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Volumn 14, Issue 6, 2008, Pages 507-518

In-depth fluorescence lifetime imaging analysis revealing SNAP25A-rabphilin 3A interactions

Author keywords

Exocytosis; Fluorescence lifetime imaging microscopy; Fluorescence resonance energy transfer; Green fluorescent protein; Image analysis; Rabphilin 3A (RPH3A); SNAP25A; Two photon excitation fluorescence microscopy

Indexed keywords

HYBRID PROTEIN; NERVE PROTEIN; PHOTOPROTEIN; RABPHILIN 3A; RABPHILIN-3A; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SNAP25 PROTEIN, RAT; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; VESICULAR TRANSPORT PROTEIN;

EID: 55749115796     PISSN: 14319276     EISSN: 14358115     Source Type: Journal    
DOI: 10.1017/S1431927608080628     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 33745758070 scopus 로고    scopus 로고
    • A second SNARE role for exocytic SNAP25 in endosome fusion
    • AIKAWA, Y., LYNCH, K.L., BOSWELL, K.L. & MARTIN, T.F.J. (2006). A second SNARE role for exocytic SNAP25 in endosome fusion. Mol Biol Cell 17, 2113-2124.
    • (2006) Mol Biol Cell , vol.17 , pp. 2113-2124
    • AIKAWA, Y.1    LYNCH, K.L.2    BOSWELL, K.L.3    MARTIN, T.F.J.4
  • 2
    • 8344255773 scopus 로고    scopus 로고
    • Tracking SNARE complex formation in live endocrine cells
    • AN, S.J. & ALMERS, W. (2004). Tracking SNARE complex formation in live endocrine cells. Science 306, 1042-1046.
    • (2004) Science , vol.306 , pp. 1042-1046
    • AN, S.J.1    ALMERS, W.2
  • 3
    • 0034760118 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy in cell biology
    • AXELROD, D. (2001). Total internal reflection fluorescence microscopy in cell biology. Traffic 2, 764-774.
    • (2001) Traffic , vol.2 , pp. 764-774
    • AXELROD, D.1
  • 4
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin-partners in exocytosis
    • BAI, J. & CHAPMAN, E.R. (2004). The C2 domains of synaptotagmin-partners in exocytosis. Trends Biochem Sci 29, 143-151.
    • (2004) Trends Biochem Sci , vol.29 , pp. 143-151
    • BAI, J.1    CHAPMAN, E.R.2
  • 5
    • 33748923996 scopus 로고    scopus 로고
    • Vesicle pools, docking, priming and release
    • BECHERER, U. & RETTIG, J. (2006). Vesicle pools, docking, priming and release. Cell Tissue Res 326, 393-407.
    • (2006) Cell Tissue Res , vol.326 , pp. 393-407
    • BECHERER, U.1    RETTIG, J.2
  • 6
    • 34249808797 scopus 로고    scopus 로고
    • The synaptic vesicle proteome
    • BURRÉ, J. & VOLKNANDT, W. (2007). The synaptic vesicle proteome. J Neurochem 101, 1448-1462.
    • (2007) J Neurochem , vol.101 , pp. 1448-1462
    • BURRÉ, J.1    VOLKNANDT, W.2
  • 7
    • 33646151431 scopus 로고    scopus 로고
    • Verification of antiparallel G-quadruplex structure in human telomeres by using two-photon excitation fluorescence lifetime imaging microscopy of the 3,6-Bis(1-methyl-4-vinylpyridinium)carbazole diiodide molecule
    • CHANG, C.C., CHU, J.F., KAO, F.J., CHIU, Y.C., LOU, P.J., CHEN, H.C. & CHANG, T.C. (2006). Verification of antiparallel G-quadruplex structure in human telomeres by using two-photon excitation fluorescence lifetime imaging microscopy of the 3,6-Bis(1-methyl-4-vinylpyridinium)carbazole diiodide molecule. Anal Chem 78, 2810-2815.
    • (2006) Anal Chem , vol.78 , pp. 2810-2815
    • CHANG, C.C.1    CHU, J.F.2    KAO, F.J.3    CHIU, Y.C.4    LOU, P.J.5    CHEN, H.C.6    CHANG, T.C.7
  • 8
    • 0347756761 scopus 로고    scopus 로고
    • Protein localization in living cells and tissues using FRET and FLIM
    • CHEN, Y., MILLS, J.D. & PERIASAMY, A. (2003). Protein localization in living cells and tissues using FRET and FLIM. Differentiation 71, 528-541.
    • (2003) Differentiation , vol.71 , pp. 528-541
    • CHEN, Y.1    MILLS, J.D.2    PERIASAMY, A.3
  • 10
    • 0141644218 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging for the two-photon microscope: Time-domain and frequency-domain methods
    • GRATTON, E., BREUSEGEM, S., SUTIN, J., RUAN, Q. & BARRY, N. (2003). Fluorescence lifetime imaging for the two-photon microscope: Time-domain and frequency-domain methods. J Biomed Optics 8, 381-390.
    • (2003) J Biomed Optics , vol.8 , pp. 381-390
    • GRATTON, E.1    BREUSEGEM, S.2    SUTIN, J.3    RUAN, Q.4    BARRY, N.5
  • 11
    • 33646185099 scopus 로고    scopus 로고
    • Fusion pores and fusion machines in Ca2+-triggered exocytosis
    • JACKSON, M.B. & CHAPMAN, E.R. (2006). Fusion pores and fusion machines in Ca2+-triggered exocytosis. Ann Rev Biophys Biomol Struct 35, 135-160.
    • (2006) Ann Rev Biophys Biomol Struct , vol.35 , pp. 135-160
    • JACKSON, M.B.1    CHAPMAN, E.R.2
  • 12
    • 38149098479 scopus 로고    scopus 로고
    • Detection of the interaction between SNAP25 and rabphilin in neuroendocrine PC12 cells using the FLIM/FRET technique
    • LEE, J.D., CHANG, Y.F., KAO, F.J., KAO, L.S., LIN, C.C., LU, A.C., SHYYU, B.C., CHIOU, S.H. & YANG, D.M. (2008). Detection of the interaction between SNAP25 and rabphilin in neuroendocrine PC12 cells using the FLIM/FRET technique. Microsc Res Tech 71, 26-34.
    • (2008) Microsc Res Tech , vol.71 , pp. 26-34
    • LEE, J.D.1    CHANG, Y.F.2    KAO, F.J.3    KAO, L.S.4    LIN, C.C.5    LU, A.C.6    SHYYU, B.C.7    CHIOU, S.H.8    YANG, D.M.9
  • 14
    • 0037072816 scopus 로고    scopus 로고
    • SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism
    • LORANGER, S.S. & LINDER, M.E. (2002). SNAP-25 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
  • 15
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • MARTENS, S., KOZLOV, M.M. & MCMAHON, H.T. (2007). How synaptotagmin promotes membrane fusion. Science 316, 1205-1208.
    • (2007) Science , vol.316 , pp. 1205-1208
    • MARTENS, S.1    KOZLOV, M.M.2    MCMAHON, H.T.3
  • 16
    • 34249099292 scopus 로고    scopus 로고
    • Time-correlated single photon counting FLIM: Some considerations for physiologists
    • MEDLINE, C., MCDONALD, A., BERGMANN, A. & DUNCAN, R.R. (2007). Time-correlated single photon counting FLIM: Some considerations for physiologists. Micros Res Tech 70, 420-425.
    • (2007) Micros Res Tech , vol.70 , pp. 420-425
    • MEDLINE, C.1    MCDONALD, A.2    BERGMANN, A.3    DUNCAN, R.R.4
  • 18
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • OSTERMEIER, C. & BRUNGER, A.T. (1999). Structural basis of rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96, 363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • OSTERMEIER, C.1    BRUNGER, A.T.2
  • 19
    • 21244478918 scopus 로고    scopus 로고
    • Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions
    • PETER, M., AMEER-BEG, S.M., HUGHES, M.K.Y., KEPPLER, M.D., PRAG, S., MARSH, M., VOJNOVIC, B. & NG, T. (2005). Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions. Biophy J 88, 1224-1237.
    • (2005) Biophy J , vol.88 , pp. 1224-1237
    • PETER, M.1    AMEER-BEG, S.M.2    HUGHES, M.K.Y.3    KEPPLER, M.D.4    PRAG, S.5    MARSH, M.6    VOJNOVIC, B.7    NG, T.8
  • 20
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • PISTON, D.W. & KREMERS, G.J. (2007). Fluorescent protein FRET: The good, the bad and the ugly. Trends Biochem Sci 32, 407-414.
    • (2007) Trends Biochem Sci , vol.32 , pp. 407-414
    • PISTON, D.W.1    KREMERS, G.J.2
  • 21
    • 20544453249 scopus 로고    scopus 로고
    • Imaging the secretory pathway: The past and future impact of live cell optical techniques
    • PRESLEY, J.F. (2005). Imaging the secretory pathway: The past and future impact of live cell optical techniques. Biochim Biophys Acta 1744, 259-272.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 259-272
    • PRESLEY, J.F.1
  • 22
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • RIZO, J., CHEN, X. & ARAC, D. (2006). Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trend Cell Biol 16, 339-350.
    • (2006) Trend Cell Biol , vol.16 , pp. 339-350
    • RIZO, J.1    CHEN, X.2    ARAC, D.3
  • 23
    • 13844267499 scopus 로고    scopus 로고
    • Total internal reflection fluorescence microscopy: Technical innovations and novel applications
    • SCHNECKENBURGER, H. (2005). Total internal reflection fluorescence microscopy: Technical innovations and novel applications. Curr Opin Biotech 16, 13-18.
    • (2005) Curr Opin Biotech , vol.16 , pp. 13-18
    • SCHNECKENBURGER, H.1
  • 25
    • 0027461829 scopus 로고
    • Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin
    • SHIRATAKI, H., KAIBUCHI, K., SAKODA, T., KISHIDA, S., YAMAGUCHI, T., WADA, K., MIYAZAKI, M. & TAKAI, Y. (1993). Rabphilin-3A, a putative target protein for smg p25A/rab3A p25 small GTP-binding protein related to synaptotagmin. Mol Cell Biol 13, 2061-2068.
    • (1993) Mol Cell Biol , vol.13 , pp. 2061-2068
    • SHIRATAKI, H.1    KAIBUCHI, K.2    SAKODA, T.3    KISHIDA, S.4    YAMAGUCHI, T.5    WADA, K.6    MIYAZAKI, M.7    TAKAI, Y.8
  • 26
    • 0035315984 scopus 로고    scopus 로고
    • A real-time view of life within 100 nm of the plasma membrane
    • STEYER, J.A. & ALMERS, W. (2001). A real-time view of life within 100 nm of the plasma membrane. Nat Rev Mol Cell Biol 2, 268-275.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 268-275
    • STEYER, J.A.1    ALMERS, W.2
  • 27
    • 38549106408 scopus 로고    scopus 로고
    • Mechanisms of exocytosis
    • doi:10.1111/j.1748-1716.2007.01803.x
    • SUGITA, S. (2007). Mechanisms of exocytosis. Acta Physiologica 192, 185-193. doi:10.1111/j.1748-1716.2007.01803.x.
    • (2007) Acta Physiologica , vol.192 , pp. 185-193
    • SUGITA, S.1
  • 29
    • 28244484879 scopus 로고    scopus 로고
    • The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells
    • TSUBOI, T. & FUKUDA, M. (2005). The C2B domain of rabphilin directly interacts with SNAP-25 and regulates the docking step of dense core vesicle exocytosis in PC12 cells. J Biol Chem 280, 39253-39259.
    • (2005) J Biol Chem , vol.280 , pp. 39253-39259
    • TSUBOI, T.1    FUKUDA, M.2
  • 30
    • 33846225536 scopus 로고    scopus 로고
    • The polybasic sequence in the C2B domain of rabphilin is required for the vesicle docking step in PC12 cells
    • TSUBOI, T., KANNO, E. & FUKUDA, M. (2007). The polybasic sequence in the C2B domain of rabphilin is required for the vesicle docking step in PC12 cells. J Neurochem 100, 770-779.
    • (2007) J Neurochem , vol.100 , pp. 770-779
    • TSUBOI, T.1    KANNO, E.2    FUKUDA, M.3
  • 33
    • 0344838541 scopus 로고    scopus 로고
    • Tracking of secretory vesicles of PC12 cells using total internal reflection fluorescence microscopy
    • YANG, D.M., HUANG, C.C., LIN, H.Y., TSAI, D.P., KAO, L.S., CHI, C.W. & LIN, C.C. (2003). Tracking of secretory vesicles of PC12 cells using total internal reflection fluorescence microscopy. J Microsc 209, 223-227.
    • (2003) J Microsc , vol.209 , pp. 223-227
    • YANG, D.M.1    HUANG, C.C.2    LIN, H.Y.3    TSAI, D.P.4    KAO, L.S.5    CHI, C.W.6    LIN, C.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.