메뉴 건너뛰기




Volumn 32, Issue 5, 2009, Pages 275-282

Friends and foes in synaptic transmission: the role of tomosyn in vesicle priming

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PROTEIN MUNC13; SNARE PROTEIN; SYNTAXIN; TOMOSYN; UNCLASSIFIED DRUG;

EID: 65349152502     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2009.01.004     Document Type: Review
Times cited : (47)

References (70)
  • 1
    • 33748923996 scopus 로고    scopus 로고
    • Vesicle pools, docking, priming, and release
    • Becherer U., and Rettig J. Vesicle pools, docking, priming, and release. Cell Tissue Res. 326 (2006) 393-407
    • (2006) Cell Tissue Res. , vol.326 , pp. 393-407
    • Becherer, U.1    Rettig, J.2
  • 2
    • 0036801359 scopus 로고    scopus 로고
    • The synaptic vesicle cycle: exocytosis and endocytosis in Drosophila and C. elegans
    • Richmond J.E., and Broadie K. The synaptic vesicle cycle: exocytosis and endocytosis in Drosophila and C. elegans. Curr. Opin. Neurobiol. 12 (2002) 499-507
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 499-507
    • Richmond, J.E.1    Broadie, K.2
  • 3
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Sudhof T.C. The synaptic vesicle cycle. Annu. Rev. Neurosci. 27 (2004) 509-547
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Sudhof, T.C.1
  • 4
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer D., et al. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 15781-15786
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 15781-15786
    • Fasshauer, D.1
  • 6
    • 3442879896 scopus 로고    scopus 로고
    • Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles
    • Sorensen J.B. Formation, stabilisation and fusion of the readily releasable pool of secretory vesicles. Pflugers Arch. 448 (2004) 347-362
    • (2004) Pflugers Arch. , vol.448 , pp. 347-362
    • Sorensen, J.B.1
  • 7
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton R.B., et al. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395 (1998) 347-353
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1
  • 8
    • 46449090904 scopus 로고    scopus 로고
    • Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion
    • Lu X., et al. Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion. Nat. Struct. Mol. Biol. 15 (2008) 700-706
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 700-706
    • Lu, X.1
  • 9
    • 2342661231 scopus 로고    scopus 로고
    • Principles of exocytosis and membrane fusion
    • Jahn R. Principles of exocytosis and membrane fusion. Ann. N. Y. Acad. Sci. 1014 (2004) 170-178
    • (2004) Ann. N. Y. Acad. Sci. , vol.1014 , pp. 170-178
    • Jahn, R.1
  • 10
    • 0037122459 scopus 로고    scopus 로고
    • RIM1α is required for presynaptic long-term potentiation
    • Castillo P.E., et al. RIM1α is required for presynaptic long-term potentiation. Nature 415 (2002) 327-330
    • (2002) Nature , vol.415 , pp. 327-330
    • Castillo, P.E.1
  • 11
    • 0034623062 scopus 로고    scopus 로고
    • Assembly of snare core complexes occurs prior to neurotransmitter release to set the readily-releasable pool of synaptic vesicles
    • Lonart G., and Sudhof T.C. Assembly of snare core complexes occurs prior to neurotransmitter release to set the readily-releasable pool of synaptic vesicles. J. Biol. Chem. 275 (2000) 27703-27707
    • (2000) J. Biol. Chem. , vol.275 , pp. 27703-27707
    • Lonart, G.1    Sudhof, T.C.2
  • 12
    • 0037204063 scopus 로고    scopus 로고
    • Differential control of vesicle priming and short-term plasticity by Munc13 isoforms
    • Rosenmund C., et al. Differential control of vesicle priming and short-term plasticity by Munc13 isoforms. Neuron 33 (2002) 411-424
    • (2002) Neuron , vol.33 , pp. 411-424
    • Rosenmund, C.1
  • 13
    • 0037022308 scopus 로고    scopus 로고
    • The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis
    • Sorensen J.B., et al. The SNARE protein SNAP-25 is linked to fast calcium triggering of exocytosis. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1627-1632
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1627-1632
    • Sorensen, J.B.1
  • 14
    • 34250857340 scopus 로고    scopus 로고
    • Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter
    • Wojcik S.M., and Brose N. Regulation of membrane fusion in synaptic excitation-secretion coupling: speed and accuracy matter. Neuron 55 (2007) 11-24
    • (2007) Neuron , vol.55 , pp. 11-24
    • Wojcik, S.M.1    Brose, N.2
  • 15
    • 17344376286 scopus 로고    scopus 로고
    • Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process
    • Fujita Y., et al. Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the neurotransmitter release process. Neuron 20 (1998) 905-915
    • (1998) Neuron , vol.20 , pp. 905-915
    • Fujita, Y.1
  • 16
    • 25444454048 scopus 로고    scopus 로고
    • 2+-dependent exocytosis of neurotransmitter
    • 2+-dependent exocytosis of neurotransmitter. J. Cell Biol. 170 (2005) 1113-1125
    • (2005) J. Cell Biol. , vol.170 , pp. 1113-1125
    • Baba, T.1
  • 17
    • 33746726458 scopus 로고    scopus 로고
    • Antagonistic regulation of synaptic vesicle priming by tomosyn and UNC-13
    • McEwen J.M., et al. Antagonistic regulation of synaptic vesicle priming by tomosyn and UNC-13. Neuron 51 (2006) 303-315
    • (2006) Neuron , vol.51 , pp. 303-315
    • McEwen, J.M.1
  • 18
    • 33750805030 scopus 로고    scopus 로고
    • Molecular anatomy of a trafficking organelle
    • Takamori S., et al. Molecular anatomy of a trafficking organelle. Cell 127 (2006) 831-846
    • (2006) Cell , vol.127 , pp. 831-846
    • Takamori, S.1
  • 19
    • 33746853822 scopus 로고    scopus 로고
    • Tomosyn-1 is involved in a post-docking event required for pancreatic β-cell exocytosis
    • Cheviet S., et al. Tomosyn-1 is involved in a post-docking event required for pancreatic β-cell exocytosis. J. Cell Sci. 119 (2006) 2912-2920
    • (2006) J. Cell Sci. , vol.119 , pp. 2912-2920
    • Cheviet, S.1
  • 20
    • 33644783907 scopus 로고    scopus 로고
    • Tomosyn is expressed in β-cells and negatively regulates insulin exocytosis
    • Zhang W., et al. Tomosyn is expressed in β-cells and negatively regulates insulin exocytosis. Diabetes 55 (2006) 574-581
    • (2006) Diabetes , vol.55 , pp. 574-581
    • Zhang, W.1
  • 21
    • 34547942015 scopus 로고    scopus 로고
    • Receptor-mediated regulation of tomosyn-syntaxin 1A interactions in bovine adrenal chromaffin cells
    • Gladycheva S.E., et al. Receptor-mediated regulation of tomosyn-syntaxin 1A interactions in bovine adrenal chromaffin cells. J. Biol. Chem. 282 (2007) 22887-22899
    • (2007) J. Biol. Chem. , vol.282 , pp. 22887-22899
    • Gladycheva, S.E.1
  • 22
    • 0042818205 scopus 로고    scopus 로고
    • Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation
    • Widberg C.H., et al. Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a role in insulin-stimulated GLUT4 translocation. J. Biol. Chem. 278 (2003) 35093-35101
    • (2003) J. Biol. Chem. , vol.278 , pp. 35093-35101
    • Widberg, C.H.1
  • 23
    • 13244292391 scopus 로고    scopus 로고
    • Two distinct genes drive expression of seven tomosyn isoforms in the mammalian brain, sharing a conserved structure with a unique variable domain
    • Groffen A.J., et al. Two distinct genes drive expression of seven tomosyn isoforms in the mammalian brain, sharing a conserved structure with a unique variable domain. J. Neurochem. 92 (2005) 554-568
    • (2005) J. Neurochem. , vol.92 , pp. 554-568
    • Groffen, A.J.1
  • 24
    • 8744252596 scopus 로고    scopus 로고
    • Structural basis for the inhibitory role of tomosyn in exocytosis
    • Pobbati A.V., et al. Structural basis for the inhibitory role of tomosyn in exocytosis. J. Biol. Chem. 279 (2004) 47192-47200
    • (2004) J. Biol. Chem. , vol.279 , pp. 47192-47200
    • Pobbati, A.V.1
  • 25
    • 0033525719 scopus 로고    scopus 로고
    • Three splicing variants of tomosyn and identification of their syntaxin- binding region
    • Yokoyama S., et al. Three splicing variants of tomosyn and identification of their syntaxin- binding region. Biochem. Biophys. Res. Commun. 256 (1999) 218-222
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 218-222
    • Yokoyama, S.1
  • 26
    • 34047100822 scopus 로고    scopus 로고
    • Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism
    • Hattendorf D.A., et al. Structure of the yeast polarity protein Sro7 reveals a SNARE regulatory mechanism. Nature 446 (2007) 567-571
    • (2007) Nature , vol.446 , pp. 567-571
    • Hattendorf, D.A.1
  • 27
    • 3142701373 scopus 로고    scopus 로고
    • Regulation of SNAREs by tomosyn and ROCK: implication in extension and retraction of neurites
    • Sakisaka T., et al. Regulation of SNAREs by tomosyn and ROCK: implication in extension and retraction of neurites. J. Cell Biol. 166 (2004) 17-25
    • (2004) J. Cell Biol. , vol.166 , pp. 17-25
    • Sakisaka, T.1
  • 28
    • 0031696595 scopus 로고    scopus 로고
    • Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil
    • Masuda E.S., et al. Tomosyn binds t-SNARE proteins via a VAMP-like coiled coil. Neuron 21 (1998) 479-480
    • (1998) Neuron , vol.21 , pp. 479-480
    • Masuda, E.S.1
  • 29
    • 33750829722 scopus 로고    scopus 로고
    • Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells
    • Nili U., et al. Munc18-1 phosphorylation by protein kinase C potentiates vesicle pool replenishment in bovine chromaffin cells. Neuroscience 143 (2006) 487-500
    • (2006) Neuroscience , vol.143 , pp. 487-500
    • Nili, U.1
  • 30
    • 33845987734 scopus 로고    scopus 로고
    • Selective activation of cognate SNAREpins by Sec1/Munc18 proteins
    • Shen J., et al. Selective activation of cognate SNAREpins by Sec1/Munc18 proteins. Cell 128 (2007) 183-195
    • (2007) Cell , vol.128 , pp. 183-195
    • Shen, J.1
  • 31
    • 0035974886 scopus 로고    scopus 로고
    • Munc18-1 promotes large dense-core vesicle docking
    • Voets T., et al. Munc18-1 promotes large dense-core vesicle docking. Neuron 31 (2001) 581-591
    • (2001) Neuron , vol.31 , pp. 581-591
    • Voets, T.1
  • 32
    • 33750241320 scopus 로고    scopus 로고
    • Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes
    • Zilly F.E., et al. Munc18-bound syntaxin readily forms SNARE complexes with synaptobrevin in native plasma membranes. PLoS Biol. 4 (2006) 1789-1797
    • (2006) PLoS Biol. , vol.4 , pp. 1789-1797
    • Zilly, F.E.1
  • 33
    • 0042733066 scopus 로고    scopus 로고
    • The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis
    • Hatsuzawa K., et al. The R-SNARE motif of tomosyn forms SNARE core complexes with syntaxin 1 and SNAP-25 and down-regulates exocytosis. J. Biol. Chem. 278 (2003) 31159-31166
    • (2003) J. Biol. Chem. , vol.278 , pp. 31159-31166
    • Hatsuzawa, K.1
  • 34
    • 24744452186 scopus 로고    scopus 로고
    • Amisyn regulates exocytosis and fusion pore stability by both syntaxin-dependent and syntaxin-independent mechanisms
    • Constable J.R., et al. Amisyn regulates exocytosis and fusion pore stability by both syntaxin-dependent and syntaxin-independent mechanisms. J. Biol. Chem. 280 (2005) 31615-31623
    • (2005) J. Biol. Chem. , vol.280 , pp. 31615-31623
    • Constable, J.R.1
  • 35
    • 34548842752 scopus 로고    scopus 로고
    • Tomosyn negatively regulates CAPS-dependent peptide release at Caenorhabditis elegans synapses
    • Gracheva E.O., et al. Tomosyn negatively regulates CAPS-dependent peptide release at Caenorhabditis elegans synapses. J. Neurosci. 27 (2007) 10176-10184
    • (2007) J. Neurosci. , vol.27 , pp. 10176-10184
    • Gracheva, E.O.1
  • 36
    • 49949098549 scopus 로고    scopus 로고
    • Modulating vesicle priming reveals that vesicle immobilization is necessary but not sufficient for fusion-competence
    • Yizhar O., and Ashery U. Modulating vesicle priming reveals that vesicle immobilization is necessary but not sufficient for fusion-competence. PLoS One 3 (2008) e2694
    • (2008) PLoS One , vol.3
    • Yizhar, O.1    Ashery, U.2
  • 37
    • 1442354782 scopus 로고    scopus 로고
    • Tomosyn inhibits priming of large dense-core vesicles in a calcium-dependent manner
    • Yizhar O., et al. Tomosyn inhibits priming of large dense-core vesicles in a calcium-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2578-2583
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2578-2583
    • Yizhar, O.1
  • 38
    • 33644745585 scopus 로고    scopus 로고
    • Using microarrays to facilitate positional cloning: identification of tomosyn as an inhibitor of neurosecretion
    • Dybbs M., et al. Using microarrays to facilitate positional cloning: identification of tomosyn as an inhibitor of neurosecretion. PLoS Genet. 1 (2005) 6-16
    • (2005) PLoS Genet. , vol.1 , pp. 6-16
    • Dybbs, M.1
  • 39
    • 33747364921 scopus 로고    scopus 로고
    • Tomosyn inhibits synaptic vesicle priming in Caenorhabditis elegans
    • Gracheva E.O., et al. Tomosyn inhibits synaptic vesicle priming in Caenorhabditis elegans. PLoS Biol. 4 (2006) 1426-1437
    • (2006) PLoS Biol. , vol.4 , pp. 1426-1437
    • Gracheva, E.O.1
  • 40
    • 55949121583 scopus 로고    scopus 로고
    • Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release
    • Sakisaka T., et al. Dual inhibition of SNARE complex formation by tomosyn ensures controlled neurotransmitter release. J. Cell Biol. 183 (2008) 323-337
    • (2008) J. Cell Biol. , vol.183 , pp. 323-337
    • Sakisaka, T.1
  • 41
    • 34848928507 scopus 로고    scopus 로고
    • Multiple functional domains are involved in tomosyn regulation of exocytosis
    • Yizhar O., et al. Multiple functional domains are involved in tomosyn regulation of exocytosis. J. Neurochem. 103 (2007) 604-616
    • (2007) J. Neurochem. , vol.103 , pp. 604-616
    • Yizhar, O.1
  • 42
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • Fasshauer D., et al. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry 37 (1998) 10354-10362
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1
  • 43
    • 20544459380 scopus 로고    scopus 로고
    • Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function
    • Gangar A., et al. Structurally conserved interaction of Lgl family with SNAREs is critical to their cellular function. Curr. Biol. 15 (2005) 1136-1142
    • (2005) Curr. Biol. , vol.15 , pp. 1136-1142
    • Gangar, A.1
  • 44
    • 0033549568 scopus 로고    scopus 로고
    • Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9
    • Lehman K., et al. Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J. Cell Biol. 146 (1999) 125-140
    • (1999) J. Cell Biol. , vol.146 , pp. 125-140
    • Lehman, K.1
  • 45
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer E.J., et al. The ancient regulatory-protein family of WD-repeat proteins. Nature 371 (1994) 297-300
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1
  • 46
    • 0033133919 scopus 로고    scopus 로고
    • The WD repeat: a common architecture for diverse functions
    • Smith T.F., et al. The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 24 (1999) 181-185
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 181-185
    • Smith, T.F.1
  • 47
    • 0028061614 scopus 로고
    • The Drosophila lethal(2)giant larvae tumor suppressor protein forms homo-oligomers and is associated with nonmuscle myosin II heavy chain
    • Strand D., et al. The Drosophila lethal(2)giant larvae tumor suppressor protein forms homo-oligomers and is associated with nonmuscle myosin II heavy chain. J. Cell Biol. 127 (1994) 1361-1373
    • (1994) J. Cell Biol. , vol.127 , pp. 1361-1373
    • Strand, D.1
  • 48
    • 0036156362 scopus 로고    scopus 로고
    • Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells
    • Musch A., et al. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells. Mol. Biol. Cell 13 (2002) 158-168
    • (2002) Mol. Biol. Cell , vol.13 , pp. 158-168
    • Musch, A.1
  • 49
    • 0031904190 scopus 로고    scopus 로고
    • Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function
    • Kagami M., et al. Sro7p, a Saccharomyces cerevisiae counterpart of the tumor suppressor l(2)gl protein, is related to myosins in function. Genetics 149 (1998) 1717-1727
    • (1998) Genetics , vol.149 , pp. 1717-1727
    • Kagami, M.1
  • 50
    • 0034618663 scopus 로고    scopus 로고
    • Tumor suppressors: linking cell polarity and growth control
    • Wodarz A. Tumor suppressors: linking cell polarity and growth control. Curr. Biol. 10 (2000) R624-R626
    • (2000) Curr. Biol. , vol.10
    • Wodarz, A.1
  • 51
    • 33646540110 scopus 로고    scopus 로고
    • Lethal giant larvae take on a life of their own
    • Wirtz-Peitz F., and Knoblich J.A. Lethal giant larvae take on a life of their own. Trends Cell Biol. 16 (2006) 234-241
    • (2006) Trends Cell Biol. , vol.16 , pp. 234-241
    • Wirtz-Peitz, F.1    Knoblich, J.A.2
  • 52
    • 26944465715 scopus 로고    scopus 로고
    • Myosin 5a controls insulin granule recruitment during late-phase secretion
    • Ivarsson R., et al. Myosin 5a controls insulin granule recruitment during late-phase secretion. Traffic 6 (2005) 1027-1035
    • (2005) Traffic , vol.6 , pp. 1027-1035
    • Ivarsson, R.1
  • 53
    • 0029027953 scopus 로고
    • Role of myosin in neurotransmitter release: functional studies at synapses formed in culture
    • Mochida S. Role of myosin in neurotransmitter release: functional studies at synapses formed in culture. J. Physiol. (Paris) 89 (1995) 83-94
    • (1995) J. Physiol. (Paris) , vol.89 , pp. 83-94
    • Mochida, S.1
  • 54
    • 3042646322 scopus 로고    scopus 로고
    • New roles of myosin II during vesicle transport and fusion in chromaffin cells
    • Neco P., et al. New roles of myosin II during vesicle transport and fusion in chromaffin cells. J. Biol. Chem. 279 (2004) 27450-27457
    • (2004) J. Biol. Chem. , vol.279 , pp. 27450-27457
    • Neco, P.1
  • 55
    • 0037387771 scopus 로고    scopus 로고
    • Myosins II and V in chromaffin cells: myosin V is a chromaffin vesicle molecular motor involved in secretion
    • Rose S.D., et al. Myosins II and V in chromaffin cells: myosin V is a chromaffin vesicle molecular motor involved in secretion. J. Neurochem. 85 (2003) 287-298
    • (2003) J. Neurochem. , vol.85 , pp. 287-298
    • Rose, S.D.1
  • 56
    • 26244449813 scopus 로고    scopus 로고
    • 2+-dependent binding of syntaxin-1A
    • 2+-dependent binding of syntaxin-1A. Mol. Biol. Cell 16 (2005) 4519-4530
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4519-4530
    • Watanabe, M.1
  • 57
    • 43749101829 scopus 로고    scopus 로고
    • Myosin II activation and actin reorganization regulate the mode of quantal exocytosis in mouse adrenal chromaffin cells
    • Doreian B.W., et al. Myosin II activation and actin reorganization regulate the mode of quantal exocytosis in mouse adrenal chromaffin cells. J. Neurosci. 28 (2008) 4470-4478
    • (2008) J. Neurosci. , vol.28 , pp. 4470-4478
    • Doreian, B.W.1
  • 58
    • 44849143151 scopus 로고    scopus 로고
    • Myosin II contributes to fusion pore expansion during exocytosis
    • Neco P., et al. Myosin II contributes to fusion pore expansion during exocytosis. J. Biol. Chem. 283 (2008) 10949-10957
    • (2008) J. Biol. Chem. , vol.283 , pp. 10949-10957
    • Neco, P.1
  • 59
    • 0032479425 scopus 로고    scopus 로고
    • o stimulates a granule-bound phosphatidylinositol 4-kinase by activating RhoA in chromaffin cells
    • o stimulates a granule-bound phosphatidylinositol 4-kinase by activating RhoA in chromaffin cells. J. Biol. Chem. 273 (1998) 16913-16920
    • (1998) J. Biol. Chem. , vol.273 , pp. 16913-16920
    • Gasman, S.1
  • 61
    • 13444267951 scopus 로고    scopus 로고
    • Phosphorylation-induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae
    • Betschinger J., et al. Phosphorylation-induced autoinhibition regulates the cytoskeletal protein Lethal (2) giant larvae. Curr. Biol. 15 (2005) 276-282
    • (2005) Curr. Biol. , vol.15 , pp. 276-282
    • Betschinger, J.1
  • 62
    • 34247588238 scopus 로고    scopus 로고
    • Budding insights on cell polarity
    • Fasshauer D., and Jahn R. Budding insights on cell polarity. Nat. Struct. Mol. Biol. 14 (2007) 360-362
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 360-362
    • Fasshauer, D.1    Jahn, R.2
  • 63
    • 54949110127 scopus 로고    scopus 로고
    • Docking of secretory vesicles is syntaxin dependent
    • de Wit H., et al. Docking of secretory vesicles is syntaxin dependent. PLoS One 1 (2006) e126
    • (2006) PLoS One , vol.1
    • de Wit, H.1
  • 64
    • 34548263167 scopus 로고    scopus 로고
    • Open syntaxin docks synaptic vesicles
    • Hammarlund M., et al. Open syntaxin docks synaptic vesicles. PLoS Biol. 5 (2007) e198
    • (2007) PLoS Biol. , vol.5
    • Hammarlund, M.1
  • 65
    • 33748129499 scopus 로고    scopus 로고
    • UNC-13 and UNC-10/rim localize synaptic vesicles to specific membrane domains
    • Weimer R.M., et al. UNC-13 and UNC-10/rim localize synaptic vesicles to specific membrane domains. J. Neurosci. 26 (2006) 8040-8047
    • (2006) J. Neurosci. , vol.26 , pp. 8040-8047
    • Weimer, R.M.1
  • 66
    • 37249047613 scopus 로고    scopus 로고
    • Tomosyn negatively regulates both synaptic transmitter and neuropeptide release at the C. elegans neuromuscular junction
    • Gracheva E.O., et al. Tomosyn negatively regulates both synaptic transmitter and neuropeptide release at the C. elegans neuromuscular junction. J. Physiol. 585 (2007) 705-709
    • (2007) J. Physiol. , vol.585 , pp. 705-709
    • Gracheva, E.O.1
  • 67
    • 0035913332 scopus 로고    scopus 로고
    • An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming
    • Richmond J.E., et al. An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming. Nature 412 (2001) 338-341
    • (2001) Nature , vol.412 , pp. 338-341
    • Richmond, J.E.1
  • 68
    • 5444228457 scopus 로고    scopus 로고
    • A new platform to study the molecular mechanisms of exocytosis
    • Mezer A., et al. A new platform to study the molecular mechanisms of exocytosis. J. Neurosci. 24 (2004) 8838-8846
    • (2004) J. Neurosci. , vol.24 , pp. 8838-8846
    • Mezer, A.1
  • 69
    • 0035341309 scopus 로고    scopus 로고
    • SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis
    • Lang T., et al. SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis. EMBO J. 20 (2001) 2202-2213
    • (2001) EMBO J. , vol.20 , pp. 2202-2213
    • Lang, T.1
  • 70
    • 22944450057 scopus 로고    scopus 로고
    • Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis
    • Zhang X., et al. Lethal giant larvae proteins interact with the exocyst complex and are involved in polarized exocytosis. J. Cell Biol. 170 (2005) 273-283
    • (2005) J. Cell Biol. , vol.170 , pp. 273-283
    • Zhang, X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.