 13377-84.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13377-13384
    • Sorkin, A.1    Mazzotti, M.2    Sorkina, T.3    Scotto, L.4    Beguinot, L.5
  • 9
    • 0028808230 scopus 로고
    • Role of auxilin in uncoating clathrin-coated vesicles
    • Ungewickell E, Ungewickell H, Holstein SE et al. Role of auxilin in uncoating clathrin-coated vesicles. Nature 1995; 378: 632-5.
    • (1995) Nature , vol.378 , pp. 632-635
    • Ungewickell, E.1    Ungewickell, H.2    Holstein, S.E.3
  • 10
    • 0027448777 scopus 로고
    • Clathrin: Its roles in receptor-mediated vesicular transport and specialised functions in neurons
    • Pley U, Parham P, Clathrin: Its roles in receptor-mediated vesicular transport and specialised functions in neurons. Crit. Rev. Biochem. Mol. Biol. 1993; 28: 431-64.
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 431-464
    • Pley, U.1    Parham, P.2
  • 11
    • 0028216869 scopus 로고
    • Synaptic vesicles and exocytosis
    • Jahn R, Sudhof TC. Synaptic vesicles and exocytosis. Annu. Rev. Neurosci. 1994; 17: 219-46.
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 219-246
    • Jahn, R.1    Sudhof, T.C.2
  • 13
    • 0029381831 scopus 로고
    • Synaptic transmission. Kinetics of synaptic vesicle recycling
    • Betz WJ, Wu LG. Synaptic transmission. Kinetics of synaptic vesicle recycling. Curr. Biol. 1995; 5: 1098-101.
    • (1995) Curr. Biol. , vol.5 , pp. 1098-1101
    • Betz, W.J.1    Wu, L.G.2
  • 14
    • 0029985418 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle endocytosis and recycling
    • DeCamilli P, Takei K. Molecular mechanisms in synaptic vesicle endocytosis and recycling. Neuron 1996; 16: 481-6.
    • (1996) Neuron , vol.16 , pp. 481-486
    • DeCamilli, P.1    Takei, K.2
  • 15
    • 0029894198 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin
    • Takei K, Mundigl O, Daniell L, De Camilli P. The synaptic vesicle cycle: A single vesicle budding step involving clathrin and dynamin. J. Cell Biol. 1996; 133: 1237-50.
    • (1996) J. Cell Biol. , vol.133 , pp. 1237-1250
    • Takei, K.1    Mundigl, O.2    Daniell, L.3    De Camilli, P.4
  • 16
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman JE. Mechanisms of intracellular protein transport. Nature 1994; 372: 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 17
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Sudhof TC. The synaptic vesicle cycle: A cascade of protein-protein interactions. Nature 1995; 375: 645-53.
    • (1995) Nature , vol.375 , pp. 645-653
    • Sudhof, T.C.1
  • 18
    • 0027402975 scopus 로고
    • Synaptic vesicle phosphoproteins and regulation of synaptic function
    • Greengard P, Valtorta F, Czernik AJ, Benfenati F. Synaptic vesicle phosphoproteins and regulation of synaptic function. Science 1993; 259: 780-5.
    • (1993) Science , vol.259 , pp. 780-785
    • Greengard, P.1    Valtorta, F.2    Czernik, A.J.3    Benfenati, F.4
  • 19
    • 0029059605 scopus 로고
    • Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice
    • Li L, Chin, LS, Shupliakov O et al. Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. Proc. Natl Acad. Sci. USA 1995; 92: 9235-9.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9235-9239
    • Li, L.1    Chin, L.S.2    Shupliakov, O.3
  • 21
    • 0029558545 scopus 로고
    • Synapsin I deficiency results in the structural change in the presynaptic terminals in the murine nervous system
    • Takei Y, Harada A, Takeda S et al. Synapsin I deficiency results in the structural change in the presynaptic terminals in the murine nervous system. J. Cell Biol. 1995; 131: 1789-800.
    • (1995) J. Cell Biol. , vol.131 , pp. 1789-1800
    • Takei, Y.1    Harada, A.2    Takeda, S.3
  • 22
    • 0029024135 scopus 로고
    • Essential functions of synapsins I and II in synaptic vesicle regulation
    • Rosahl TW, Spillane D, Missler M et al. Essential functions of synapsins I and II in synaptic vesicle regulation. Nature 1995; 375: 488-93.
    • (1995) Nature , vol.375 , pp. 488-493
    • Rosahl, T.W.1    Spillane, D.2    Missler, M.3
  • 24
    • 0028921368 scopus 로고
    • 2+/calmodulin- and cAMP-dependent protein kinases in vitro
    • 2+/calmodulin- and cAMP-dependent protein kinases in vitro. J. Neurosci. 1995; 15: 2385-95.
    • (1995) J. Neurosci. , vol.15 , pp. 2385-2395
    • Fykse, E.M.1    Li, C.2    Sudhof, T.C.3
  • 25
    • 0029935431 scopus 로고    scopus 로고
    • Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras
    • Stahl B, Chou JH, Li C, Sudhof TC, Jahn R. Rab3 reversibly recruits rabphilin to synaptic vesicles by a mechanism analogous to raf recruitment by ras. EMBO J. 1996; 15: 1799-809.
    • (1996) EMBO J. , vol.15 , pp. 1799-1809
    • Stahl, B.1    Chou, J.H.2    Li, C.3    Sudhof, T.C.4    Jahn, R.5
  • 26
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18 000 Da present in small synaptic vesicles of rat brain
    • Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R. Synaptobrevin: An integral membrane protein of 18 000 Da present in small synaptic vesicles of rat brain. EMBO J. 1989; 8: 379-84.
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 27
    • 0024308501 scopus 로고
    • Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system
    • Elferink LA, Trimble WS, Scheller RH. Two vesicle-associated membrane protein genes are differentially expressed in the rat central nervous system. J. Biol. Chem. 1989; 264: 11 061-4.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11061-11064
    • Elferink, L.A.1    Trimble, W.S.2    Scheller, R.H.3
  • 28
    • 0025007115 scopus 로고
    • Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2
    • Archer BTD, Ozcelik T, Jahn R, Francke U, Sudhof TC. Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2. J. Biol. Chem. 1990; 265: 17267-73.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17267-17273
    • Archer, B.T.D.1    Ozcelik, T.2    Jahn, R.3    Francke, U.4    Sudhof, T.C.5
  • 29
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon HT, Missler M, Li C, Sudhof TC. Complexins: Cytosolic proteins that regulate SNAP receptor function. Cell 1995; 83: 111-19.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Sudhof, T.C.4
  • 30
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann L, Hanson PI, Chapman ER, Jahn R. Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine. EMBO J. 1995; 14: 224-31.
    • (1995) EMBO J. , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 31
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett MK, Calakos N, Scheller RH. Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 1992; 257: 255-9.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 32
    • 0028587383 scopus 로고
    • Two components of transmitter release at a central synapse
    • Goda Y, Stevens CF. Two components of transmitter release at a central synapse. Proc. Natl Acad. Sci. USA 1994; 91: 12942-6.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12942-12946
    • Goda, Y.1    Stevens, C.F.2
  • 33
    • 0028973239 scopus 로고
    • 2+ sensors for the fast and slow components of neurotransmitter release
    • 2+ sensors for the fast and slow components of neurotransmitter release. J. Biol. Chem. 1995; 270: 24898-902.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24898-24902
    • Li, C.1    Davletov, B.A.2    Sudhof, T.C.3
  • 34
    • 0024816522 scopus 로고
    • The role of coated vesicles in recycling of synaptic vesicle membrane
    • Heuser J. The role of coated vesicles in recycling of synaptic vesicle membrane. Cell Biol. Int. Rep. 1989; 13: 1063-76.
    • (1989) Cell Biol. Int. Rep. , vol.13 , pp. 1063-1076
    • Heuser, J.1
  • 35
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson MS. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol 1994; 6: 538-44.
    • (1994) Curr. Opin. Cell Biol , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 36
    • 8544263568 scopus 로고    scopus 로고
    • Dynamic dynamin
    • Liu J-P. Dynamic dynamin. Today's Life Sci. 1996; 8: 23-6.
    • (1996) Today's Life Sci. , vol.8 , pp. 23-26
    • Liu, J.-P.1
  • 37
    • 0025006964 scopus 로고
    • Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins
    • Obar RA, Collins CA, Hammarback JA, Shpetner HS, Vallee RB. Molecular cloning of the microtubule-associated mechanochemical enzyme dynamin reveals homology with a new family of GTP-binding proteins. Nature 1990; 347: 256-61.
    • (1990) Nature , vol.347 , pp. 256-261
    • Obar, R.A.1    Collins, C.A.2    Hammarback, J.A.3    Shpetner, H.S.4    Vallee, R.B.5
  • 38
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K, McPherson PS, Schmid SL, De-Camilli P. Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 1995; 374: 186-90.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De-Camilli, P.4
  • 39
    • 0028986797 scopus 로고
    • The appendage domain of alpha-adaptin is a high affinity binding site for dynamin
    • Wang LH, Sudhof TC, Anderson RG. The appendage domain of alpha-adaptin is a high affinity binding site for dynamin. J. Biol. Chem. 1995; 270: 10079-83.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Sudhof, T.C.2    Anderson, R.G.3
  • 40
    • 0027315119 scopus 로고
    • In vitro fusion of endocytic vesicles is inhibited by cyclin A cdc2 kinase
    • Woodman PG, Adamczewski JP, Hunt T, Warren G. In vitro fusion of endocytic vesicles is inhibited by cyclin A cdc2 kinase. Mol. Biol. Cell 1993; 4: 541-53.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 541-553
    • Woodman, P.G.1    Adamczewski, J.P.2    Hunt, T.3    Warren, G.4
  • 41
    • 0030020444 scopus 로고    scopus 로고
    • Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells
    • Cox ME, Ely CM, Catling AD, Weber MJ, Parsons SJ. Tyrosine kinases are required for catecholamine secretion and mitogen-activated protein kinase activation in bovine adrenal chromaffin cells. J. Neurochem. 1996; 66: 1103-12.
    • (1996) J. Neurochem. , vol.66 , pp. 1103-1112
    • Cox, M.E.1    Ely, C.M.2    Catling, A.D.3    Weber, M.J.4    Parsons, S.J.5
  • 42
    • 0029666287 scopus 로고    scopus 로고
    • 2+-dependent translocation of protein kinase C and glucose-induced insulin release
    • 2+-dependent translocation of protein kinase C and glucose-induced insulin release. J. Biol. Chem. 1996; 271: 18154-60.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18154-18160
    • Deeney, J.T.1    Cunningham, B.A.2    Chheda, S.3
  • 43
    • 13344269671 scopus 로고    scopus 로고
    • PKC-dependent stimulation of exocytosis by sulfonylureas in pancreatic beta cells
    • Eliasson L, Renstrom E, Ammala C et al. PKC-dependent stimulation of exocytosis by sulfonylureas in pancreatic beta cells. Science 1996; 271: 813-15.
    • (1996) Science , vol.271 , pp. 813-815
    • Eliasson, L.1    Renstrom, E.2    Ammala, C.3
  • 45
    • 0029857103 scopus 로고    scopus 로고
    • Role of the Golgi apparatus in the phosphorylation of apolipoprotein B
    • Swift LL. Role of the Golgi apparatus in the phosphorylation of apolipoprotein B. J. Biol. Chem. 1996; 271: 31491-5.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31491-31495
    • Swift, L.L.1
  • 46
    • 0029869763 scopus 로고    scopus 로고
    • Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions
    • Jovanovic JN, Benfenati F, Siow YL et al. Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions. Proc. Natl Acad. Sci. USA 1996; 93: 3679-83.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 3679-3683
    • Jovanovic, J.N.1    Benfenati, F.2    Siow, Y.L.3
  • 47
    • 0029829890 scopus 로고    scopus 로고
    • Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions
    • Matsubara M, Kusubata M, Ishiguro K, Uchida T, Titani K, Taniguchi H. Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions. J. Biol. Chem. 1996; 271: 21 108-13.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21108-21113
    • Matsubara, M.1    Kusubata, M.2    Ishiguro, K.3    Uchida, T.4    Titani, K.5    Taniguchi, H.6
  • 48
    • 0029091466 scopus 로고
    • Phosphorylation of VAMP/synaptobrevin in synaptic vesicles by endogenous protein kinases
    • Nielander HB, Onofri F, Valtorta F et al. Phosphorylation of VAMP/synaptobrevin in synaptic vesicles by endogenous protein kinases. J. Neurochem. 1995; 65: 1712-20.
    • (1995) J. Neurochem. , vol.65 , pp. 1712-1720
    • Nielander, H.B.1    Onofri, F.2    Valtorta, F.3
  • 49
    • 0027419826 scopus 로고
    • Calcium-dependent serine phosphorylation of synaptophysin
    • Rubenstein JL, Greengard P, Czernik AJ. Calcium-dependent serine phosphorylation of synaptophysin. Synapse 1993; 13: 161-72.
    • (1993) Synapse , vol.13 , pp. 161-172
    • Rubenstein, J.L.1    Greengard, P.2    Czernik, A.J.3
  • 50
    • 0027511827 scopus 로고
    • Casein kinase II phosphorylates the synaptic vesicle protein p65
    • Bennett MK, Miller KG, Scheller RH. Casein kinase II phosphorylates the synaptic vesicle protein p65. J. Neurosci. 1993; 13: 1701-7.
    • (1993) J. Neurosci. , vol.13 , pp. 1701-1707
    • Bennett, M.K.1    Miller, K.G.2    Scheller, R.H.3
  • 51
    • 0027457763 scopus 로고
    • Phosphorylation of synaptotagmin I by casein kinase II
    • Davletov B, Sontag J-M, Hata Y et al. Phosphorylation of synaptotagmin I by casein kinase II. J. Biol. Chem. 1993; 268: 6816-22.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6816-6822
    • Davletov, B.1    Sontag, J.-M.2    Hata, Y.3
  • 52
    • 0027464680 scopus 로고
    • 2+/calmodulin protein kinase II in synaptic vesicles
    • 2+/calmodulin protein kinase II in synaptic vesicles. FEBS Lett. 1993; 317: 85-8.
    • (1993) FEBS Lett. , vol.317 , pp. 85-88
    • Popoli, M.1
  • 53
    • 0029963857 scopus 로고    scopus 로고
    • Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: Its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin
    • Fujita Y, Sasaki T, Fukui K et al. Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: Its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin. J. Biol. Chem. 1996; 271: 7265-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7265-7268
    • Fujita, Y.1    Sasaki, T.2    Fukui, K.3
  • 55
    • 0029971330 scopus 로고    scopus 로고
    • Growth-associated protein-43 (GAP-43) facilitates peptide hormone secretion in mouse anterior pituitary AtT-20 cells
    • Gamby C, Waage MC, Allen RG, Baizer L. Growth-associated protein-43 (GAP-43) facilitates peptide hormone secretion in mouse anterior pituitary AtT-20 cells. J. Biol. Chem. 1996; 271: 10023-8.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10023-10028
    • Gamby, C.1    Waage, M.C.2    Allen, R.G.3    Baizer, L.4
  • 56
    • 0030584097 scopus 로고    scopus 로고
    • Protein kinase C and its substrates
    • Liu J-P. Protein kinase C and its substrates. Mol. Cell. Endocrinol. 1996; 116: 1-29.
    • (1996) Mol. Cell. Endocrinol. , vol.116 , pp. 1-29
    • Liu, J.-P.1
  • 57
    • 0030013509 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 et al. Annexin II in exocytosis: Catecholamine secretion requires the translocation of p36 to the subplasmalemmal region in chromaffin cells. J. Cell Biol. 1946; 133: 1217-36.
    • (1946) J. Cell Biol. , vol.133 , pp. 1217-1236
    • Chasserot-Golaz, S.1    Vitale, N.2    Sagot, I.3
  • 58
    • 0029825766 scopus 로고    scopus 로고
    • In vivo phosphorylation of adaptors regulates their interaction with clathrin
    • Wilde A, Brodsky FM. In vivo phosphorylation of adaptors regulates their interaction with clathrin. J. Cell Biol. 1996; 135; 635-45.
    • (1996) J. Cell Biol. , vol.135 , pp. 635-645
    • Wilde, A.1    Brodsky, F.M.2
  • 59
    • 0028169459 scopus 로고
    • Presence of a beta II protein kinase C-selective nuclear membrane activation factor in human leukemia cells
    • Murray NR, Burns DJ, Fields AP. Presence of a beta II protein kinase C-selective nuclear membrane activation factor in human leukemia cells. J. Biol. Chem. 1994; 269: 21 385-90.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21385-21390
    • Murray, N.R.1    Burns, D.J.2    Fields, A.P.3
  • 60
    • 0028952767 scopus 로고
    • Dephosphorylated synapsin 1 anchors synaptic vesicles to actin cytoskeleton: An analysis by videomicroscopy
    • Ceccaldi PE, Grohovaz F, Benfenati F, Chieregatti E, Greengard P, Valtorta F. Dephosphorylated synapsin 1 anchors synaptic vesicles to actin cytoskeleton: An analysis by videomicroscopy. J. Cell Biol. 1995; 128: 905-12.
    • (1995) J. Cell Biol. , vol.128 , pp. 905-912
    • Ceccaldi, P.E.1    Grohovaz, F.2    Benfenati, F.3    Chieregatti, E.4    Greengard, P.5    Valtorta, F.6
  • 65
    • 0026788468 scopus 로고
    • Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes
    • Robinson PJ. Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes. J. Biol. Chem. 1992; 267: 21637-44.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21637-21644
    • Robinson, P.J.1
  • 66
    • 0027175638 scopus 로고
    • Activation of protein kinase C in vitro and in intact cells or synaptosomes determined by acetic acid extraction of MARCKS
    • Robinson PJ, Liu J-P, Chen W, Wenzel T. Activation of protein kinase C in vitro and in intact cells or synaptosomes determined by acetic acid extraction of MARCKS. Anal. Biochem. 1993; 210: 172-8.
    • (1993) Anal. Biochem. , vol.210 , pp. 172-178
    • Robinson, P.J.1    Liu, J.-P.2    Chen, W.3    Wenzel, T.4
  • 67
    • 0028196832 scopus 로고
    • Arginine vasopressin (AVP) causes the reversible phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in the ovine anterior pituitary. Evidence that MARCKS phosphorylation is associated with adrenocorticotropin (ACTH) secretion
    • Liu J-P, Engler D, Funder JW, Robinson PJ. Arginine vasopressin (AVP) causes the reversible phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in the ovine anterior pituitary. Evidence that MARCKS phosphorylation is associated with adrenocorticotropin (ACTH) secretion. Mol. Cell. Endocrinol. 1994; 101: 247-56.
    • (1994) Mol. Cell. Endocrinol. , vol.101 , pp. 247-256
    • Liu, J.-P.1    Engler, D.2    Funder, J.W.3    Robinson, P.J.4
  • 68
    • 0028028022 scopus 로고
    • Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles
    • Kim J, Shishido T, Jiang X, Aderem A, McLaughlin S. Phosphorylation, high ionic strength, and calmodulin reverse the binding of MARCKS to phospholipid vesicles. J. Biol. Chem. 1994; 269: 28214-19.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28214-28219
    • Kim, J.1    Shishido, T.2    Jiang, X.3    Aderem, A.4    McLaughlin, S.5
  • 69
    • 0028169455 scopus 로고
    • Dynamin is a calcium-sensitive phospholipid-binding protein with very high affinity for protein kinase C
    • Lin J-P, Powell KA, Sudhof TC, Robinson PJ. Dynamin is a calcium-sensitive phospholipid-binding protein with very high affinity for protein kinase C. J. Biol. Chem. 1994; 269: 21043-50.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21043-21050
    • Lin, J.-P.1    Powell, K.A.2    Sudhof, T.C.3    Robinson, P.J.4
  • 70
    • 0027186188 scopus 로고
    • Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals
    • Robinson PJ, Sontag J-M, Liu J-P et al. Dynamin GTPase regulated by protein kinase C phosphorylation in nerve terminals. Nature 1993; 365: 163-6.
    • (1993) Nature , vol.365 , pp. 163-166
    • Robinson, P.J.1    Sontag, J.-M.2    Liu, J.-P.3
  • 71
  • 72
    • 0027998457 scopus 로고
    • Calcineurin inhibition of dynamin I GTPase activity is coupled to nerve terminal depolarization
    • Liu J-P, Sim ATR, Robinson PJ. Calcineurin inhibition of dynamin I GTPase activity is coupled to nerve terminal depolarization. Science 1994; 265: 970-3.
    • (1994) Science , vol.265 , pp. 970-973
    • Liu, J.-P.1    Sim, A.T.R.2    Robinson, P.J.3
  • 74
    • 0030604917 scopus 로고    scopus 로고
    • Phosphorylation of dynamin by ERK2 inhibits the dynamin-microtubule interaction
    • Earnest S, Khokhlatchev A, Albanesi JP, Barylko B. Phosphorylation of dynamin by ERK2 inhibits the dynamin-microtubule interaction. FEBS Lett. 1996; 396: 62-6.
    • (1996) FEBS Lett. , vol.396 , pp. 62-66
    • Earnest, S.1    Khokhlatchev, A.2    Albanesi, J.P.3    Barylko, B.4
  • 75
    • 0028784414 scopus 로고
    • Dynamin forms polymeric complexes in the presence of lipid vesicles. Characterisation of chemically cross-linked dynamin molecules
    • Tuma PL, Collins CA, Dynamin forms polymeric complexes in the presence of lipid vesicles. Characterisation of chemically cross-linked dynamin molecules. J. Biol. Chem. 1995; 270: 26707-14.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26707-26714
    • Tuma, P.L.1    Collins, C.A.2
  • 76
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw JE, Schmid SL. Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature 1995; 374: 190-2.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.