메뉴 건너뛰기




Volumn 13, Issue 9, 2014, Pages 2337-2353

The global phosphoproteome of chlamydomonas reinhardtii reveals complex organellar phosphorylation in the flagella and thylakoid membrane

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPEPTIDE; PHOSPHOPROTEOME; PROTEOME; UNCLASSIFIED DRUG; ALGAL PROTEIN; PHOSPHOPROTEIN; POLYMER; TITANIUM; TITANIUM DIOXIDE;

EID: 84907209314     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.038281     Document Type: Article
Times cited : (89)

References (94)
  • 2
    • 77955619699 scopus 로고    scopus 로고
    • An outlook on microalgal biofuels
    • Wijffels, R. H., and Barbosa, M. J. (2010) An outlook on microalgal biofuels. Science 329, 796-799
    • (2010) Science , vol.329 , pp. 796-799
    • Wijffels, R.H.1    Barbosa, M.J.2
  • 4
    • 84865096530 scopus 로고    scopus 로고
    • Why nature chose phosphate to modify proteins
    • Hunter, T. (2012) Why nature chose phosphate to modify proteins. Philos. T. R. Soc. B 367, 2513-2516
    • (2012) Philos. T. R. Soc. B , vol.367 , pp. 2513-2516
    • Hunter, T.1
  • 6
    • 33748333438 scopus 로고    scopus 로고
    • Environmentally modulated phosphoproteome of photosynthetic membranes in the green alga Chlamydomonas reinhardtii
    • Turkina, M. V., Kargul, J., Blanco-Rivero, A., Villarejo, A., Barber, J., and Vener, A. V. (2006) Environmentally modulated phosphoproteome of photosynthetic membranes in the green alga Chlamydomonas reinhardtii. Mol. Cell. Proteomics 5, 1412-1425
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1412-1425
    • Turkina, M.V.1    Kargul, J.2    Blanco-Rivero, A.3    Villarejo, A.4    Barber, J.5    Vener, A.V.6
  • 7
    • 33646720305 scopus 로고    scopus 로고
    • CO2 limitation induces specific redox-dependent protein phosphorylation in Chlamydomonas reinhardtii
    • Turkina, M. V., Blanco-Rivero, A., Vainonen, J. P., Vener, A. V., and Villarejo, A. (2006) CO2 limitation induces specific redox-dependent protein phosphorylation in Chlamydomonas reinhardtii. Proteomics 6, 2693-2704
    • (2006) Proteomics , vol.6 , pp. 2693-2704
    • Turkina, M.V.1    Blanco-Rivero, A.2    Vainonen, J.P.3    Vener, A.V.4    Villarejo, A.5
  • 8
    • 77953152308 scopus 로고    scopus 로고
    • Stt7-dependent phosphorylation during state transitions in the green alga Chlamydomonas reinhardtii
    • Lemeille, S., Turkina, M. V., Vener, A. V., and Rochaix, J.-D. (2010) Stt7-dependent phosphorylation during state transitions in the green alga Chlamydomonas reinhardtii. Mol. Cell. Proteomics 9, 1281-1295
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1281-1295
    • Lemeille, S.1    Turkina, M.V.2    Vener, A.V.3    Rochaix, J.-D.4
  • 9
    • 38949093001 scopus 로고    scopus 로고
    • The phosphoproteome of a Chlamydomonas reinhardtii eyespot fraction includes key proteins of the light signaling pathway
    • Wagner, V., Ullmann, K., Mollwo, A., Kaminski, M., Mittag, M., and Kreimer, G. (2008) The phosphoproteome of a Chlamydomonas reinhardtii eyespot fraction includes key proteins of the light signaling pathway. Plant Physiol. 146, 772-788
    • (2008) Plant Physiol. , vol.146 , pp. 772-788
    • Wagner, V.1    Ullmann, K.2    Mollwo, A.3    Kaminski, M.4    Mittag, M.5    Kreimer, G.6
  • 10
    • 79961240127 scopus 로고    scopus 로고
    • Protein phosphorylation is a key event of flagellar disassembly revealed by analysis of flagellar phosphoproteins during flagellar shortening in Chlamydomonas
    • Pan, J., Naumann-Busch, B., Wang, L., Specht, M., Scholz, M., Trompelt, K., and Hippler, M. (2011) Protein phosphorylation is a key event of flagellar disassembly revealed by analysis of flagellar phosphoproteins during flagellar shortening in Chlamydomonas. J. Proteome Res. 10, 3830-3839
    • (2011) J. Proteome Res. , vol.10 , pp. 3830-3839
    • Pan, J.1    Naumann-Busch, B.2    Wang, L.3    Specht, M.4    Scholz, M.5    Trompelt, K.6    Hippler, M.7
  • 11
    • 67650469447 scopus 로고    scopus 로고
    • Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii
    • Boesger, J., Wagner, V., Weisheit, W., and Mittag, M. (2009) Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii. Eukaryot. Cell 8, 922-932
    • (2009) Eukaryot. Cell , vol.8 , pp. 922-932
    • Boesger, J.1    Wagner, V.2    Weisheit, W.3    Mittag, M.4
  • 12
    • 33645068852 scopus 로고    scopus 로고
    • Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways
    • Wagner, V., Gessner, G., Heiland, I., Kaminski, M., Hawat, S., Scheffler, K., and Mittag, M. (2006) Analysis of the phosphoproteome of Chlamydomonas reinhardtii provides new insights into various cellular pathways. Eukaryot. Cell 5, 457-468
    • (2006) Eukaryot. Cell , vol.5 , pp. 457-468
    • Wagner, V.1    Gessner, G.2    Heiland, I.3    Kaminski, M.4    Hawat, S.5    Scheffler, K.6    Mittag, M.7
  • 13
    • 43849091451 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection
    • McNulty, D. E., and Annan, R. S. (2008) Hydrophilic interaction chromatography reduces the complexity of the phosphoproteome and improves global phosphopeptide isolation and detection. Mol. Cell. Proteomics 7, 971-980
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 971-980
    • McNulty, D.E.1    Annan, R.S.2
  • 14
    • 26444539668 scopus 로고    scopus 로고
    • Orthogonality of separation in two-dimensional liquid chromatography
    • Gilar, M., Olivova, P., Daly, A. E., and Gebler, J. C. (2005) Orthogonality of separation in two-dimensional liquid chromatography. Anal. Chem. 77, 6426-6434
    • (2005) Anal. Chem. , vol.77 , pp. 6426-6434
    • Gilar, M.1    Olivova, P.2    Daly, A.E.3    Gebler, J.C.4
  • 15
    • 77957978971 scopus 로고    scopus 로고
    • In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ion-functionalized soluble nanopolymers
    • Iliuk, A. B., Martin, V. A., Alicie, B. M., Geahlen, R. L., and Tao, W. A. (2010) In-depth analyses of kinase-dependent tyrosine phosphoproteomes based on metal ion-functionalized soluble nanopolymers. Mol. Cell. Proteomics 9, 2162-2172
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2162-2172
    • Iliuk, A.B.1    Martin, V.A.2    Alicie, B.M.3    Geahlen, R.L.4    Tao, W.A.5
  • 17
    • 84862923173 scopus 로고    scopus 로고
    • Comprehensive comparison of iTRAQ and label-free LC-based quantitative proteomics approaches using two Chlamydomonas reinhardtii strains of interest for biofuels engineering
    • Wang, H., Alvarez, S., and Hicks, L. M. (2012) Comprehensive comparison of iTRAQ and label-free LC-based quantitative proteomics approaches using two Chlamydomonas reinhardtii strains of interest for biofuels engineering. J. Proteome Res. 11, 487-501
    • (2012) J. Proteome Res. , vol.11 , pp. 487-501
    • Wang, H.1    Alvarez, S.2    Hicks, L.M.3
  • 18
    • 69849085788 scopus 로고    scopus 로고
    • The development of an improved simple titanium dioxide enrichment method for phosphoproteomic research
    • Bai, Z., Liu, B., Li, W., Li, P., and Wang, H. (2009) The development of an improved simple titanium dioxide enrichment method for phosphoproteomic research. Rapid Commun Mass Sp. 23, 3013-3017
    • (2009) Rapid Commun Mass Sp. , vol.23 , pp. 3013-3017
    • Bai, Z.1    Liu, B.2    Li, W.3    Li, P.4    Wang, H.5
  • 19
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii, A. I., Keller, A., Kolker, E., and Aebersold, R. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal. Chem. 75, 4646-4658
    • (2003) Anal. Chem. , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 20
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller, A., Nesvizhskii, A. I., Kolker, E., and Aebersold, R. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal. Chem. 74, 5383-5392
    • (2002) Anal. Chem. , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 21
    • 33749853607 scopus 로고    scopus 로고
    • A probability-based approach for high-throughput protein phosphorylation analysis and site localization
    • Beausoleil, S. A., Villen, J., Gerber, S. A., Rush, J., and Gygi, S. P. (2006) A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat. Biotech. 24, 1285-1292
    • (2006) Nat. Biotech. , vol.24 , pp. 1285-1292
    • Beausoleil, S.A.1    Villen, J.2    Gerber, S.A.3    Rush, J.4    Gygi, S.P.5
  • 25
    • 84868332245 scopus 로고    scopus 로고
    • The Plasmodium falciparum schizont phosphoproteome reveals extensive phosphatidylinositol and cAMPprotein kinase a signaling
    • Lasonder, E., Green, J. L., Camarda, G., Talabani, H., Holder, A. A., Langsley, G., and Alano, P. (2012) The Plasmodium falciparum schizont phosphoproteome reveals extensive phosphatidylinositol and cAMPprotein kinase a signaling. J. Proteome Res. 11, 5323-5337
    • (2012) J. Proteome Res. , vol.11 , pp. 5323-5337
    • Lasonder, E.1    Green, J.L.2    Camarda, G.3    Talabani, H.4    Holder, A.A.5    Langsley, G.6    Alano, P.7
  • 26
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., and Gygi, S. P. (2005) An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotech. 23, 1391-1398
    • (2005) Nat. Biotech. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 27
    • 84891764407 scopus 로고    scopus 로고
    • Biological sequence motif discovery using motif-x
    • John Wiley & Sons, Inc
    • Chou, M. F., and Schwartz, D. (2002) Biological sequence motif discovery using motif-x. Current Protocols in Bioinformatics, John Wiley & Sons, Inc.
    • (2002) Current Protocols in Bioinformatics
    • Chou, M.F.1    Schwartz, D.2
  • 28
    • 1842861617 scopus 로고    scopus 로고
    • The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation
    • Turkina, M. V., Villarejo, A., and Vener, A. V. (2004) The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation. FEBS Lett. 564, 104-108
    • (2004) FEBS Lett. , vol.564 , pp. 104-108
    • Turkina, M.V.1    Villarejo, A.2    Vener, A.V.3
  • 29
    • 66749108480 scopus 로고    scopus 로고
    • A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the-proteobacterial mitochondrial ancestor
    • Atteia, A., Adrait, A., Brugière, S., Tardif, M., van Lis, R., Deusch, O., Dagan, T., Kuhn, L., Gontero, B., Martin, W., Garin, J., Joyard, J., and Rolland, N. (2009) A proteomic survey of Chlamydomonas reinhardtii mitochondria sheds new light on the metabolic plasticity of the organelle and on the nature of the-proteobacterial mitochondrial ancestor. Mol. Biol. Evol. 26, 1533-1548
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 1533-1548
    • Atteia, A.1    Adrait, A.2    Brugière, S.3    Tardif, M.4    Van Lis, R.5    Deusch, O.6    Dagan, T.7    Kuhn, L.8    Gontero, B.9    Martin, W.10    Garin, J.11    Joyard, J.12    Rolland, N.13
  • 30
    • 33747780498 scopus 로고    scopus 로고
    • Comparative proteomics of high light stress in the model alga Chlamydomonas reinhardtii
    • Förster, B., Mathesius, U., and Pogson, B. J. (2006) Comparative proteomics of high light stress in the model alga Chlamydomonas reinhardtii. Proteomics 6, 4309-4320
    • (2006) Proteomics , vol.6 , pp. 4309-4320
    • Förster, B.1    Mathesius, U.2    Pogson, B.J.3
  • 31
    • 77952825427 scopus 로고    scopus 로고
    • Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics
    • Terashima, M., Specht, M., Naumann, B., and Hippler, M. (2010) Characterizing the anaerobic response of Chlamydomonas reinhardtii by quantitative proteomics. Mol. Cell. Proteomics 9, 1514-1532
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1514-1532
    • Terashima, M.1    Specht, M.2    Naumann, B.3    Hippler, M.4
  • 32
    • 84859103646 scopus 로고    scopus 로고
    • Quantitative shotgun proteomics using a uniform (1)(5)N-labeled standard to monitor proteome dynamics in time course experiments reveals new insights into the heat stress response of Chlamydomonas reinhardtii
    • M110 004739
    • Muhlhaus, T., Weiss, J., Hemme, D., Sommer, F., and Schroda, M. (2011) Quantitative shotgun proteomics using a uniform (1)(5)N-labeled standard to monitor proteome dynamics in time course experiments reveals new insights into the heat stress response of Chlamydomonas reinhardtii. Mol. Cell. Proteomics 10, M110 004739
    • (2011) Mol. Cell. Proteomics , vol.10
    • Muhlhaus, T.1    Weiss, J.2    Hemme, D.3    Sommer, F.4    Schroda, M.5
  • 34
    • 0034722338 scopus 로고    scopus 로고
    • The 9 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility
    • Porter, M. E., and Sale, W. S. (2000) The 9 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phosphatases that control motility. J. Cell Biol. 151, F37-F42
    • (2000) J. Cell Biol. , vol.151 , pp. F37-F42
    • Porter, M.E.1    Sale, W.S.2
  • 35
    • 0033647305 scopus 로고    scopus 로고
    • Signal transduction during fertilization in the unicellular green alga, Chlamydomonas
    • Pan, J., and Snell, W. J. (2000) Signal transduction during fertilization in the unicellular green alga, Chlamydomonas. Curr. Opin. Microbiol. 3, 596-602
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 596-602
    • Pan, J.1    Snell, W.J.2
  • 36
    • 6344226513 scopus 로고    scopus 로고
    • Regulation of flagellar assembly by Glycogen Synthase Kinase 3 in Chlamydomonas reinhardtii
    • Wilson, N. F., and Lefebvre, P. A. (2004) Regulation of flagellar assembly by Glycogen Synthase Kinase 3 in Chlamydomonas reinhardtii. Eukaryot. Cell 3, 1307-1319
    • (2004) Eukaryot. Cell , vol.3 , pp. 1307-1319
    • Wilson, N.F.1    Lefebvre, P.A.2
  • 39
    • 0028095507 scopus 로고
    • Multiple sites of phosphorylation within the alpha heavy chain of Chlamydomonas outer arm dynein
    • King, S. M., and Witman, G. B. (1994) Multiple sites of phosphorylation within the alpha heavy chain of Chlamydomonas outer arm dynein. J. Biol. Chem. 269, 5452-5457
    • (1994) J. Biol. Chem. , vol.269 , pp. 5452-5457
    • King, S.M.1    Witman, G.B.2
  • 41
    • 0029113132 scopus 로고
    • Flagellar assembly in two hundred and fifty easy-tofollow steps
    • Dutcher, S. K. (1995) Flagellar assembly in two hundred and fifty easy-tofollow steps. Trends Genet. 11, 398-404
    • (1995) Trends Genet. , vol.11 , pp. 398-404
    • Dutcher, S.K.1
  • 42
    • 0017411320 scopus 로고
    • Phosphorylation of chloroplast membrane polypeptides
    • Bennett, J. (1977) Phosphorylation of chloroplast membrane polypeptides. Nature 269, 344-346
    • (1977) Nature , vol.269 , pp. 344-346
    • Bennett, J.1
  • 43
    • 36849155728 scopus 로고
    • Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems
    • Allen, J. F., Bennett, J., Steinback, K. E., and Arntzen, C. J. (1981) Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. Nature 291, 25-29
    • (1981) Nature , vol.291 , pp. 25-29
    • Allen, J.F.1    Bennett, J.2    Steinback, K.E.3    Arntzen, C.J.4
  • 45
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad, F., Ren, S., Cox, J., Olsen, J., Macek, B., Oroshi, M., and Mann, M. (2007) PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 8, R250
    • (2007) Genome Biol. , vol.8 , pp. R250
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.4    Macek, B.5    Oroshi, M.6    Mann, M.7
  • 47
    • 84984996500 scopus 로고    scopus 로고
    • The Gene Ontology project in 2008
    • Consortium, T. G. O. (2008) The Gene Ontology project in 2008. Nucleic Acids Res. 36, D440-D444
    • (2008) Nucleic Acids Res. , vol.36 , pp. D440-D444
    • Consortium, T.G.O.1
  • 48
    • 24644503098 scopus 로고    scopus 로고
    • Blast2GO: A universal tool for annotation, visualization, and analysis in functional genomics research
    • Conesa, A., Götz, S., García-Gómez, J. M., Terol, J., Talón, M., and Robles, M. (2005) Blast2GO: a universal tool for annotation, visualization, and analysis in functional genomics research. Bioinformatics 21, 3674-3676
    • (2005) Bioinformatics , vol.21 , pp. 3674-3676
    • Conesa, A.1    Götz, S.2    García-Gómez, J.M.3    Terol, J.4    Talón, M.5    Robles, M.6
  • 52
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann, M., Ong, S. E., Gronborg, M., Steen, H., Jensen, O. N., and Pandey, A. (2002) Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 20, 261-268
    • (2002) Trends Biotechnol. , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 53
    • 0034651752 scopus 로고    scopus 로고
    • Protein phosphorylation and protein phosphatases. de Panne, Belgium, September 19-24, 1999
    • Zolnierowicz, S., and Bollen, M. (2000) Protein phosphorylation and protein phosphatases. De Panne, Belgium, September 19-24, 1999. The EMBO J. 19, 483-488
    • (2000) The EMBO J. , vol.19 , pp. 483-488
    • Zolnierowicz, S.1    Bollen, M.2
  • 55
    • 77956630634 scopus 로고    scopus 로고
    • Chapter 13-Analysis of the Central Pair Microtubule Complex in Chlamydomonas reinhardtii
    • Stephen, M. K., and Gregory, J. P., eds. Academic Press
    • Mitchell, D. R., and Smith, B. (2009) Chapter 13-Analysis of the Central Pair Microtubule Complex in Chlamydomonas reinhardtii. In: Stephen, M. K., and Gregory, J. P., eds. Methods in Cell Biology, pp. 197-213, Academic Press
    • (2009) Methods in Cell Biology , pp. 197-213
    • Mitchell, D.R.1    Smith, B.2
  • 56
    • 84882908168 scopus 로고    scopus 로고
    • Axonemal dyneins: Assembly, structure, and force generation
    • King, S. M., and Kamiya, R. (2009) Axonemal dyneins: assembly, structure, and force generation. The Chlamydomonas Sourcebook 3, 131-208
    • (2009) The Chlamydomonas Sourcebook , vol.3 , pp. 131-208
    • King, S.M.1    Kamiya, R.2
  • 57
    • 0034677929 scopus 로고    scopus 로고
    • The dynein microtubule motor
    • King, S. M. (2000) The dynein microtubule motor. Biochim. Biophys. Acta 1496, 60-75
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 60-75
    • King, S.M.1
  • 58
    • 67749114279 scopus 로고    scopus 로고
    • An outer arm dynein light chain acts in a conformational switch for flagellar motility
    • Patel-King, R. S., and King, S. M. (2009) An outer arm dynein light chain acts in a conformational switch for flagellar motility. J. Cell Biol. 186, 283-295
    • (2009) J. Cell Biol. , vol.186 , pp. 283-295
    • Patel-King, R.S.1    King, S.M.2
  • 59
    • 84860316583 scopus 로고    scopus 로고
    • Outer dynein arm light chain 1 is essential for controlling the ciliary response to cyclic AMP in Paramecium tetraurelia
    • Kutomi, O., Hori, M., Ishida, M., Tominaga, T., Kamachi, H., Koll, F., Cohen, J., Yamada, N., and Noguchi, M. (2012) Outer dynein arm light chain 1 is essential for controlling the ciliary response to cyclic AMP in Paramecium tetraurelia. Eukaryot. Cell 11, 645-653
    • (2012) Eukaryot. Cell , vol.11 , pp. 645-653
    • Kutomi, O.1    Hori, M.2    Ishida, M.3    Tominaga, T.4    Kamachi, H.5    Koll, F.6    Cohen, J.7    Yamada, N.8    Noguchi, M.9
  • 60
    • 0019365126 scopus 로고
    • Radial spokes of Chlamydomonas flagella: Polypeptide composition and phosphorylation of stalk components
    • Piperno, G., Huang, B., Ramanis, Z., and Luck, D. J. (1981) Radial spokes of Chlamydomonas flagella: polypeptide composition and phosphorylation of stalk components. J. Cell Biol. 88, 73-79
    • (1981) J. Cell Biol. , vol.88 , pp. 73-79
    • Piperno, G.1    Huang, B.2    Ramanis, Z.3    Luck, D.J.4
  • 61
    • 0027436318 scopus 로고
    • Assembly of flagellar radial spoke proteins in Chlamydomonas: Identification of the axoneme binding domain of radial spoke protein 1
    • Diener, D. R., Ang, L. H., and Rosenbaum, J. L. (1993) Assembly of flagellar radial spoke proteins in Chlamydomonas: identification of the axoneme binding domain of radial spoke protein 1. J. Cell Biol. 123, 183-190
    • (1993) J. Cell Biol. , vol.123 , pp. 183-190
    • Diener, D.R.1    Ang, L.H.2    Rosenbaum, J.L.3
  • 62
    • 38349000827 scopus 로고    scopus 로고
    • Intraflagellar transport motors in cilia: Moving along the cell's antenna
    • Scholey, J. M. (2008) Intraflagellar transport motors in cilia: moving along the cell's antenna. J. Cell Biol. 180, 23-29
    • (2008) J. Cell Biol. , vol.180 , pp. 23-29
    • Scholey, J.M.1
  • 63
    • 63849291991 scopus 로고    scopus 로고
    • A microtubule depolymerizing kinesin functions during both flagellar disassembly and flagellar assembly in Chlamydomonas
    • Piao, T., Luo, M., Wang, L., Guo, Y., Li, D., Li, P., Snell, W. J., and Pan, J. (2009) A microtubule depolymerizing kinesin functions during both flagellar disassembly and flagellar assembly in Chlamydomonas. Proc. Natl. Acad. Sci. 106, 4713-4718
    • (2009) Proc. Natl. Acad. Sci. , vol.106 , pp. 4713-4718
    • Piao, T.1    Luo, M.2    Wang, L.3    Guo, Y.4    Li, D.5    Li, P.6    Snell, W.J.7    Pan, J.8
  • 64
    • 33847413590 scopus 로고    scopus 로고
    • Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella
    • Hou, Y., Qin, H., Follit, J. A., Pazour, G. J., Rosenbaum, J. L., and Witman, G. B. (2007) Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella. J. Cell Biol. 176, 653-665
    • (2007) J. Cell Biol. , vol.176 , pp. 653-665
    • Hou, Y.1    Qin, H.2    Follit, J.A.3    Pazour, G.J.4    Rosenbaum, J.L.5    Witman, G.B.6
  • 65
    • 23044441462 scopus 로고    scopus 로고
    • Characterization of the intraflagellar transport complex B core: Direct interaction of the IFT81 and IFT74/72 subunits
    • Lucker, B. F., Behal, R. H., Qin, H., Siron, L. C., Taggart, W. D., Rosenbaum, J. L., and Cole, D. G. (2005) Characterization of the intraflagellar transport complex B core: direct interaction of the IFT81 and IFT74/72 subunits. J. Biol. Chem. 280, 27688-27696
    • (2005) J. Biol. Chem. , vol.280 , pp. 27688-27696
    • Lucker, B.F.1    Behal, R.H.2    Qin, H.3    Siron, L.C.4    Taggart, W.D.5    Rosenbaum, J.L.6    Cole, D.G.7
  • 66
    • 0037744859 scopus 로고    scopus 로고
    • The intraflagellar transport machinery of Chlamydomonas reinhardtii
    • Cole, D. G. (2003) The intraflagellar transport machinery of Chlamydomonas reinhardtii. Traffic 4, 435-442
    • (2003) Traffic , vol.4 , pp. 435-442
    • Cole, D.G.1
  • 67
    • 4644274566 scopus 로고    scopus 로고
    • A dynein light intermediate chain, D1bLIC, is required for retrograde intraflagellar transport
    • Hou, Y., Pazour, G. J., and Witman, G. B. (2004) A dynein light intermediate chain, D1bLIC, is required for retrograde intraflagellar transport. Mol. Biol. Cell 15, 4382-4394
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4382-4394
    • Hou, Y.1    Pazour, G.J.2    Witman, G.B.3
  • 68
    • 0037810853 scopus 로고    scopus 로고
    • A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product
    • Rupp, G., and Porter, M. E. (2003) A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest-specific gene product. J. Cell Biol. 162, 47-57
    • (2003) J. Cell Biol. , vol.162 , pp. 47-57
    • Rupp, G.1    Porter, M.E.2
  • 69
    • 33749528009 scopus 로고    scopus 로고
    • Trypanin, a component of the flagellar dynein regulatory complex, is essential in bloodstream form african trypanosomes
    • Ralston, K. S., and Hill, K. L. (2006) Trypanin, a component of the flagellar dynein regulatory complex, is essential in bloodstream form african trypanosomes. PLoS Pathog. 2, e101
    • (2006) PLoS Pathog. , vol.2 , pp. e101
    • Ralston, K.S.1    Hill, K.L.2
  • 70
    • 58149352343 scopus 로고    scopus 로고
    • The dynein regulatory complex is required for ciliary motility and otolith biogenesis in the inner ear
    • Colantonio, J. R., Vermot, J., Wu, D., Langenbacher, A. D., Fraser, S., Chen, J.-N., and Hill, K. L. (2009) The dynein regulatory complex is required for ciliary motility and otolith biogenesis in the inner ear. Nature 457, 205-209
    • (2009) Nature , vol.457 , pp. 205-209
    • Colantonio, J.R.1    Vermot, J.2    Wu, D.3    Langenbacher, A.D.4    Fraser, S.5    Chen, J.-N.6    Hill, K.L.7
  • 71
    • 0026584179 scopus 로고
    • Calcium-regulated phosphorylation of proteins in the membrane-matrix compartment of the Chlamydomonas flagellum
    • Bloodgood, R. A. (1992) Calcium-regulated phosphorylation of proteins in the membrane-matrix compartment of the Chlamydomonas flagellum. Exp. Cell Res. 198, 228-236
    • (1992) Exp. Cell Res. , vol.198 , pp. 228-236
    • Bloodgood, R.A.1
  • 72
    • 84880848290 scopus 로고    scopus 로고
    • Regulation of flagellar biogenesis by a calcium dependent protein kinase in Chlamydomonas reinhardtii
    • Liang, Y., and Pan, J. (2013) Regulation of flagellar biogenesis by a calcium dependent protein kinase in Chlamydomonas reinhardtii. Plos One 8, e69902
    • (2013) Plos One , vol.8 , pp. e69902
    • Liang, Y.1    Pan, J.2
  • 73
    • 3342954733 scopus 로고    scopus 로고
    • Localization of the blue-light receptor phototropin to the flagella of the green alga Chlamydomonas reinhardtii
    • Huang, K., Kunkel, T., and Beck, C. F. (2004) Localization of the blue-light receptor phototropin to the flagella of the green alga Chlamydomonas reinhardtii. Mol. Biol. Cell 15, 3605-3614
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3605-3614
    • Huang, K.1    Kunkel, T.2    Beck, C.F.3
  • 74
    • 0033967129 scopus 로고    scopus 로고
    • Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme
    • Yang, P., Fox, L., Colbran, R. J., and Sale, W. S. (2000) Protein phosphatases PP1 and PP2A are located in distinct positions in the Chlamydomonas flagellar axoneme. J. Cell Sci. 113, 91-102
    • (2000) J. Cell Sci. , vol.113 , pp. 91-102
    • Yang, P.1    Fox, L.2    Colbran, R.J.3    Sale, W.S.4
  • 75
    • 0028988014 scopus 로고
    • A Post-translational modification of the photosystem II subunit CP29 protects maize from cold stress
    • Bergantino, E., Dainese, P., Cerovic, Z., Sechi, S., and Bassi, R. (1995) A Post-translational modification of the photosystem II subunit CP29 protects maize from cold stress. J. Biol. Chem. 270, 8474-8481
    • (1995) J. Biol. Chem. , vol.270 , pp. 8474-8481
    • Bergantino, E.1    Dainese, P.2    Cerovic, Z.3    Sechi, S.4    Bassi, R.5
  • 76
    • 65549147263 scopus 로고    scopus 로고
    • CP29, a monomeric lightharvesting complex II protein, is essential for state transitions in Chlamydomonas reinhardtii
    • Tokutsu, R., Iwai, M., and Minagawa, J. (2009) CP29, a monomeric lightharvesting complex II protein, is essential for state transitions in Chlamydomonas reinhardtii. J. Biol. Chem. 284, 7777-7782
    • (2009) J. Biol. Chem. , vol.284 , pp. 7777-7782
    • Tokutsu, R.1    Iwai, M.2    Minagawa, J.3
  • 77
    • 0037423885 scopus 로고    scopus 로고
    • Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas
    • Depège, N., Bellafiore, S., and Rochaix, J.-D. (2003) Role of chloroplast protein kinase Stt7 in LHCII phosphorylation and state transition in Chlamydomonas. Science 299, 1572-1575
    • (2003) Science , vol.299 , pp. 1572-1575
    • Depège, N.1    Bellafiore, S.2    Rochaix, J.-D.3
  • 78
    • 14544282417 scopus 로고    scopus 로고
    • State transitions and light adaptation require chloroplast thylakoid protein kinase STN7
    • Bellafiore, S., Barneche, F., Peltier, G., and Rochaix, J.-D. (2005) State transitions and light adaptation require chloroplast thylakoid protein kinase STN7. Nature 433, 892-895
    • (2005) Nature , vol.433 , pp. 892-895
    • Bellafiore, S.1    Barneche, F.2    Peltier, G.3    Rochaix, J.-D.4
  • 79
    • 75749085797 scopus 로고    scopus 로고
    • Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow
    • Pribil, M., Pesaresi, P., Hertle, A., Barbato, R., and Leister, D. (2010) Role of plastid protein phosphatase TAP38 in LHCII dephosphorylation and thylakoid electron flow. Plos Biol. 8, e1000288
    • (2010) Plos Biol. , vol.8 , pp. e1000288
    • Pribil, M.1    Pesaresi, P.2    Hertle, A.3    Barbato, R.4    Leister, D.5
  • 80
    • 79958147357 scopus 로고    scopus 로고
    • Dynamics of reversible protein phosphorylation in thylakoids of flowering plants: The roles of STN7, STN8 and TAP38
    • Pesaresi, P., Pribil, M., Wunder, T., and Leister, D. (2011) Dynamics of reversible protein phosphorylation in thylakoids of flowering plants: the roles of STN7, STN8 and TAP38. Biochim. Biophys. Acta 1807, 887-896
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 887-896
    • Pesaresi, P.1    Pribil, M.2    Wunder, T.3    Leister, D.4
  • 81
    • 0024195969 scopus 로고
    • The role of cyclic AMP in rapid and long-term regulation of gluconeogenesis and glycolysis
    • Pilkis, S. J., Claus, T. H., and el-Maghrabi, M. R. (1988) The role of cyclic AMP in rapid and long-term regulation of gluconeogenesis and glycolysis. Adv. Sec. Mess. Phosph. 22, 175-191
    • (1988) Adv. Sec. Mess. Phosph. , vol.22 , pp. 175-191
    • Pilkis, S.J.1    Claus, T.H.2    El-Maghrabi, M.R.3
  • 83
    • 84874603489 scopus 로고    scopus 로고
    • "Round up the usual suspects": A comment on nonexistent plant G protein-coupled receptors
    • Urano, D., and Jones, A. M. (2013) "Round up the usual suspects": a comment on nonexistent plant G protein-coupled receptors. Plant Physiol. 161, 1097-1102
    • (2013) Plant Physiol. , vol.161 , pp. 1097-1102
    • Urano, D.1    Jones, A.M.2
  • 86
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, In vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 87
    • 33847782587 scopus 로고    scopus 로고
    • Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry
    • Molina, H., Horn, D. M., Tang, N., Mathivanan, S., and Pandey, A. (2007) Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 104, 2199-2204
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2199-2204
    • Molina, H.1    Horn, D.M.2    Tang, N.3    Mathivanan, S.4    Pandey, A.5
  • 88
    • 73249138597 scopus 로고    scopus 로고
    • Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes
    • Grimsrud, P. A., den Os, D., Wenger, C. D., Swaney, D. L., Schwartz, D., Sussman, M. R., Ané, J.-M., and Coon, J. J. (2010) Large-scale phosphoprotein analysis in Medicago truncatula roots provides insight into in vivo kinase activity in legumes. Plant Physiol. 152, 19-28
    • (2010) Plant Physiol. , vol.152 , pp. 19-28
    • Grimsrud, P.A.1    Den Os, D.2    Wenger, C.D.3    Swaney, D.L.4    Schwartz, D.5    Sussman, M.R.6    Ané, J.-M.7    Coon, J.J.8
  • 90
    • 82755163993 scopus 로고    scopus 로고
    • Multidimensional strategy for sensitive phosphoproteomics incorporating protein prefractionation combined with SIMAC, HILIC, and TiO2 chromatography applied to proximal EGF signaling
    • Engholm-Keller, K., Hansen, T. A., Palmisano, G., and Larsen, M. R. (2011) Multidimensional strategy for sensitive phosphoproteomics incorporating protein prefractionation combined with SIMAC, HILIC, and TiO2 chromatography applied to proximal EGF signaling. J. Proteome Res. 10, 5383-5397
    • (2011) J. Proteome Res. , vol.10 , pp. 5383-5397
    • Engholm-Keller, K.1    Hansen, T.A.2    Palmisano, G.3    Larsen, M.R.4
  • 92
    • 84863323068 scopus 로고    scopus 로고
    • Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues
    • Lundby, A., Secher, A., Lage, K., Nordsborg, N. B., Dmytriyev, A., Lundby, C., and Olsen, J. V. (2012) Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nat. Commun. 3, 876
    • (2012) Nat. Commun. , vol.3 , pp. 876
    • Lundby, A.1    Secher, A.2    Lage, K.3    Nordsborg, N.B.4    Dmytriyev, A.5    Lundby, C.6    Olsen, J.V.7
  • 93
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller, B., Mueller, L. N., Mueller, M., Domon, B., and Aebersold, R. (2007) Reproducible isolation of distinct, overlapping segments of the phosphoproteome. Nat. Methods 4, 231-237
    • (2007) Nat. Methods , vol.4 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 94
    • 25844479829 scopus 로고    scopus 로고
    • STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation of photosystem II core proteins
    • Vainonen, J. P., Hansson, M., and Vener, A. V. (2005) STN8 protein kinase in Arabidopsis thaliana is specific in phosphorylation of photosystem II core proteins. J. Biol. Chem. 280, 33679-33686
    • (2005) J. Biol. Chem. , vol.280 , pp. 33679-33686
    • Vainonen, J.P.1    Hansson, M.2    Vener, A.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.