메뉴 건너뛰기




Volumn 17, Issue 2, 2006, Pages 711-722

SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 6; CLATHRIN; DYNAMIN; F ACTIN; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN; SYNTAXIN 13; SYNTAXIN 1A; TRIPHOSPHOINOSITIDE; UNCLASSIFIED DRUG;

EID: 31944441121     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-05-0382     Document Type: Article
Times cited : (33)

References (74)
  • 1
    • 0033930208 scopus 로고    scopus 로고
    • Assembly of presynaptic active zones from cytoplasmic transport packets
    • Ahmari, S., Buchanan, J., and Smith, S. (2000). Assembly of presynaptic active zones from cytoplasmic transport packets. Nat. Neurosci. 3, 445-451.
    • (2000) Nat. Neurosci. , vol.3 , pp. 445-451
    • Ahmari, S.1    Buchanan, J.2    Smith, S.3
  • 2
    • 0041475820 scopus 로고    scopus 로고
    • ARF6 regulates a plasma membrane pool of phosphatidylinositol (4,5) bisphosphate required for regulated exocytosis
    • Aikawa, Y., and Martin, T.F.J. (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
  • 3
    • 0032561327 scopus 로고    scopus 로고
    • Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues
    • Arni, S., Keilbaugh, S., Ostermeyer, A., and Brown, D. (1998). Association of GAP-43 with detergent-resistant membranes requires two palmitoylated cysteine residues. J. Biol. Chem. 273, 28478-28485.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28478-28485
    • Arni, S.1    Keilbaugh, S.2    Ostermeyer, A.3    Brown, D.4
  • 4
    • 0033514468 scopus 로고    scopus 로고
    • A presynaptic role for the ADP ribosylation factor-specific GDP/GTP exchange factor msec7-l
    • Ashery, U., Koch, H., Scheuss, V., Brose, N., and Rettig, J. (1999). A presynaptic role for the ADP ribosylation factor-specific GDP/GTP exchange factor msec7-l. Proc. Natl. Acad. Sci. USA 96, 1094-1099.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1094-1099
    • Ashery, U.1    Koch, H.2    Scheuss, V.3    Brose, N.4    Rettig, J.5
  • 7
    • 0035865345 scopus 로고    scopus 로고
    • A genomic perspective on membrane compartment organization
    • Bock, J. B., Matern, H. T., Peden, A. A., and Scheller, R. H. (2001). A genomic perspective on membrane compartment organization. Nature 409, 839-841.
    • (2001) Nature , vol.409 , pp. 839-841
    • Bock, J.B.1    Matern, H.T.2    Peden, A.A.3    Scheller, R.H.4
  • 9
    • 0035802108 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate and ARF6-regulated membrane traffic
    • Brown, F. D., Rozelle, A. L., Yin, H. L., Balla, T., and Donaldson, J. G. (2001). Phosphatidylinositol 4,5-bisphosphate and ARF6-regulated membrane traffic. J. Cell Biol. 154, 1007-1017.
    • (2001) J. Cell Biol. , vol.154 , pp. 1007-1017
    • Brown, F.D.1    Rozelle, A.L.2    Yin, H.L.3    Balla, T.4    Donaldson, J.G.5
  • 10
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri, L., and Lithgow, T. (2004). A complete set of SNAREs in yeast. Traffic 5, 45-52.
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 12
    • 0034947026 scopus 로고    scopus 로고
    • Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes
    • Cheever, M. L., Sato, T. K., deBeer, T., Kutateladze, T. G., Emr, S. D., and Overduin, M. (2001). Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes. Nat. Cell Biol. 4, 613-618.
    • (2001) Nat. Cell Biol. , vol.4 , pp. 613-618
    • Cheever, M.L.1    Sato, T.K.2    Debeer, T.3    Kutateladze, T.G.4    Emr, S.D.5    Overduin, M.6
  • 13
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner, S., and Schmid, S. (2003). Regulated portals of entry into the cell. Nature 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.1    Schmid, S.2
  • 14
    • 0028036513 scopus 로고
    • Induction of mutant dynamin specifically blocks endocytic vesicle formation
    • Damke, H., Baba, T., Warnock, D. E., and Schmid, S. L. (1994). Induction of mutant dynamin specifically blocks endocytic vesicle formation. J. Cell Biol. 127, 915-934.
    • (1994) J. Cell Biol. , vol.127 , pp. 915-934
    • Damke, H.1    Baba, T.2    Warnock, D.E.3    Schmid, S.L.4
  • 15
    • 0037031482 scopus 로고    scopus 로고
    • Transfer of M2 muscarinic acetylcholine receptors to clathrin-derived early endosomes following clathrin-independent endocytosis
    • Delaney, K. A., Murph, M. M., Brown, L. M., and Radhakrishna, H. (2002). Transfer of M2 muscarinic acetylcholine receptors to clathrin-derived early endosomes following clathrin-independent endocytosis. J. Biol. Chem. 277, 33439-33446.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33439-33446
    • Delaney, K.A.1    Murph, M.M.2    Brown, L.M.3    Radhakrishna, H.4
  • 16
    • 0030766987 scopus 로고    scopus 로고
    • A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytockeletal rearrangements
    • D'Souza-Schorey, C., Boshans, R. L., McDonough, M., Stahl, P. D., and Van Aelst, L. (1997). A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytockeletal rearrangements. EMBO J. 16, 5445-5454.
    • (1997) EMBO J. , vol.16 , pp. 5445-5454
    • D'Souza-Schorey, C.1    Boshans, R.L.2    McDonough, M.3    Stahl, P.D.4    Van Aelst, L.5
  • 17
    • 0028914182 scopus 로고
    • A regulatory role for ARF6 in receptor-mediated endocytosis
    • D'Souza-Schorey, Li, G., Columbo, M. I., and Stahl, P. D. (1995). A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267, 1175-1178.
    • (1995) Science , vol.267 , pp. 1175-1178
    • D'Souza-Schorey1    Li, G.2    Columbo, M.I.3    Stahl, P.D.4
  • 18
    • 0029065157 scopus 로고
    • Ultrastructural localization of SNAP25 within the rat spinal cord and peripheral nervous system
    • Due, C., and Catsicas, S. (1995). Ultrastructural localization of SNAP25 within the rat spinal cord and peripheral nervous system. J. Comp. Neurol. 356, 152-163.
    • (1995) J. Comp. Neurol. , vol.356 , pp. 152-163
    • Due, C.1    Catsicas, S.2
  • 19
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • Ghosh, R. N., Mallet, W. G., Soe, T. T., McGraw, T. E., and Maxfield, F. R. (1998). An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J. Cell Biol. 142, 923-936.
    • (1998) J. Cell Biol. , vol.142 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 20
    • 0033597815 scopus 로고    scopus 로고
    • SNAP25 is targeted to the plasma membrane through a novel membrane-binding domain
    • Gonzalo, S., Greentree, W. K., and Linder, M. E. (1999). SNAP25 is targeted to the plasma membrane through a novel membrane-binding domain. J. Biol. Chem. 274, 21313-21318.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21313-21318
    • Gonzalo, S.1    Greentree, W.K.2    Linder, M.E.3
  • 21
    • 0031952838 scopus 로고    scopus 로고
    • SNAP25 palmitoylation and plasma membrane targeting required for a functional secretory pathway
    • Gonzalo, S., and Linder, M. E. (1998). SNAP25 palmitoylation and plasma membrane targeting required for a functional secretory pathway. Mol. Bio. Cell 9, 585-597.
    • (1998) Mol. Bio. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 22
    • 0035929157 scopus 로고    scopus 로고
    • Direct observation of membrane retrieval in chromaffin cells by capacitance measurements
    • Henkel, A. W., Horstmann, H., and Henkel, M. K. (2001). Direct observation of membrane retrieval in chromaffin cells by capacitance measurements. FEBS. Let. 505, 414-418.
    • (2001) FEBS. Let. , vol.505 , pp. 414-418
    • Henkel, A.W.1    Horstmann, H.2    Henkel, M.K.3
  • 23
    • 0026471991 scopus 로고
    • The 25kDa synaptosomal-associated protein SNAP25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess, D., Slater, T., Wilson, M., and Skene, J. (1992). The 25kDa synaptosomal-associated protein SNAP25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 12, 4634-4641.
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.1    Slater, T.2    Wilson, M.3    Skene, J.4
  • 24
    • 0033601075 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G. protein ARF6 in membrane ruffle formation
    • Honda, K., et. al. (1999). Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G. protein ARF6 in membrane ruffle formation. Cell 99, 521-532.
    • (1999) Cell , vol.99 , pp. 521-532
    • Honda, K.1
  • 25
    • 10444287633 scopus 로고    scopus 로고
    • Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins
    • Huang, K., et al. (2004). Huntingtin-interacting protein HIP14 is a palmitoyl transferase involved in palmitoylation and trafficking of multiple neuronal proteins. Neuron 44, 977-986.
    • (2004) Neuron , vol.44 , pp. 977-986
    • Huang, K.1
  • 26
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., Lang, T., and Sudhof, T. C. (2003). Membrane fusion. Cell 112, 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 27
    • 0038825177 scopus 로고    scopus 로고
    • ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ
    • Krauss, M., Kinuta, M., Wenk, M. R., De Camilli, P., Takei, K., and 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    Kinuta, M.2    Wenk, M.R.3    De Camilli, P.4    Takei, K.5    Haucke, V.6
  • 28
    • 0028837490 scopus 로고
    • Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane
    • Kutay, U., Ahnert-Hilger, G., Hartmann, E., Wiedenmann, B., and Rapoport, T. (1995). Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane. EMBO J. 14, 217-223.
    • (1995) EMBO J. , vol.14 , pp. 217-223
    • Kutay, U.1    Ahnert-Hilger, G.2    Hartmann, E.3    Wiedenmann, B.4    Rapoport, T.5
  • 29
    • 0030800671 scopus 로고    scopus 로고
    • Characterization of the palmitoylation domain of SNAP25
    • Lane, S., and Liu, Y. (1997). Characterization of the palmitoylation domain of SNAP25. J. Neurochem. 69, 1864-1869.
    • (1997) J. Neurochem. , vol.69 , pp. 1864-1869
    • Lane, S.1    Liu, Y.2
  • 30
    • 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., and 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
  • 31
    • 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., Holzer, H., and 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    Holzer, H.3    Jahn, R.4
  • 32
    • 0025940101 scopus 로고
    • Brefeldin A's effect on endosome, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., Yuan, L., Tipper, C., Amherdt, M., Orci, L., and Klausner, R. (1991). Brefeldin A's effect on endosome, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67, 601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.6
  • 33
    • 0029874859 scopus 로고    scopus 로고
    • Axonal transport and targeting of the t-SNAREs SNAP25 and syntaxin 1 in the peripheral nervous system
    • Li, J.-Y., Jahn, R., and Dahlstrom, A. (1996). Axonal transport and targeting of the t-SNAREs SNAP25 and syntaxin 1 in the peripheral nervous system. Eur. J. Cell Biol. 70, 12-22.
    • (1996) Eur. J. Cell Biol. , vol.70 , pp. 12-22
    • Li, J.-Y.1    Jahn, R.2    Dahlstrom, A.3
  • 34
    • 0037072816 scopus 로고    scopus 로고
    • SNAP25 traffics to the plasma membrane by a syntaxin-independent mechanism
    • Loranger, S. S., and Linder, M. E. (2002). SNAP25 traffics to the plasma membrane by a syntaxin-independent mechanism. J. Biol. Chem. 277, 34303-34309.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34303-34309
    • Loranger, S.S.1    Linder, M.E.2
  • 35
    • 0041806509 scopus 로고    scopus 로고
    • A dual mechanism controlling the localization and function of exocytic v-SNAREs
    • Martinez-Arca, S., et al. (2003). A dual mechanism controlling the localization and function of exocytic v-SNAREs. Proc. Natl. Acad. Sci. USA 100, 9011-9016.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9011-9016
    • Martinez-Arca, S.1
  • 36
    • 0032851639 scopus 로고    scopus 로고
    • +-stimulation contain a plethora of presynaptic membrane proteins
    • +-stimulation contain a plethora of presynaptic membrane proteins. Neuroscience 94, 985-996.
    • (1999) Neuroscience , vol.94 , pp. 985-996
    • Marxen, M.1    Volknandt, W.2    Zimmerman, H.3
  • 38
    • 0034677078 scopus 로고    scopus 로고
    • SNAP25 is present on the Golgi apparatus of retinal neurons
    • Morgans, C, and Brandstatter, J. H. (2000). SNAP25 is present on the Golgi apparatus of retinal neurons. Neuroreport 11, 85-88.
    • (2000) Neuroreport , vol.11 , pp. 85-88
    • Morgans, C.1    Brandstatter, J.H.2
  • 40
    • 0032498607 scopus 로고    scopus 로고
    • Visualization of the dynamic synaptic vesicle and plasma membrane proteins in living axons
    • Nakata, T., Terada, S., and Hirokawa, N. (1998). Visualization of the dynamic synaptic vesicle and plasma membrane proteins in living axons. J. Cell Biol. 140, 659-674.
    • (1998) J. Cell Biol. , vol.140 , pp. 659-674
    • Nakata, T.1    Terada, S.2    Hirokawa, N.3
  • 41
    • 0037328748 scopus 로고    scopus 로고
    • Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides
    • Naslavsky, N., Weigert, R., and Donaldson, J. G. (2003). Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides. Mol. Biol. Cell. 14, 417-431.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 417-431
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 42
    • 3342977736 scopus 로고    scopus 로고
    • Characterization of a nonclathrin endocytic pathway: Membrane cargo and lipid requirements
    • Naslavsky, N., Weigert, R., and Donaldson, J. G. (2004). Characterization of a nonclathrin endocytic pathway: membrane cargo and lipid requirements. Mol. Biol. Cell 15, 3542-3552.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3542-3552
    • Naslavsky, N.1    Weigert, R.2    Donaldson, J.G.3
  • 46
    • 0022571412 scopus 로고
    • Exocytotic exposure and recycling of membrane antigens of chromaffin granules: Ultrastructure evaluation after immunolabelling
    • Patzak, A., and Winkler, H. (1986). Exocytotic exposure and recycling of membrane antigens of chromaffin granules: ultrastructure evaluation after immunolabelling. J. Cell Biol. 102, 510-515.
    • (1986) J. Cell Biol. , vol.102 , pp. 510-515
    • Patzak, A.1    Winkler, H.2
  • 47
    • 0028951905 scopus 로고
    • Overexpression of wild-type and mutant ARF1 and ARF 6, distinct perturbations of non overlapping membrane compartments
    • Peters, P. J., Hsu, V. W., Ooi, C. E., Finazzi, D., Teal, S. B., Oorschot, V., Donaldson, J. G., and Klausner, R. D. (1995). Overexpression of wild-type and mutant ARF1 and ARF 6, distinct perturbations of non overlapping membrane compartments. J. Cell Biol. 128, 1003-1017.
    • (1995) J. Cell Biol. , vol.128 , pp. 1003-1017
    • Peters, P.J.1    Hsu, V.W.2    Ooi, C.E.3    Finazzi, D.4    Teal, S.B.5    Oorschot, V.6    Donaldson, J.G.7    Klausner, R.D.8
  • 48
    • 0032538835 scopus 로고    scopus 로고
    • Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes
    • Prekeris, R., Klumperman, J., Chen, Y. A., and Scheller, R. H. (1998). Syntaxin 13 mediates cycling of plasma membrane proteins via tubulovesicular recycling endosomes. J. Cell Biol. 143, 957-971.
    • (1998) J. Cell Biol. , vol.143 , pp. 957-971
    • Prekeris, R.1    Klumperman, J.2    Chen, Y.A.3    Scheller, R.H.4
  • 49
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna, H., Al-Awar, O., Khachikian, Z., and Donaldson, J. G. (1999). ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell. Sci. 112, 855-866.
    • (1999) J. Cell. Sci. , vol.112 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 50
    • 0030816319 scopus 로고    scopus 로고
    • ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway
    • Radhakrishna, H., and Donaldson, J. G. (1997). ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway. J. Cell Biol. 139, 49-61.
    • (1997) J. Cell Biol. , vol.139 , pp. 49-61
    • Radhakrishna, H.1    Donaldson, J.G.2
  • 51
    • 0034700364 scopus 로고    scopus 로고
    • Molecular aspects of the cellular activities of ADP-ribosylation factors
    • Randazzo, P. A., Nie, Z., Miura, K., and Hsu, V. W. (2000). Molecular aspects of the cellular activities of ADP-ribosylation factors. Sci. STKE 2000, re1.
    • (2000) Sci. STKE , vol.2000
    • Randazzo, P.A.1    Nie, Z.2    Miura, K.3    Hsu, V.W.4
  • 52
    • 0027447921 scopus 로고
    • TGN38/41 recycles between the cell surface and the TGN: Brefeldin A affects its rate of return to the TGN
    • Reaves, B., Horn, M., and Banting, G. (1993). TGN38/41 recycles between the cell surface and the TGN: brefeldin A affects its rate of return to the TGN. Mol. Biol. Cell 4, 93-105.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 93-105
    • Reaves, B.1    Horn, M.2    Banting, G.3
  • 53
    • 0026627966 scopus 로고
    • Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators
    • Robinson, M. S., and Kreis, T. E. (1992). Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: effects of brefeldin A and G protein activators. Cell 69, 129-138.
    • (1992) Cell , vol.69 , pp. 129-138
    • Robinson, M.S.1    Kreis, T.E.2
  • 54
    • 0032775945 scopus 로고    scopus 로고
    • Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells
    • Rowe, J., Corradi, N., Malosio, M., Taverna, E., Halban, P., Meldolesi, J., and Rosa, P. (1999). Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells. J. Cell Sci. 112, 1865-1877.
    • (1999) J. Cell Sci. , vol.112 , pp. 1865-1877
    • Rowe, J.1    Corradi, N.2    Malosio, M.3    Taverna, E.4    Halban, P.5    Meldolesi, J.6    Rosa, P.7
  • 55
    • 12544252686 scopus 로고    scopus 로고
    • The SNARE proteins SNAP25 and SNAP23 display different affinities for lipid rafts in PC12 cells
    • Salaun, C., Gould, G. W., and Chamberlain, L. H. (2005). The SNARE proteins SNAP25 and SNAP23 display different affinities for lipid rafts in PC12 cells. J. Biol. Chem. 280, 1236-1240.
    • (2005) J. Biol. Chem. , vol.280 , pp. 1236-1240
    • Salaun, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 57
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J., and Linder, M. (2004). Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 73, 559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.1    Linder, M.2
  • 58
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Sollner, T., Bennet, M. K., Whiteheart, S. W., Scheller, R. H., and Rothman, J. E. (1993). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell. 75, 409-418.
    • (1993) Cell. , vol.75 , pp. 409-418
    • Sollner, T.1    Bennet, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 60
    • 0038825173 scopus 로고    scopus 로고
    • Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex
    • Sun, W., Yan, Q., Vida, T. A., and Bean, A. J. (2003). Hrs regulates early endosome fusion by inhibiting formation of an endosomal SNARE complex. J. Cell Biol. 162, 125-137.
    • (2003) J. Cell Biol. , vol.162 , pp. 125-137
    • Sun, W.1    Yan, Q.2    Vida, T.A.3    Bean, A.J.4
  • 61
    • 0033709492 scopus 로고    scopus 로고
    • SNAP25 is polarized to axons and abundant along the axolemma: An immunogold study of intact neurons
    • Tao-Cheng, J. H., Du, J., and McBain, C. J. (2000). SNAP25 is polarized to axons and abundant along the axolemma: an immunogold study of intact neurons. J. Neurocytol. 29, 67-77.
    • (2000) J. Neurocytol. , vol.29 , pp. 67-77
    • Tao-Cheng, J.H.1    Du, J.2    McBain, C.J.3
  • 62
  • 63
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferring receptor recycling by endosome-derived clathrin-coated vesicles
    • van Dam, E., and Stoorvogel, W. (2002). Dynamin-dependent transferring receptor recycling by endosome-derived clathrin-coated vesicles. Mol. Biol. Cell 13, 169-182.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 169-182
    • Van Dam, E.1    Stoorvogel, W.2
  • 64
    • 0034723194 scopus 로고    scopus 로고
    • Targeting of SNAP25 to membranes is mediated by its association with the target SNARE syntaxin
    • Vogel, K., Cabaniols, J.-P., and Roche, P. (2000). Targeting of SNAP25 to membranes is mediated by its association with the target SNARE syntaxin. J. Biol. Chem. 275, 2959-2965.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2959-2965
    • Vogel, K.1    Cabaniols, J.-P.2    Roche, P.3
  • 65
    • 0028815453 scopus 로고
    • The t-SNAREs syntaxin 1 and SNAP25 are present on organelles that participate in synaptic vesicle recycling
    • Walch-Solimena, C., Blasi, J., Edelmann, L., Chapman, E. R., von Mollard, G. F., and Jahn, R. (1995). The t-SNAREs syntaxin 1 and SNAP25 are present on organelles that participate in synaptic vesicle recycling. J. Cell Biol. 128, 637-645.
    • (1995) J. Cell Biol. , vol.128 , pp. 637-645
    • Walch-Solimena, C.1    Blasi, J.2    Edelmann, L.3    Chapman, E.R.4    Von Mollard, G.F.5    Jahn, R.6
  • 66
    • 0035425203 scopus 로고    scopus 로고
    • Cysteine residues of SNAP25 are required for SNARE disassembly and exocytosis but not for membrane targeting
    • Washbourne, P., Cansino, V., Mathews, J., Graham, M., Burgoyne, R., and Wilson, M. (2001). Cysteine residues of SNAP25 are required for SNARE disassembly and exocytosis but not for membrane targeting. Biochem. J. 357, 625-634.
    • (2001) Biochem. J. , vol.357 , pp. 625-634
    • Washbourne, P.1    Cansino, V.2    Mathews, J.3    Graham, M.4    Burgoyne, R.5    Wilson, M.6
  • 67
    • 0032479158 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate synthesis in immunoisolated caveolae-like vesicles and low buoyant density non-caveolar membranes
    • Waugh, M., Lawson, D., Tan, S., and Hsuan, J. (1998). Phosphatidylinositol 4-phosphate synthesis in immunoisolated caveolae-like vesicles and low buoyant density non-caveolar membranes. J. Biol. Chem. 273, 17115-17121.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17115-17121
    • Waugh, M.1    Lawson, D.2    Tan, S.3    Hsuan, J.4
  • 69
    • 0345737131 scopus 로고    scopus 로고
    • An immunohistochemical method that distinguishes free from complexed SNAP25
    • Xiao, J., Xia, Z., Pradhan, A., Zhou, Q., and Liu, Y. (2004). An immunohistochemical method that distinguishes free from complexed SNAP25. J. Neurosci. Res. 75, 143-151.
    • (2004) J. Neurosci. Res. , vol.75 , pp. 143-151
    • Xiao, J.1    Xia, Z.2    Pradhan, A.3    Zhou, Q.4    Liu, Y.5
  • 70
    • 0038311944 scopus 로고    scopus 로고
    • Phosphoinositide regulation of the actin cytoskeleton
    • Yin, H. L., and Janmey, P. A. (2003). Phosphoinositide regulation of the actin cytoskeleton. Annu. Rev. Physiol. 65, 761-789.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 761-789
    • Yin, H.L.1    Janmey, P.A.2
  • 71
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D., Violin, J., Newton, A., and Tsien, R. (2002). Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916.
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.1    Violin, J.2    Newton, A.3    Tsien, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.