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Volumn 76, Issue 2, 2013, Pages 287-296

Phosphorylation of S344 in the calmodulin-binding domain negatively affects CCaMK function during bacterial and fungal symbioses

Author keywords

arbuscular mycorrhizal symbiosis; autophosphorylation; calcium and Ca2+ calmodulin dependent protein kinase; calcium signaling; calmodulin binding domain; Medicago truncatula; protein kinase; root nodule symbiosis

Indexed keywords

ARBUSCULAR MYCORRHIZAL SYMBIOSIS; AUTOPHOSPHORYLATION; CALCIUM SIGNALING; CALMODULIN BINDING DOMAIN; MEDICAGO TRUNCATULA; PROTEIN KINASE; ROOT NODULES;

EID: 84885325783     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12288     Document Type: Article
Times cited : (25)

References (40)
  • 1
    • 56449127013 scopus 로고    scopus 로고
    • Divergence of evolutionary ways among common sym genes: CASTOR and CCaMK show functional conservation between two symbiosis systems and constitute the root of a common signaling pathway
    • Banba, M., Gutjahr, C., Miyao, A., Hirochika, H., Paszkowski, U., Kouchi, H., and, Imaizumi-Anraku, H., (2008) Divergence of evolutionary ways among common sym genes: CASTOR and CCaMK show functional conservation between two symbiosis systems and constitute the root of a common signaling pathway. Plant Cell Physiol. 49, 1659-1671.
    • (2008) Plant Cell Physiol. , vol.49 , pp. 1659-1671
    • Banba, M.1    Gutjahr, C.2    Miyao, A.3    Hirochika, H.4    Paszkowski, U.5    Kouchi, H.6    Imaizumi-Anraku, H.7
  • 2
    • 0034998287 scopus 로고    scopus 로고
    • Agrobacterium rhizogenes-transformed roots of Medicago truncatula for the study of nitrogen-fixing and endomycorrhizal symbiotic associations
    • Boisson-Dernier, A., Chabaud, M., Garcia, F., Becard, G., Rosenberg, C., and, Barker, D.G., (2001) Agrobacterium rhizogenes-transformed roots of Medicago truncatula for the study of nitrogen-fixing and endomycorrhizal symbiotic associations. Mol. Plant-Microbe Interact. 14, 695-700.
    • (2001) Mol. Plant-Microbe Interact. , vol.14 , pp. 695-700
    • Boisson-Dernier, A.1    Chabaud, M.2    Garcia, F.3    Becard, G.4    Rosenberg, C.5    Barker, D.G.6
  • 3
    • 52649106035 scopus 로고    scopus 로고
    • OsIPD3, an ortholog of the Medicago truncatula DMI3 interacting protein IPD3, is required for mycorrhizal symbiosis in rice
    • Chen, C., Ane, J.M., and, Zhu, H., (2008) OsIPD3, an ortholog of the Medicago truncatula DMI3 interacting protein IPD3, is required for mycorrhizal symbiosis in rice. New Phytol. 180, 311-315.
    • (2008) New Phytol. , vol.180 , pp. 311-315
    • Chen, C.1    Ane, J.M.2    Zhu, H.3
  • 4
    • 0025301783 scopus 로고
    • Calcium/calmodulin-independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. Studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides
    • Colbran, R.J., and, Soderling, T.R., (1990) Calcium/calmodulin- independent autophosphorylation sites of calcium/calmodulin-dependent protein kinase II. Studies on the effect of phosphorylation of threonine 305/306 and serine 314 on calmodulin binding using synthetic peptides. J. Biol. Chem. 265, 11213-11219.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11213-11219
    • Colbran, R.J.1    Soderling, T.R.2
  • 6
    • 4444325076 scopus 로고    scopus 로고
    • 2+/calmodulin-binding proteins involved in transcriptional regulation: Interaction with fsh/Ring3 class transcription activators
    • 2+/calmodulin-binding proteins involved in transcriptional regulation: interaction with fsh/Ring3 class transcription activators. Plant Mol. Biol. 54, 549-569.
    • (2004) Plant Mol. Biol. , vol.54 , pp. 549-569
    • Du, L.1    Poovaiah, B.W.2
  • 7
    • 0029895156 scopus 로고    scopus 로고
    • Calcium spiking in plant root hairs responding to Rhizobium nodulation signals
    • Ehrhardt, D.W., Wais, R., and, Long, S.R., (1996) Calcium spiking in plant root hairs responding to Rhizobium nodulation signals. Cell, 85, 673-681.
    • (1996) Cell , vol.85 , pp. 673-681
    • Ehrhardt, D.W.1    Wais, R.2    Long, S.R.3
  • 8
    • 33745621580 scopus 로고    scopus 로고
    • Nodulation independent of rhizobia induced by a calcium-activated kinase lacking autoinhibition
    • Gleason, C., Chaudhuri, S., Yang, T., Munoz, A., Poovaiah, B.W., and, Oldroyd, G.E., (2006) Nodulation independent of rhizobia induced by a calcium-activated kinase lacking autoinhibition. Nature, 441, 1149-1152.
    • (2006) Nature , vol.441 , pp. 1149-1152
    • Gleason, C.1    Chaudhuri, S.2    Yang, T.3    Munoz, A.4    Poovaiah, B.W.5    Oldroyd, G.E.6
  • 9
    • 33646355940 scopus 로고    scopus 로고
    • A rice calcium- and calmodulin-dependent protein kinase restores nodulation to a legume mutant
    • Godfroy, O., Debelle, F., Timmers, T., and, Rosenberg, C., (2006) A rice calcium- and calmodulin-dependent protein kinase restores nodulation to a legume mutant. Mol. Plant-Microbe Interact. 19, 495-501.
    • (2006) Mol. Plant-Microbe Interact. , vol.19 , pp. 495-501
    • Godfroy, O.1    Debelle, F.2    Timmers, T.3    Rosenberg, C.4
  • 10
    • 0026806967 scopus 로고
    • 2+/ calmodulin-dependent protein kinase analyzed by site-directed mutagenesis
    • 2+/calmodulin-dependent protein kinase analyzed by site-directed mutagenesis. J. Biol. Chem. 267, 17216-17224.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17216-17224
    • Hanson, P.I.1    Schulman, H.2
  • 11
    • 84870506564 scopus 로고    scopus 로고
    • Cellular programs for arbuscular mycorrhizal symbiosis
    • Harrison, M.J., (2012) Cellular programs for arbuscular mycorrhizal symbiosis. Curr. Opin. Plant Biol. 15, 691-698.
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 691-698
    • Harrison, M.J.1
  • 12
    • 80054738908 scopus 로고    scopus 로고
    • Medicago truncatula IPD3 is a member of the common symbiotic signaling pathway required for rhizobial and mycorrhizal symbioses
    • Horvath, B., Yeun, L.H., and, Domonkos, A., et al. (2011) Medicago truncatula IPD3 is a member of the common symbiotic signaling pathway required for rhizobial and mycorrhizal symbioses. Mol. Plant-Microbe Interact. 24, 1345-1358.
    • (2011) Mol. Plant-Microbe Interact. , vol.24 , pp. 1345-1358
    • Horvath, B.1    Yeun, L.H.2    Domonkos, A.3
  • 15
    • 8844258388 scopus 로고    scopus 로고
    • 2+ and calmodulin-dependent protein kinase required for bacterial and fungal symbioses
    • 2+ and calmodulin-dependent protein kinase required for bacterial and fungal symbioses. Science, 303, 1361-1364.
    • (2004) Science , vol.303 , pp. 1361-1364
    • Levy, J.1    Bres, C.2    Geurts, R.3
  • 16
    • 84868479703 scopus 로고    scopus 로고
    • Negative regulation of CCaMK is essential for symbiotic infection
    • Liao, J., Singh, S., and, Hossain, M.S., et al. (2012) Negative regulation of CCaMK is essential for symbiotic infection. Plant J. 72, 572-584.
    • (2012) Plant J. , vol.72 , pp. 572-584
    • Liao, J.1    Singh, S.2    Hossain, M.S.3
  • 17
    • 0032215639 scopus 로고    scopus 로고
    • Chimeric calcium/calmodulin-dependent protein kinase in tobacco: Differential regulation by calmodulin isoforms
    • Liu, Z., Xia, M., and, Poovaiah, B.W., (1998) Chimeric calcium/calmodulin-dependent protein kinase in tobacco: differential regulation by calmodulin isoforms. Plant Mol. Biol. 38, 889-897.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 889-897
    • Liu, Z.1    Xia, M.2    Poovaiah, B.W.3
  • 18
    • 84865504636 scopus 로고    scopus 로고
    • Nitric oxide-activated calcium/calmodulin-dependent protein kinase regulates the abscisic acid-induced antioxidant defence in maize
    • Ma, F., Lu, R., Liu, H., Shi, B., Zhang, J., Tan, M., Zhang, A., and, Jiang, M., (2012) Nitric oxide-activated calcium/calmodulin-dependent protein kinase regulates the abscisic acid-induced antioxidant defence in maize. J. Exp. Bot. 63, 4835-4847.
    • (2012) J. Exp. Bot. , vol.63 , pp. 4835-4847
    • Ma, F.1    Lu, R.2    Liu, H.3    Shi, B.4    Zhang, J.5    Tan, M.6    Zhang, A.7    Jiang, M.8
  • 19
    • 78650994503 scopus 로고    scopus 로고
    • Fungal lipochitooligosaccharide symbiotic signals in arbuscular mycorrhiza
    • Maillet, F., Poinsot, V., and, Andre, O., et al. (2011) Fungal lipochitooligosaccharide symbiotic signals in arbuscular mycorrhiza. Nature, 469, 58-63.
    • (2011) Nature , vol.469 , pp. 58-63
    • Maillet, F.1    Poinsot, V.2    Andre, O.3
  • 20
    • 34547111290 scopus 로고    scopus 로고
    • A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula
    • Messinese, E., Mun, J.H., and, Yeun, L.H., et al. (2007) A novel nuclear protein interacts with the symbiotic DMI3 calcium- and calmodulin-dependent protein kinase of Medicago truncatula. Mol. Plant-Microbe Interact. 20, 912-921.
    • (2007) Mol. Plant-Microbe Interact. , vol.20 , pp. 912-921
    • Messinese, E.1    Mun, J.H.2    Yeun, L.H.3
  • 22
    • 44649141367 scopus 로고    scopus 로고
    • Coordinating nodule morphogenesis with rhizobial infection in legumes
    • Oldroyd, G.E., and, Downie, J.A., (2008) Coordinating nodule morphogenesis with rhizobial infection in legumes. Annu. Rev. Plant Biol. 59, 519-546.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 519-546
    • Oldroyd, G.E.1    Downie, J.A.2
  • 23
  • 24
    • 80054735372 scopus 로고    scopus 로고
    • IPD3 controls the formation of nitrogen-fixing symbiosomes in pea and Medicago spp
    • Ovchinnikova, E., Journet, E.P., and, Chabaud, M., et al. (2011) IPD3 controls the formation of nitrogen-fixing symbiosomes in pea and Medicago spp. Mol. Plant-Microbe Interact. 24, 1333-1344.
    • (2011) Mol. Plant-Microbe Interact. , vol.24 , pp. 1333-1344
    • Ovchinnikova, E.1    Journet, E.P.2    Chabaud, M.3
  • 25
    • 0034937828 scopus 로고    scopus 로고
    • Zea mays CCaMK: Autophosphorylation-dependent substrate phosphorylation and down-regulation by red light
    • Pandey, S., and, Sopory, S.K., (2001) Zea mays CCaMK: autophosphorylation-dependent substrate phosphorylation and down-regulation by red light. J. Exp. Bot. 52, 691-700.
    • (2001) J. Exp. Bot. , vol.52 , pp. 691-700
    • Pandey, S.1    Sopory, S.K.2
  • 26
    • 0029065702 scopus 로고
    • Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain
    • Patil, S., Takezawa, D., and, Poovaiah, B.W., (1995) Chimeric plant calcium/calmodulin-dependent protein kinase gene with a neural visinin-like calcium-binding domain. Proc. Natl Acad. Sci. USA, 92, 4897-4901.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 4897-4901
    • Patil, S.1    Takezawa, D.2    Poovaiah, B.W.3
  • 28
    • 0142041483 scopus 로고    scopus 로고
    • Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases
    • Radutoiu, S., Madsen, L.H., and, Madsen, E.B., et al. (2003) Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases. Nature, 425, 585-592.
    • (2003) Nature , vol.425 , pp. 585-592
    • Radutoiu, S.1    Madsen, L.H.2    Madsen, E.B.3
  • 29
    • 0030981112 scopus 로고    scopus 로고
    • Functional domains of plant chimeric calcium/calmodulin-dependent protein kinase: Regulation by autoinhibitory and visinin-like domains
    • Ramachandiran, S., Takezawa, D., Wang, W., and, Poovaiah, B.W., (1997) Functional domains of plant chimeric calcium/calmodulin-dependent protein kinase: regulation by autoinhibitory and visinin-like domains. J. Biochem. 121, 984-990.
    • (1997) J. Biochem. , vol.121 , pp. 984-990
    • Ramachandiran, S.1    Takezawa, D.2    Wang, W.3    Poovaiah, B.W.4
  • 30
    • 34250660449 scopus 로고    scopus 로고
    • NUCLEOPORIN85 is required for calcium spiking, fungal and bacterial symbioses, and seed production in Lotus japonicus
    • Saito, K., Yoshikawa, M., and, Yano, K., et al. (2007) NUCLEOPORIN85 is required for calcium spiking, fungal and bacterial symbioses, and seed production in Lotus japonicus. Plant Cell, 19, 610-624.
    • (2007) Plant Cell , vol.19 , pp. 610-624
    • Saito, K.1    Yoshikawa, M.2    Yano, K.3
  • 31
    • 0034730245 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity
    • 2+/calmodulin-dependent protein kinase. Role of the neural visinin-like domain in regulating autophosphorylation and calmodulin affinity. J. Biol. Chem. 275, 30417-30422.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30417-30422
    • Sathyanarayanan, P.V.1    Cremo, C.R.2    Poovaiah, B.W.3
  • 32
    • 0035980012 scopus 로고    scopus 로고
    • Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase
    • Sathyanarayanan, P.V., Siems, W.F., Jones, J.P., and, Poovaiah, B.W., (2001) Calcium-stimulated autophosphorylation site of plant chimeric calcium/calmodulin-dependent protein kinase. J. Biol. Chem. 276, 32940-32947.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32940-32947
    • Sathyanarayanan, P.V.1    Siems, W.F.2    Jones, J.P.3    Poovaiah, B.W.4
  • 33
    • 0035283099 scopus 로고    scopus 로고
    • Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding
    • Shani, G., Henis-Korenblit, S., Jona, G., Gileadi, O., Eisenstein, M., Ziv, T., Admon, A., and, Kimchi, A., (2001) Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding. EMBO J. 20, 1099-1113.
    • (2001) EMBO J. , vol.20 , pp. 1099-1113
    • Shani, G.1    Henis-Korenblit, S.2    Jona, G.3    Gileadi, O.4    Eisenstein, M.5    Ziv, T.6    Admon, A.7    Kimchi, A.8
  • 34
    • 84857775647 scopus 로고    scopus 로고
    • Rhizobial and fungal symbioses show different requirements for calmodulin binding to calcium calmodulin-dependent protein kinase in Lotus japonicus
    • Shimoda, Y., Han, L., Yamazaki, T., Suzuki, R., Hayashi, M., and, Imaizumi-Anraku, H., (2012) Rhizobial and fungal symbioses show different requirements for calmodulin binding to calcium calmodulin-dependent protein kinase in Lotus japonicus. Plant Cell, 24, 304-321.
    • (2012) Plant Cell , vol.24 , pp. 304-321
    • Shimoda, Y.1    Han, L.2    Yamazaki, T.3    Suzuki, R.4    Hayashi, M.5    Imaizumi-Anraku, H.6
  • 36
    • 20544441300 scopus 로고    scopus 로고
    • NSP1 of the GRAS protein family is essential for rhizobial Nod factor-induced transcription
    • Smit, P., Raedts, J., Portyanko, V., Debelle, F., Gough, C., Bisseling, T., and, Geurts, R., (2005) NSP1 of the GRAS protein family is essential for rhizobial Nod factor-induced transcription. Science, 308, 1789-1791.
    • (2005) Science , vol.308 , pp. 1789-1791
    • Smit, P.1    Raedts, J.2    Portyanko, V.3    Debelle, F.4    Gough, C.5    Bisseling, T.6    Geurts, R.7
  • 37
    • 0029924239 scopus 로고    scopus 로고
    • Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/calmodulin
    • Takezawa, D., Ramachandiran, S., Paranjape, V., and, Poovaiah, B.W., (1996) Dual regulation of a chimeric plant serine/threonine kinase by calcium and calcium/calmodulin. J. Biol. Chem. 271, 8126-8132.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8126-8132
    • Takezawa, D.1    Ramachandiran, S.2    Paranjape, V.3    Poovaiah, B.W.4
  • 38
    • 33646684841 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinase leads to spontaneous nodule development
    • 2+/calmodulin-dependent kinase leads to spontaneous nodule development. Nature, 441, 1153-1156.
    • (2006) Nature , vol.441 , pp. 1153-1156
    • Tirichine, L.1    Imaizumi-Anraku, H.2    Yoshida, S.3
  • 39
    • 0039981125 scopus 로고
    • Calcium-promoted protein phosphorylation in plants
    • Veluthambi, K., and, Poovaiah, B.W., (1984) Calcium-promoted protein phosphorylation in plants. Science, 223, 167-169.
    • (1984) Science , vol.223 , pp. 167-169
    • Veluthambi, K.1    Poovaiah, B.W.2
  • 40
    • 56449107115 scopus 로고    scopus 로고
    • CYCLOPS, a mediator of symbiotic intracellular accommodation
    • Yano, K., Yoshida, S., and, Muller, J., et al. (2008) CYCLOPS, a mediator of symbiotic intracellular accommodation. Proc. Natl Acad. Sci. USA, 105, 20540-20545.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20540-20545
    • Yano, K.1    Yoshida, S.2    Muller, J.3


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