메뉴 건너뛰기




Volumn 22, Issue 7, 2012, Pages 1155-1168

S-acylation-dependent association of the calcium sensor CBL2 with the vacuolar membrane is essential for proper abscisic acid responses

Author keywords

ABA; calcium; CBL; S acylation; vacuolar membrane

Indexed keywords

ABSCISIC ACID; ARABIDOPSIS PROTEIN; CALCIUM; CALCIUM BINDING PROTEIN; CBL2 PROTEIN, ARABIDOPSIS;

EID: 84863480170     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2012.71     Document Type: Article
Times cited : (89)

References (47)
  • 2
    • 0036269927 scopus 로고    scopus 로고
    • Calcium at the crossroads of signaling
    • Sanders D, Pelloux J, Brownlee C, Harper JF. Calcium at the crossroads of signaling. Plant Cell 2002; 14Suppl:S401-S417. (Pubitemid 34609250)
    • (2002) Plant Cell , vol.14 , Issue.SUPPL.
    • Sanders, D.1    Pelloux, J.2    Brownlee, C.3    Harper, J.F.4
  • 4
    • 0033388972 scopus 로고    scopus 로고
    • Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis
    • DOI 10.1105/tpc.11.12.2393
    • Shi J, Kim KN, Ritz O, et al. Novel protein kinases associated with calcineurin B-like calcium sensors in Arabidopsis. Plant Cell 1999; 11:2393-2405. (Pubitemid 30031383)
    • (1999) Plant Cell , vol.11 , Issue.12 , pp. 2393-2405
    • Shi, J.1    Kim, K.-N.2    Ritz, O.3    Albrecht, V.4    Gupta, R.5    Harter, K.6    Luan, S.7    Kudla, J.8
  • 5
    • 7044226261 scopus 로고    scopus 로고
    • Integration and channeling of calcium signalling through the CBL calcium sensor/CIPK protein kinase network
    • DOI 10.1007/s00425-004-1333-3
    • Batistic O, Kudla J. Integration and channeling of calcium signaling through the CBL calcium sensor/CIPK protein kinase network. Planta 2004; 219:915-924. (Pubitemid 39415378)
    • (2004) Planta , vol.219 , Issue.6 , pp. 915-924
    • Batistic, O.1    Kudla, J.2
  • 7
    • 70350125202 scopus 로고    scopus 로고
    • The cbl-cipk ca(2+)-decoding signaling network: Function and perspectives
    • Weinl S, Kudla J. The CBL-CIPK Ca(2+)-decoding signaling network: function and perspectives. New Phytol 2009; 184:517-528.
    • (2009) New Phytol , vol.184 , pp. 517-528
    • Weinl, S.1    Kudla, J.2
  • 8
    • 67349229820 scopus 로고    scopus 로고
    • Plant calcineurin b-like proteins and their interacting protein kinases
    • Batistic O, Kudla J. Plant calcineurin B-like proteins and their interacting protein kinases. Biochim Biophys Acta 2009; 1793:985-992.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 985-992
    • Batistic, O.1    Kudla, J.2
  • 9
    • 33745228053 scopus 로고    scopus 로고
    • + uptake
    • DOI 10.1016/j.cell.2006.06.017, PII S0092867406007756
    • Hedrich R, Kudla J. Calcium signaling networks channel plant K+ uptake. Cell 2006; 125:1221-1223. (Pubitemid 43929102)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1221-1223
    • Hedrich, R.1    Kudla, J.2
  • 10
    • 77953184082 scopus 로고    scopus 로고
    • Calcium signals: The lead currency of plant information processing
    • Kudla J, Batistic O, Hashimoto K. Calcium signals: the lead currency of plant information processing. Plant Cell 2010; 22:541-563.
    • (2010) Plant Cell , vol.22 , pp. 541-563
    • Kudla, J.1    Batistic, O.2    Hashimoto, K.3
  • 11
    • 33745251949 scopus 로고    scopus 로고
    • + transporter AKT1 in arabidopsis
    • DOI 10.1016/j.cell.2006.06.011, PII S0092867406007690
    • Xu J, Li HD, Chen LQ, et al. A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell 2006; 125:1347-1360. (Pubitemid 43929097)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1347-1360
    • Xu, J.1    Li, H.-D.2    Chen, L.-Q.3    Wang, Y.4    Liu, L.-L.5    He, L.6    Wu, W.-H.7
  • 12
    • 35148841967 scopus 로고    scopus 로고
    • Two calcineurin B-like calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis
    • DOI 10.1111/j.1365-313X.2007.03236.x
    • Cheong YH, Pandey GK, Grant JJ, et al. Two calcineurin Blike calcium sensors, interacting with protein kinase CIPK23, regulate leaf transpiration and root potassium uptake in Arabidopsis. Plant J 2007; 52:223-239. (Pubitemid 47537582)
    • (2007) Plant Journal , vol.52 , Issue.2 , pp. 223-239
    • Cheong, Y.H.1    Pandey, G.K.2    Grant, J.J.3    Batistic, O.4    Li, L.5    Kim, B.-G.6    Lee, S.-C.7    Kudla, J.8    Luan, S.9
  • 14
    • 0031444350 scopus 로고    scopus 로고
    • Abscisic acid signaling through cyclic ADP-ribose in plants
    • DOI 10.1126/science.278.5346.2126
    • Wu Y, Kuzma J, Marechal E, et al. Abscisic acid signaling through cyclic ADP-ribose in plants. Science 1997; 278:2126-2130. (Pubitemid 28028323)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2126-2130
    • Wu, Y.1    Kuzma, J.2    Marechal, E.3    Graeff, R.4    Lee, H.C.5    Foster, R.6    Chua, N.-H.7
  • 15
    • 0034710888 scopus 로고    scopus 로고
    • Aba activates multiple ca(2+) fluxes in stomatal guard cells, triggering vacuolar k(+)(rb(+)) release
    • MacRobbie EA. ABA activates multiple Ca(2+) fluxes in stomatal guard cells, triggering vacuolar K(+)(Rb(+)) release. Proc Natl Acad Sci USA 2000; 97:12361-12368.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12361-12368
    • MacRobbie, E.A.1
  • 16
    • 73849141867 scopus 로고    scopus 로고
    • Cbl-mediated targeting of cipks facilitates the decoding of calcium signals emanating from distinct cellular stores
    • Batistic O, Waadt R, Steinhorst L, Held K, Kudla J. CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores. Plant J 2010; 61:211-222.
    • (2010) Plant J , vol.61 , pp. 211-222
    • Batistic, O.1    Waadt, R.2    Steinhorst, L.3    Held, K.4    Kudla, J.5
  • 17
    • 51549089239 scopus 로고    scopus 로고
    • 21 signaling complexes in Arabidopsis
    • DOI 10.1105/tpc.108.058123
    • Batistic O, Sorek N, Schultke S, Yalovsky S, Kudla J. Dual fatty acyl modification determines the localization and plasma membrane targeting of CBL/CIPK Ca2+ signaling complexes in Arabidopsis. Plant Cell 2008; 20:1346-1362. (Pubitemid 352844187)
    • (2008) Plant Cell , vol.20 , Issue.5 , pp. 1346-1362
    • Batistic, O.1    Sorek, N.2    Schultke, S.3    Yalovsky, S.4    Kudla, J.5
  • 18
    • 78650718836 scopus 로고    scopus 로고
    • The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins. Cell 2010; 141:458-471. 19 salaun c, greaves j, chamberlain lh. The intracellular dynamic of protein palmitoylation
    • Rocks O, Gerauer M, Vartak N, et al. The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins. Cell 2010; 141:458-471. 19 Salaun C, Greaves J, Chamberlain LH. The intracellular dynamic of protein palmitoylation. J Cell Biol 2010; 191:1229-1238.
    • (2010) J Cell Biol , vol.191 , pp. 1229-1238
    • Rocks, O.1    Gerauer, M.2    Vartak, N.3
  • 20
    • 61449189902 scopus 로고    scopus 로고
    • Palmitoyl acyltransferases, their substrates, and novel assays to connect them (review)
    • Planey SL, Zacharias DA. Palmitoyl acyltransferases, their substrates, and novel assays to connect them (Review). Mol Membr Biol 2009; 26:14-31.
    • (2009) Mol Membr Biol , vol.26 , pp. 14-31
    • Planey, S.L.1    Zacharias, D.A.2
  • 21
    • 54249148026 scopus 로고    scopus 로고
    • Css-palm 2.0: An updated software for palmitoylation sites prediction
    • Ren J, Wen L, Gao X, Jin C, Xue Y, Yao X. CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng Des Sel 2008; 21:639-644.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5    Yao, X.6
  • 22
    • 30944443590 scopus 로고    scopus 로고
    • Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis
    • DOI 10.1083/jcb.200507067
    • Abrami L, Leppla SH, van der Goot FG. Receptor palmitoylation and ubiquitination regulate anthrax toxin endocytosis. J Cell Biol 2006; 172:309-320. (Pubitemid 43112976)
    • (2006) Journal of Cell Biology , vol.172 , Issue.2 , pp. 309-320
    • Abrami, L.1    Leppla, S.H.2    Van Der Goot, F.3
  • 23
    • 33750630572 scopus 로고    scopus 로고
    • Nba-palm: Prediction of palmitoylation site implemented in na?ve bayes algorithm
    • Xue Y, Chen H, Jin C, Sun Z, Yao X. NBA-Palm: prediction of palmitoylation site implemented in Na?ve Bayes algorithm. BMC Bioinformatics 2006; 7:458.
    • (2006) BMC Bioinformatics , vol.7 , pp. 458
    • Xue, Y.1    Chen, H.2    Jin, C.3    Sun, Z.4    Yao, X.5
  • 24
    • 77950838149 scopus 로고    scopus 로고
    • Analysis of protein s-acylation by gas chromatography-coupled mass spectrometry using purified proteins
    • Sorek N, Yalovsky S. Analysis of protein S-acylation by gas chromatography-coupled mass spectrometry using purified proteins. Nat Protoc 2010; 5:834-840.
    • (2010) Nat Protoc , vol.5 , pp. 834-840
    • Sorek, N.1    Yalovsky, S.2
  • 25
    • 33947266606 scopus 로고    scopus 로고
    • Activation status-coupled transient S acylation determines membrane partitioning of a plant Rho-related GTPase
    • DOI 10.1128/MCB.02347-06
    • Sorek N, Poraty L, Sternberg H, Bar E, Lewinsohn E, Yalovsky S. Activation status-coupled transient S acylation determines membrane partitioning of a plant Rho-related GTPase. Mol Cell Biol 2007; 27:2144-2154. (Pubitemid 46418471)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.6 , pp. 2144-2154
    • Sorek, N.1    Poraty, L.2    Sternberg, H.3    Bar, E.4    Lewinsohn, E.5    Yalovsky, S.6
  • 27
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • DOI 10.1105/tpc.000620
    • Brandizzi F, Frangne N, Marc-Martin S, Hawes C, Neuhaus JM, Paris N. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002; 14:1077-1092. (Pubitemid 34609218)
    • (2002) Plant Cell , vol.14 , Issue.5 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.-M.5    Paris, N.6
  • 29
    • 0842328861 scopus 로고    scopus 로고
    • Calcium sensors and their interacting protein kinases: Genomics of the arabidopsis and rice CBL-CIPK signaling networks
    • DOI 10.1104/pp.103.033068
    • Kolukisaoglu U, Weinl S, Blazevic D, Batistic O, Kudla J. Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks. Plant Physiol 2004; 134:43-58. (Pubitemid 38178679)
    • (2004) Plant Physiology , vol.134 , Issue.1 , pp. 43-58
    • Kolukisaoglu, U.1    Weinl, S.2    Blazevic, D.3    Batistic, O.4    Kudla, J.5
  • 32
    • 78049511240 scopus 로고    scopus 로고
    • Palmitoylationdependent association with cd63 targets the ca2+ sensor synaptotagmin vii to lysosomes
    • Flannery AR, Czibener C, Andrews NW. Palmitoylationdependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes. J Cell Biol 2010; 191:599-613.
    • (2010) J Cell Biol , vol.191 , pp. 599-613
    • Flannery, A.R.1    Czibener, C.2    Andrews, N.W.3
  • 33
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • DOI 10.1016/S0962-8924(02)00008-9, PII S0962892402000089
    • Bijlmakers MJ, Marsh M. The on-off story of protein palmitoylation. Trends Cell Biol 2003; 13:32-42. (Pubitemid 35453893)
    • (2003) Trends in Cell Biology , vol.13 , Issue.1 , pp. 32-42
    • Bijlmakers, M.-J.1    Marsh, M.2
  • 35
    • 0036007915 scopus 로고    scopus 로고
    • Uptake of a fluorescent marker in plant cells is sensitive to brefeldin a and wortmannin
    • DOI 10.1105/tpc.010339
    • Emans N, Zimmermann S, Fischer R. Uptake of a fluorescent marker in plant cells is sensitive to brefeldin A and wortmannin. Plant Cell 2002; 14:71-86. (Pubitemid 34140399)
    • (2002) Plant Cell , vol.14 , Issue.1 , pp. 71-86
    • Emans, N.1    Zimmermann, S.2    Fischer, R.3
  • 36
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka K, Bassham DC, Raikhel NV, Nakamura K. Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J Cell Biol 1995; 130:1307-1318.
    • (1995) J Cell Biol , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 37
    • 54049132555 scopus 로고    scopus 로고
    • Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein
    • Greaves J, Salaun C, Fukata Y, Fukata M, Chamberlain LH. Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein. J Biol Chem 2008; 283:25014-25026.
    • (2008) J Biol Chem , vol.283 , pp. 25014-25026
    • Greaves, J.1    Salaun, C.2    Fukata, Y.3    Fukata, M.4    Chamberlain, L.H.5
  • 38
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • DOI 10.1016/j.bbalip.2006.03.010, PII S1388198106000709
    • Ohno Y, Kihara A, Sano T, Igarashi Y. Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins. Biochim Biophys Acta 2006; 1761:474-483. (Pubitemid 43776463)
    • (2006) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1761 , Issue.4 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 39
    • 25444491476 scopus 로고    scopus 로고
    • The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p
    • DOI 10.1083/jcb.200507048
    • Smotrys JE, Schoenfish MJ, Stutz MA, Linder ME. The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p. J Cell Biol 2005; 170:1091-1099. (Pubitemid 41362641)
    • (2005) Journal of Cell Biology , vol.170 , Issue.7 , pp. 1091-1099
    • Smotrys, J.E.1    Schoenfish, M.J.2    Stutz, M.A.3    Linder, M.E.4
  • 41
    • 67650540764 scopus 로고    scopus 로고
    • Molecular recognition of the palmitoylation substrate vac8 by its palmitoyltransferase pfa3
    • Nadolski MJ, Linder ME. Molecular recognition of the palmitoylation substrate Vac8 by its palmitoyltransferase Pfa3. J Biol Chem 2009; 284:17720-17730.
    • (2009) J Biol Chem , vol.284 , pp. 17720-17730
    • Nadolski, M.J.1    Linder, M.E.2
  • 43
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels DJ, Mitchell DA, Dong X, Deschenes RJ. Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol Cell Biol 1999; 19:6775-6787. (Pubitemid 29441861)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.10 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 44
    • 67649882018 scopus 로고    scopus 로고
    • Analysis of dhhc acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism
    • Hou H, John Peter AT, Meiringer C, Subramanian K, Ungermann C. Analysis of DHHC acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism. Traffic 2009; 10:1061-1073.
    • (2009) Traffic , vol.10 , pp. 1061-1073
    • Hou, H.1    John Peter, A.T.2    Meiringer, C.3    Subramanian, K.4    Ungermann, C.5
  • 46
    • 44949161848 scopus 로고    scopus 로고
    • In planta visualization of protein interactions using bimolecular fluorescence complementation (bifc)
    • doi:10.1101/pdb.prot4995pdb.prot4995
    • Waadt R, Kudla J. In Planta visualization of protein interactions using bimolecular fluorescence complementation (BiFC). CSH Protocols 2008; 2008:pdb.prot4995. doi:10.1101/pdb. prot4995
    • (2008) CSH Protocols , vol.2008
    • Waadt, R.1    Kudla, J.2
  • 47
    • 69449106537 scopus 로고    scopus 로고
    • Optimization of conditions for transient agrobacterium-mediated gene expression assays in arabidopsis
    • Kim MJ, Baek K, Park CM. Optimization of conditions for transient Agrobacterium-mediated gene expression assays in Arabidopsis. Plant Cell Rep 2009; 28:1159-1167.
    • (2009) Plant Cell Rep , vol.28 , pp. 1159-1167
    • Kim, M.J.1    Baek, K.2    Park, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.