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Volumn 10, Issue 8, 2009, Pages 1034-1046

Fluorescence lifetime imaging of interactions between Golgi tethering factors and Small GTPases in plants

Author keywords

Flim; FRET; GFP; Golgi; Small GTPase; Tethering factor

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR LIKE 1; GOLGIN CANDIDATE 5; GREEN FLUORESCENT PROTEIN; GRIP PROTEIN; GUANOSINE TRIPHOSPHATASE; RAB PROTEIN; RED FLUORESCENT PROTEIN; TATA ELEMENT MODULATORY FACTOR; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; VPS52 PROTEIN;

EID: 67649887900     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2009.00930.x     Document Type: Article
Times cited : (43)

References (82)
  • 1
    • 20444386846 scopus 로고    scopus 로고
    • The plant Golgi apparatus-going with the flow
    • Hawes C, Satiat-Jeunemaitre B. The plant Golgi apparatus-going with the flow. Biochim Biophys Acta 2005;1744:466-480.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 466-480
    • Hawes, C.1    Satiat-Jeunemaitre, B.2
  • 4
    • 0035983848 scopus 로고    scopus 로고
    • Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching
    • Brandizzi F, Snapp EL, Roberts AG, Lippincott-Schwartz J, Hawes C. Membrane protein transport between the endoplasmic reticulum and the Golgi in tobacco leaves is energy dependent but cytoskeleton independent: Evidence from selective photobleaching. Plant Cell 2002;14:1293-1309.
    • (2002) Plant Cell , vol.14 , pp. 1293-1309
    • Brandizzi, F.1    Snapp, E.L.2    Roberts, A.G.3    Lippincott-Schwartz, J.4    Hawes, C.5
  • 5
    • 29344456761 scopus 로고    scopus 로고
    • Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane
    • Runions J, Brach T, Kuhner S, Hawes C. Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J Exp Bot 2006;57:43-50.
    • (2006) J Exp Bot , vol.57 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kuhner, S.3    Hawes, C.4
  • 6
    • 15144343944 scopus 로고
    • Ultrastructure and a possible function of the intercisternal elements in dictyosomes
    • Kristen U. Ultrastructure and a possible function of the intercisternal elements in dictyosomes. Planta 1978;138:29-33.
    • (1978) Planta , vol.138 , pp. 29-33
    • Kristen, U.1
  • 7
    • 0028855261 scopus 로고
    • The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms
    • Staehelin LA, Moore I. The plant Golgi apparatus: Structure, functional organization and trafficking mechanisms. Annu Rev Plant Physiol Plant Mol Biol 1995;46:261-288.
    • (1995) Annu Rev Plant Physiol Plant Mol Biol , vol.46 , pp. 261-288
    • Staehelin, L.A.1    Moore, I.2
  • 9
    • 0013085340 scopus 로고    scopus 로고
    • Golgins in the structure and dynamics of the Golgi apparatus
    • Barr FA, Short B. Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 2003;15:405-413.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 405-413
    • Barr, F.A.1    Short, B.2
  • 10
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short B, Haas A, Barr FA. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim Biophys Acta 2005;1744:383-395.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 11
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul E, Lupashin V. Role of tethering factors in secretory membrane traffic. Am J Physiol Cell Physiol 2006;290:C11-C26.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Sztul, E.1    Lupashin, V.2
  • 12
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr FA, Puype M, Vandekerckhove J, Warren G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 1997;91:253-262.
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 13
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter J, Watson R, Giannakou ME, Clarke M, Warren G, Barr FA. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO 1999;18:4949-4960.
    • (1999) EMBO , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 15
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam J, Satoh A, Pelletier L, Warren G. Golgin tethers define subpopulations of COPI vesicles. Science 2005;307:1095-1098.
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 17
    • 26844526297 scopus 로고    scopus 로고
    • Holding it all together? Candidate proteins for the plant Golgi matrix
    • Latijnhouwers M, Hawes C, Carvalho C. Holding it all together? Candidate proteins for the plant Golgi matrix. Curr Opin Plant Biol 2005;8:632-639.
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 632-639
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3
  • 18
  • 19
    • 33644838123 scopus 로고    scopus 로고
    • An Arabidopsis GRIP domain protein locates to the trans - Golgi and binds the small GTPase ARL1
    • Latijnhouwers M, Hawes C, Carvalho C, Oparka K, Gillingham AK, Boevink P. An Arabidopsis GRIP domain protein locates to the trans - Golgi and binds the small GTPase ARL1. Plant J 2005;44:459-470.
    • (2005) Plant J , vol.44 , pp. 459-470
    • Latijnhouwers, M.1    Hawes, C.2    Carvalho, C.3    Oparka, K.4    Gillingham, A.K.5    Boevink, P.6
  • 20
    • 34249823659 scopus 로고    scopus 로고
    • Multiple roles of ADP-ribosylation factor 1 in plant cells include spatially regulated recruitment of coatomer and elements of the Golgi matrix
    • Matheson LA, Hanton SL, Rossi M, Latijnhouwers M, Stefano G, Renna L, Brandizzi F. Multiple roles of ADP-ribosylation factor 1 in plant cells include spatially regulated recruitment of coatomer and elements of the Golgi matrix. Plant Physiol 2007;143:1615-1627.
    • (2007) Plant Physiol , vol.143 , pp. 1615-1627
    • Matheson, L.A.1    Hanton, S.L.2    Rossi, M.3    Latijnhouwers, M.4    Stefano, G.5    Renna, L.6    Brandizzi, F.7
  • 21
    • 33745700235 scopus 로고    scopus 로고
    • ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix protein to the Golgi apparatus in plant cells
    • Stefano G, Renna L, Hanton SL, Chatre L, Haas TA, Brandizzi F. ARL1 plays a role in the binding of the GRIP domain of a peripheral matrix protein to the Golgi apparatus in plant cells. Plant Mol Biol 2006;61:431-449.
    • (2006) Plant Mol Biol , vol.61 , pp. 431-449
    • Stefano, G.1    Renna, L.2    Hanton, S.L.3    Chatre, L.4    Haas, T.A.5    Brandizzi, F.6
  • 23
    • 57249095874 scopus 로고    scopus 로고
    • ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix
    • Kang BH, Staehelin LA. ER-to-Golgi transport by COPII vesicles in Arabidopsis involves a ribosome-excluding scaffold that is transferred with the vesicles to the Golgi matrix. Protoplasma 2008;234:51-64.
    • (2008) Protoplasma , vol.234 , pp. 51-64
    • Kang, B.H.1    Staehelin, L.A.2
  • 26
    • 0033535585 scopus 로고    scopus 로고
    • The GRIP domain-a novel Golgi-targeting domain found in several coiled-coil proteins
    • Munro S, Nichols BJ. The GRIP domain-a novel Golgi-targeting domain found in several coiled-coil proteins. Curr Biol 1999;9:377-380.
    • (1999) Curr Biol , vol.9 , pp. 377-380
    • Munro, S.1    Nichols, B.J.2
  • 27
    • 0033535542 scopus 로고    scopus 로고
    • A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins
    • Kjer-Nielsen L, Teasdale RD, van Vliet C, Gleeson PA. A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr Biol 1999;9:385-388.
    • (1999) Curr Biol , vol.9 , pp. 385-388
    • Kjer-Nielsen, L.1    Teasdale, R.D.2    van Vliet, C.3    Gleeson, P.A.4
  • 29
    • 0037418580 scopus 로고    scopus 로고
    • Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3
    • Setty SR, Shin ME, Yoshino A, Marks MS, Burd CG. Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3. Curr Biol 2003;13:401-404.
    • (2003) Curr Biol , vol.13 , pp. 401-404
    • Setty, S.R.1    Shin, M.E.2    Yoshino, A.3    Marks, M.S.4    Burd, C.G.5
  • 31
    • 0035503740 scopus 로고    scopus 로고
    • An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes
    • Siniossoglou S, Pelham HR. An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes. EMBO 2001;20:5991-5998.
    • (2001) EMBO , vol.20 , pp. 5991-5998
    • Siniossoglou, S.1    Pelham, H.R.2
  • 32
    • 67649867409 scopus 로고    scopus 로고
    • AtRAB-H1 b and AtRAB-H1 c GTPases, homologues of the yeast Ypt6, target reporter proteins to the Golgi when expressed in Nicotiana tabacum and Arabidopsis thaliana
    • (In press)
    • Johansen JN, Chow CM, Moore I, Hawes C. AtRAB-H1 b and AtRAB-H1 c GTPases, homologues of the yeast Ypt6, target reporter proteins to the Golgi when expressed in Nicotiana tabacum and Arabidopsis thaliana. J Exp Biol 2009; (In press).
    • (2009) J Exp Biol
    • Johansen, J.N.1    Chow, C.M.2    Moore, I.3    Hawes, C.4
  • 33
    • 0037418595 scopus 로고    scopus 로고
    • The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus
    • Panic B, Whyte JR, Munro S. The ARF-like GTPases Arl1p and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr Biol 2003;13:405-410.
    • (2003) Curr Biol , vol.13 , pp. 405-410
    • Panic, B.1    Whyte, J.R.2    Munro, S.3
  • 34
    • 0141856316 scopus 로고    scopus 로고
    • Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi
    • Lu L, Hong W. Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell 2003;14:3767-3781.
    • (2003) Mol Biol Cell , vol.14 , pp. 3767-3781
    • Lu, L.1    Hong, W.2
  • 35
    • 0033535617 scopus 로고    scopus 로고
    • A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins
    • Barr FA. A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr Biol 1999;9:381-384.
    • (1999) Curr Biol , vol.9 , pp. 381-384
    • Barr, F.A.1
  • 36
    • 0033972955 scopus 로고    scopus 로고
    • Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi
    • Conibear E, Stevens TH. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell 2000;11:305-323.
    • (2000) Mol Biol Cell , vol.11 , pp. 305-323
    • Conibear, E.1    Stevens, T.H.2
  • 37
    • 0013468039 scopus 로고    scopus 로고
    • Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p
    • Conibear E, Cleck JN, Stevens TH. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlg1p. Mol Biol Cell 2003;14:1610-1623.
    • (2003) Mol Biol Cell , vol.14 , pp. 1610-1623
    • Conibear, E.1    Cleck, J.N.2    Stevens, T.H.3
  • 38
    • 0037073694 scopus 로고    scopus 로고
    • Vps51p links the VFT complex to the SNARE Tlg1p
    • Siniossoglou S, Pelham HR. Vps51p links the VFT complex to the SNARE Tlg1p. J Biol Chem 2002;277:48318-48324.
    • (2002) J Biol Chem , vol.277 , pp. 48318-48324
    • Siniossoglou, S.1    Pelham, H.R.2
  • 40
    • 3543008987 scopus 로고    scopus 로고
    • The putative Arabidopsis homolog of yeast vps52p is required for pollen tube elongation, localizes to Golgi, and might be involved in vesicle trafficking
    • Lobstein E, Guyon A, Ferault M, Twell D, Pelletier G, Bonhomme S. The putative Arabidopsis homolog of yeast vps52p is required for pollen tube elongation, localizes to Golgi, and might be involved in vesicle trafficking. Plant Physiol 2004;135:1480-1490.
    • (2004) Plant Physiol , vol.135 , pp. 1480-1490
    • Lobstein, E.1    Guyon, A.2    Ferault, M.3    Twell, D.4    Pelletier, G.5    Bonhomme, S.6
  • 42
    • 51049106560 scopus 로고    scopus 로고
    • Advanced technologies for studies on protein interactomes
    • Guan H, Kiss-Toth E. Advanced technologies for studies on protein interactomes. Adv Biochem Eng Biotechnol 2008;110:1-24.
    • (2008) Adv Biochem Eng Biotechnol , vol.110 , pp. 1-24
    • Guan, H.1    Kiss-Toth, E.2
  • 44
    • 53249155165 scopus 로고    scopus 로고
    • Detecting protein-protein interactions in vivo with FRET using multiphoton fluorescence lifetime imaging microscopy (FLIM)
    • Chapter 12: Unit 12 10
    • Lleres D, Swift S, Lamond AI. Detecting protein-protein interactions in vivo with FRET using multiphoton fluorescence lifetime imaging microscopy (FLIM). Curr Protoc Cytom 2007; Chapter 12: Unit 12 10.
    • (2007) Curr Protoc Cytom
    • Lleres, D.1    Swift, S.2    Lamond, A.I.3
  • 45
    • 33748456465 scopus 로고    scopus 로고
    • The visible touch: In planta visualization of protein-protein interactions by fluorophore-based methods
    • Bhat RA, Lahaye T, Panstruga R. The visible touch: In planta visualization of protein-protein interactions by fluorophore-based methods. Plant Methods 2006;2:12.
    • (2006) Plant Methods , vol.2 , pp. 12
    • Bhat, R.A.1    Lahaye, T.2    Panstruga, R.3
  • 46
    • 53949107378 scopus 로고    scopus 로고
    • Fluorescence complementation: An emerging tool for biological research
    • Shyu YJ, Hu CD. Fluorescence complementation: An emerging tool for biological research. Trends Biotechnol 2008;26:622-630.
    • (2008) Trends Biotechnol , vol.26 , pp. 622-630
    • Shyu, Y.J.1    Hu, C.D.2
  • 47
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • Wallrabe H, Periasamy A. Imaging protein molecules using FRET and FLIM microscopy. Curr Opin Biotechnol 2005;16:19-27.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 48
    • 33644853883 scopus 로고    scopus 로고
    • Using intrinsically fluorescent proteins for plant cell imaging
    • Dixit R, Cyr R, Gilroy S. Using intrinsically fluorescent proteins for plant cell imaging. Plant J 2006;45:599-615.
    • (2006) Plant J , vol.45 , pp. 599-615
    • Dixit, R.1    Cyr, R.2    Gilroy, S.3
  • 50
    • 0027767493 scopus 로고
    • Fluorescence lifetime imaging microscopy (FLIM) - Spatial resolution of microstructures on the nanosecond time-scale
    • Gadella TWJ, Jovin TM, Clegg RM. Fluorescence lifetime imaging microscopy (FLIM) - spatial resolution of microstructures on the nanosecond time-scale. Biophys Chem 1993;48:221-239.
    • (1993) Biophys Chem , vol.48 , pp. 221-239
    • Gadella, T.W.J.1    Jovin, T.M.2    Clegg, R.M.3
  • 51
    • 0347756761 scopus 로고    scopus 로고
    • Protein localization in living cells and tissues using FRET and FLIM
    • Chen Y, Mills JD, Periasamy A. Protein localization in living cells and tissues using FRET and FLIM. Differentiation 2003;71:528-541.
    • (2003) Differentiation , vol.71 , pp. 528-541
    • Chen, Y.1    Mills, J.D.2    Periasamy, A.3
  • 52
    • 84900271966 scopus 로고    scopus 로고
    • Practical fluorescence resonance energy transfer of molecular nanobioscopy of living cells
    • 3rd edn. In: Pawley JB, editor
    • Majoul I, Jia Y, Duden R. Practical fluorescence resonance energy transfer of molecular nanobioscopy of living cells, 3rd edn. In: Pawley JB, editor. Handbook of Biological Confocal Microscopy New York Springer 2006; p. 788-808.
    • (2006) Handbook of Biological Confocal Microscopy New York Springer , pp. 788-808
    • Majoul, I.1    Jia, Y.2    Duden, R.3
  • 53
    • 2142762991 scopus 로고    scopus 로고
    • Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy
    • Vermeer JE, Van Munster EB, Vischer NO, Gadella TW Jr. Probing plasma membrane microdomains in cowpea protoplasts using lipidated GFP-fusion proteins and multimode FRET microscopy. J Microsc 2004;214:190-200.
    • (2004) J Microsc , vol.214 , pp. 190-200
    • Vermeer, J.E.1    Van Munster, E.B.2    Vischer, N.O.3    Gadella, T.W.4
  • 55
    • 33846159104 scopus 로고    scopus 로고
    • Plant G protein heterotrimers require dual lipidation motifs of Galpha and Ggamma and do not dissociate upon activation
    • Adjobo-Hermans MJ, Goedhart J, Gadella TW, Jr. Plant G protein heterotrimers require dual lipidation motifs of Galpha and Ggamma and do not dissociate upon activation. J Cell Sci 2006;119:5087-5097.
    • (2006) J Cell Sci , vol.119 , pp. 5087-5097
    • Adjobo-Hermans, M.J.1    Goedhart, J.2    Gadella, T.W.3
  • 57
    • 57049119012 scopus 로고    scopus 로고
    • Tomato spotted wilt virus nucleocapsid protein interacts with both viral glycoproteins Gn and Gc in planta
    • Ribeiro D, Borst JW, Goldbach R, Kormelink R. Tomato spotted wilt virus nucleocapsid protein interacts with both viral glycoproteins Gn and Gc in planta. Virology 2009;383:121-130.
    • (2009) Virology , vol.383 , pp. 121-130
    • Ribeiro, D.1    Borst, J.W.2    Goldbach, R.3    Kormelink, R.4
  • 58
    • 34547625251 scopus 로고    scopus 로고
    • FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localization
    • Zelazny E, Borst JW, Muylaert M, Batoko H, Hemminga MA, Chaumont F. FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localization. Proc Natl Acad Sci U S A 2007;104:12359-12364.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12359-12364
    • Zelazny, E.1    Borst, J.W.2    Muylaert, M.3    Batoko, H.4    Hemminga, M.A.5    Chaumont, F.6
  • 59
    • 33749246845 scopus 로고    scopus 로고
    • The Arabidopsis thaliana AAA Protein CDC48A interacts in vivo with the somatic embryogenesis receptor-like kinase 1 receptor at the plasma membrane
    • Aker J, Borst JW, Karlova R, de Vries S. The Arabidopsis thaliana AAA Protein CDC48A interacts in vivo with the somatic embryogenesis receptor-like kinase 1 receptor at the plasma membrane. J Struct Biol 2006;156:62-71.
    • (2006) J Struct Biol , vol.156 , pp. 62-71
    • Aker, J.1    Borst, J.W.2    Karlova, R.3    de Vries, S.4
  • 60
    • 35348840808 scopus 로고    scopus 로고
    • In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using Forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy
    • Aker J, Hesselink R, Engel R, Karlova R, Borst JW, Visser AJ, de Vries SC. In vivo hexamerization and characterization of the Arabidopsis AAA ATPase CDC48A complex using Forster resonance energy transfer-fluorescence lifetime imaging microscopy and fluorescence correlation spectroscopy. Plant Physiol 2007;145:339-350.
    • (2007) Plant Physiol , vol.145 , pp. 339-350
    • Aker, J.1    Hesselink, R.2    Engel, R.3    Karlova, R.4    Borst, J.W.5    Visser, A.J.6    de Vries, S.C.7
  • 61
    • 14544267172 scopus 로고    scopus 로고
    • Recruitment and interaction dynamics of plant penetration resistance components in a plasma membrane microdomain
    • Bhat RA, Miklis M, Schmelzer E, Schulze-Lefert P, Panstruga R. Recruitment and interaction dynamics of plant penetration resistance components in a plasma membrane microdomain. Proc Natl Acad Sci U S A 2005;102:3135-3140.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3135-3140
    • Bhat, R.A.1    Miklis, M.2    Schmelzer, E.3    Schulze-Lefert, P.4    Panstruga, R.5
  • 62
    • 48549107461 scopus 로고    scopus 로고
    • Tobacco mosaic virus movement protein interacts with green fluorescent protein-tagged microtubule end-binding protein 1
    • Brandner K, Sambade A, Boutant E, Didier P, Mely Y, Ritzenthaler C, Heinlein M. Tobacco mosaic virus movement protein interacts with green fluorescent protein-tagged microtubule end-binding protein 1. Plant Physiol 2008;147:611-623.
    • (2008) Plant Physiol , vol.147 , pp. 611-623
    • Brandner, K.1    Sambade, A.2    Boutant, E.3    Didier, P.4    Mely, Y.5    Ritzenthaler, C.6    Heinlein, M.7
  • 63
    • 55549087588 scopus 로고    scopus 로고
    • Combination of novel green fluorescent protein mutant TSapphire and DsRed variant mOrange to set up a versatile in planta FRET-FLIM assay
    • Bayle V, Nussaume L, Bhat RA. Combination of novel green fluorescent protein mutant TSapphire and DsRed variant mOrange to set up a versatile in planta FRET-FLIM assay. Plant Physiol 2008;148:51-60.
    • (2008) Plant Physiol , vol.148 , pp. 51-60
    • Bayle, V.1    Nussaume, L.2    Bhat, R.A.3
  • 64
    • 0345306636 scopus 로고    scopus 로고
    • Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases
    • Larijani B, Hume AN, Tarafder AK, Seabra MC. Multiple factors contribute to inefficient prenylation of Rab27a in Rab prenylation diseases. J Biol Chem 2003;278:46798-46804.
    • (2003) J Biol Chem , vol.278 , pp. 46798-46804
    • Larijani, B.1    Hume, A.N.2    Tarafder, A.K.3    Seabra, M.C.4
  • 66
    • 42049093463 scopus 로고    scopus 로고
    • Real-time cellular uptake of serotonin using fluorescence lifetime imaging with two-photon excitation
    • Botchway SW, Parker AW, Bisby RH, Crisostomo AG. Real-time cellular uptake of serotonin using fluorescence lifetime imaging with two-photon excitation. Microsc Res Tech 2008;71:267-273.
    • (2008) Microsc Res Tech , vol.71 , pp. 267-273
    • Botchway, S.W.1    Parker, A.W.2    Bisby, R.H.3    Crisostomo, A.G.4
  • 67
    • 30944450665 scopus 로고    scopus 로고
    • Deep tissue two-photon microscopy
    • Helmchen F, Denk W. Deep tissue two-photon microscopy. Nat Methods 2005;2:932-940.
    • (2005) Nat Methods , vol.2 , pp. 932-940
    • Helmchen, F.1    Denk, W.2
  • 68
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien CT, Bartel PL, Sternglanz R, Fields S. The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest. Proc Natl Acad Sci U S A 1991;88:9578-9582.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 69
    • 58149181656 scopus 로고    scopus 로고
    • Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins
    • Sinka R, Gillingham AK, Kondylis V, Munro S. Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins. J Cell Biol 2008;183:607-615.
    • (2008) J Cell Biol , vol.183 , pp. 607-615
    • Sinka, R.1    Gillingham, A.K.2    Kondylis, V.3    Munro, S.4
  • 70
    • 0032614376 scopus 로고    scopus 로고
    • GFP variants for multispectral imaging of living cells
    • Haseloff J. GFP variants for multispectral imaging of living cells. Methods Cell Biol 1999;58:139-151.
    • (1999) Methods Cell Biol , vol.58 , pp. 139-151
    • Haseloff, J.1
  • 72
    • 53749085917 scopus 로고    scopus 로고
    • Advances in fluorescent protein-based imaging for the analysis of plant endomembranes
    • Held MA, Boulaflous A, Brandizzi F. Advances in fluorescent protein-based imaging for the analysis of plant endomembranes. Plant Physiol 2008;147:1469-1481.
    • (2008) Plant Physiol , vol.147 , pp. 1469-1481
    • Held, M.A.1    Boulaflous, A.2    Brandizzi, F.3
  • 73
    • 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 SM, Hughes MK, Keppler MD, Prag S, Marsh M, Vojnovic B, Ng T. Multiphoton-FLIM quantification of the EGFP-mRFP1 FRET pair for localization of membrane receptor-kinase interactions. Biophys J 2005;88:1224-1237.
    • (2005) Biophys J , vol.88 , pp. 1224-1237
    • Peter, M.1    Ameer-Beg, S.M.2    Hughes, M.K.3    Keppler, M.D.4    Prag, S.5    Marsh, M.6    Vojnovic, B.7    Ng, T.8
  • 75
    • 0034682666 scopus 로고    scopus 로고
    • EFGP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy
    • Jakobs S, Subramaniam V, Schonle A, Jovin TM, Hell SW. EFGP and DsRed expressing cultures of Escherichia coli imaged by confocal, two-photon and fluorescence lifetime microscopy. FEBS Lett 2000;479:131-135.
    • (2000) FEBS Lett , vol.479 , pp. 131-135
    • Jakobs, S.1    Subramaniam, V.2    Schonle, A.3    Jovin, T.M.4    Hell, S.W.5
  • 76
    • 0142245636 scopus 로고    scopus 로고
    • A gateway cloning vector set for high-throughput functional analysis of genes in planta
    • Curtis MD, Grossniklaus U. A gateway cloning vector set for high-throughput functional analysis of genes in planta. Plant Physiol 2003;133:462-469.
    • (2003) Plant Physiol , vol.133 , pp. 462-469
    • Curtis, M.D.1    Grossniklaus, U.2
  • 78
    • 38749150383 scopus 로고    scopus 로고
    • Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185
    • Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. Cell 2008;132:286-298.
    • (2008) Cell , vol.132 , pp. 286-298
    • Burguete, A.S.1    Fenn, T.D.2    Brunger, A.T.3    Pfeffer, S.R.4
  • 80
    • 0030989517 scopus 로고    scopus 로고
    • Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly
    • Haseloff J, Siemering KR, Prasher DC, Hodge S. Removal of a cryptic intron and subcellular localization of green fluorescent protein are required to mark transgenic Arabidopsis plants brightly. Proc Natl Acad Sci U S A 1997;94:2122-2127.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2122-2127
    • Haseloff, J.1    Siemering, K.R.2    Prasher, D.C.3    Hodge, S.4
  • 81
    • 0028954118 scopus 로고
    • Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/ PEG procedure
    • Gietz RD, Schiestl RH, Willems AR, Woods RA. Studies on the transformation of intact yeast cells by the LiAc/SS-DNA/PEG procedure. Yeast 1995;11:355-360.
    • (1995) Yeast , vol.11 , pp. 355-360
    • Gietz, R.D.1    Schiestl, R.H.2    Willems, A.R.3    Woods, R.A.4
  • 82
    • 34248653184 scopus 로고    scopus 로고
    • Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants
    • Sparkes IA, Runions J, Kearns A, Hawes C. Rapid, transient expression of fluorescent fusion proteins in tobacco plants and generation of stably transformed plants. Nat Protoc 2006;1:2019-2025.
    • (2006) Nat Protoc , vol.1 , pp. 2019-2025
    • Sparkes, I.A.1    Runions, J.2    Kearns, A.3    Hawes, C.4


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