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Volumn 391, Issue 1, 2010, Pages 78-84

Regulation of phosphorylation at the postsynaptic density during different activity states of Ca2+/calmodulin-dependent protein kinase II

Author keywords

CaMKII; GKAP; iTRAQ; PSD; SAPAP; Shank

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALCIUM ION; SCAFFOLD PROTEIN;

EID: 72949122110     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.167     Document Type: Article
Times cited : (36)

References (29)
  • 1
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: a more quantitative view
    • Sheng M., and Hoogenraad C.C. The postsynaptic architecture of excitatory synapses: a more quantitative view. Annu. Rev. Biochem. 76 (2007) 823-847
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 2
    • 0036513485 scopus 로고    scopus 로고
    • The molecular basis of CaMKII function in synaptic and behavioural memory
    • Lisman J., Schulman H., and Cline H. The molecular basis of CaMKII function in synaptic and behavioural memory. Nat. Rev. Neurosci. 3 (2002) 175-190
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 175-190
    • Lisman, J.1    Schulman, H.2    Cline, H.3
  • 3
    • 1542344969 scopus 로고    scopus 로고
    • Targeting of calcium/calmodulin-dependent protein kinase II
    • Colbran R.J. Targeting of calcium/calmodulin-dependent protein kinase II. Biochem. J. 378 (2004) 1-16
    • (2004) Biochem. J. , vol.378 , pp. 1-16
    • Colbran, R.J.1
  • 4
    • 3543028051 scopus 로고    scopus 로고
    • Identification of novel phosphorylation sites on postsynaptic density proteins
    • Jaffe H., Vinade L., and Dosemeci A. Identification of novel phosphorylation sites on postsynaptic density proteins. Biochem. Biophys. Res. Commun. 321 (2004) 210-218
    • (2004) Biochem. Biophys. Res. Commun. , vol.321 , pp. 210-218
    • Jaffe, H.1    Vinade, L.2    Dosemeci, A.3
  • 10
    • 0034734813 scopus 로고    scopus 로고
    • Investigation of protein substrates of Ca(2+)/calmodulin-dependent protein kinase II translocated to the postsynaptic density
    • Yoshimura Y., Aoi C., and Yamauchi T. Investigation of protein substrates of Ca(2+)/calmodulin-dependent protein kinase II translocated to the postsynaptic density. Brain Res. Mol. Brain Res. 81 (2000) 118-128
    • (2000) Brain Res. Mol. Brain Res. , vol.81 , pp. 118-128
    • Yoshimura, Y.1    Aoi, C.2    Yamauchi, T.3
  • 11
    • 0036297663 scopus 로고    scopus 로고
    • Identification of protein substrates of Ca(2+)/calmodulin-dependent protein kinase II in the postsynaptic density by protein sequencing and mass spectrometry
    • Yoshimura Y., Shinkawa T., Taoka M., Kobayashi K., Isobe T., and Yamauchi T. Identification of protein substrates of Ca(2+)/calmodulin-dependent protein kinase II in the postsynaptic density by protein sequencing and mass spectrometry. Biochem. Biophys. Res. Commun. 290 (2002) 948-954
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 948-954
    • Yoshimura, Y.1    Shinkawa, T.2    Taoka, M.3    Kobayashi, K.4    Isobe, T.5    Yamauchi, T.6
  • 12
    • 0024077809 scopus 로고
    • Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+independent activity
    • Thiel G., Czernik A.J., Gorelick F., Nairn A.C., and Greengard P. Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+independent activity. Proc. Natl. Acad. Sci. USA 85 (1988) 6337-6341
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 6337-6341
    • Thiel, G.1    Czernik, A.J.2    Gorelick, F.3    Nairn, A.C.4    Greengard, P.5
  • 13
    • 0023819289 scopus 로고
    • Ca2+/calmodulin dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains
    • Schworer C.M., Colbran R.J., Keefer J.R., and Soderling T.R. Ca2+/calmodulin dependent protein kinase II. Identification of a regulatory autophosphorylation site adjacent to the inhibitory and calmodulin-binding domains. J. Biol. Chem. 263 (1988) 13486-13489
    • (1988) J. Biol. Chem. , vol.263 , pp. 13486-13489
    • Schworer, C.M.1    Colbran, R.J.2    Keefer, J.R.3    Soderling, T.R.4
  • 14
    • 0024693410 scopus 로고
    • Expression of a multifunctional Ca2+/calmodulin-dependent protein kinase and mutational analysis of its autoregulation
    • Hanson P.I., Kapiloff M.S., Lou L.L., Rosenfeld M.G., and Schulman H. Expression of a multifunctional Ca2+/calmodulin-dependent protein kinase and mutational analysis of its autoregulation. Neuron 3 (1989) 59-70
    • (1989) Neuron , vol.3 , pp. 59-70
    • Hanson, P.I.1    Kapiloff, M.S.2    Lou, L.L.3    Rosenfeld, M.G.4    Schulman, H.5
  • 15
    • 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. 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 (1990) 11213-11219
    • (1990) J. Biol. Chem. , vol.265 , pp. 11213-11219
    • Colbran, R.J.1    Soderling, T.R.2
  • 16
    • 0025294106 scopus 로고
    • Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain
    • Patton B.L., Miller S.G., and Kennedy M.B. Activation of type II calcium/calmodulin-dependent protein kinase by Ca2+/calmodulin is inhibited by autophosphorylation of threonine within the calmodulin-binding domain. J. Biol. Chem. 265 (1990) 11204-11212
    • (1990) J. Biol. Chem. , vol.265 , pp. 11204-11212
    • Patton, B.L.1    Miller, S.G.2    Kennedy, M.B.3
  • 17
    • 0028007142 scopus 로고
    • Identification of a major autophosphorylation site on postsynaptic density-associated Ca2+/calmodulin-dependent protein kinase
    • Dosemeci A., Gollop N., and Jaffe H. Identification of a major autophosphorylation site on postsynaptic density-associated Ca2+/calmodulin-dependent protein kinase. J. Biol. Chem. 269 (1994) 31330-31333
    • (1994) J. Biol. Chem. , vol.269 , pp. 31330-31333
    • Dosemeci, A.1    Gollop, N.2    Jaffe, H.3
  • 19
    • 34548653718 scopus 로고    scopus 로고
    • A structural mechanism for maintaining the 'on-state' of the CaMKII memory switch in the post-synaptic density
    • Mullasseril P., Dosemeci A., Lisman J.E., and Griffith L.C. A structural mechanism for maintaining the 'on-state' of the CaMKII memory switch in the post-synaptic density. J. Neurochem. 103 (2007) 357-364
    • (2007) J. Neurochem. , vol.103 , pp. 357-364
    • Mullasseril, P.1    Dosemeci, A.2    Lisman, J.E.3    Griffith, L.C.4
  • 21
    • 2342437016 scopus 로고    scopus 로고
    • Regulation of the neuron-specific Ras GTPase-activating protein, synGAP, by Ca2+/calmodulin-dependent protein kinase II
    • Oh J.S., Manzerra P., and Kennedy M.B. Regulation of the neuron-specific Ras GTPase-activating protein, synGAP, by Ca2+/calmodulin-dependent protein kinase II. J. Biol. Chem. 279 (2004) 17980-17988
    • (2004) J. Biol. Chem. , vol.279 , pp. 17980-17988
    • Oh, J.S.1    Manzerra, P.2    Kennedy, M.B.3
  • 22
    • 3142671973 scopus 로고    scopus 로고
    • Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase II resulting in regulation of its binding to F-actin
    • Grossman S.D., Futter M., Snyder G.L., Allen P.B., Nairn A.C., Greengard P., and Hsieh-Wilson L.C. Spinophilin is phosphorylated by Ca2+/calmodulin-dependent protein kinase II resulting in regulation of its binding to F-actin. J. Neurochem. 90 (2004) 317-324
    • (2004) J. Neurochem. , vol.90 , pp. 317-324
    • Grossman, S.D.1    Futter, M.2    Snyder, G.L.3    Allen, P.B.4    Nairn, A.C.5    Greengard, P.6    Hsieh-Wilson, L.C.7
  • 23
    • 0024475162 scopus 로고
    • Regulation of Ca2+/calmodulin-dependent cyclic nucleotide phosphodiesterase by the autophosphorylated form of Ca2+/calmodulin-dependent protein kinase II
    • Hashimoto Y., Sharma R.K., and Soderling T.R. Regulation of Ca2+/calmodulin-dependent cyclic nucleotide phosphodiesterase by the autophosphorylated form of Ca2+/calmodulin-dependent protein kinase II. J. Biol. Chem. 264 (1989) 10884-10887
    • (1989) J. Biol. Chem. , vol.264 , pp. 10884-10887
    • Hashimoto, Y.1    Sharma, R.K.2    Soderling, T.R.3
  • 24
    • 62649083636 scopus 로고    scopus 로고
    • Densin-180: revised membrane topology, domain structure and phosphorylation status
    • Thalhammer A., Trinidad J.C., Burlingame A.L., and Schoepfer R. Densin-180: revised membrane topology, domain structure and phosphorylation status. J. Neurochem. 109 (2009) 297-302
    • (2009) J. Neurochem. , vol.109 , pp. 297-302
    • Thalhammer, A.1    Trinidad, J.C.2    Burlingame, A.L.3    Schoepfer, R.4
  • 26
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J., Weinberg R.J., Worley P.F., and Sheng M. Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23 (1999) 569-582
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1    Kim, E.2    Tu, J.C.3    Xiao, B.4    Sala, C.5    Valtschanoff, J.6    Weinberg, R.J.7    Worley, P.F.8    Sheng, M.9
  • 27
    • 0030744875 scopus 로고    scopus 로고
    • Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation (see comments)
    • Barria A., Muller D., Derkach V., Griffith L.C., and Soderling T.R. Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation (see comments). Science 276 (1997) 2042-2045
    • (1997) Science , vol.276 , pp. 2042-2045
    • Barria, A.1    Muller, D.2    Derkach, V.3    Griffith, L.C.4    Soderling, T.R.5
  • 28
    • 0034708587 scopus 로고    scopus 로고
    • Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction
    • Hayashi Y., Shi S.H., Esteban J.A., Piccini A., Poncer J.C., and Malinow R. Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287 (2000) 2262-2267
    • (2000) Science , vol.287 , pp. 2262-2267
    • Hayashi, Y.1    Shi, S.H.2    Esteban, J.A.3    Piccini, A.4    Poncer, J.C.5    Malinow, R.6
  • 29
    • 0038222585 scopus 로고    scopus 로고
    • AMPA receptor trafficking and long-term potentiation
    • Malinow R. AMPA receptor trafficking and long-term potentiation. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358 (2003) 707-714
    • (2003) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.358 , pp. 707-714
    • Malinow, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.