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Angaben zur Quelle [Bearbeiten]

Autor     Robert D. Blitzer, Ravi Iyengar, Emmanuel M. Landau
Titel    Postsynaptic Signaling Networks: Cellular Cogwheels Underlying Long-Term Plasticity
Zeitschrift    Biological Psychiatry
Datum    15. January 2005
Jahrgang    57
Nummer    2
Seiten    113-119
DOI    doi:10.1016/j.biopsych.2004.02.031
URL    http://www.biologicalpsychiatryjournal.com/article/S0006-3223%2804%2900390-7/abstract , http://www.researchgate.net/publication/8078259_Postsynaptic_signaling_networks_cellular_cogwheels_underlying_long-term_plasticity/file/5046351d2ea9d2bbe3.pdf

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Fragmente der Quelle:
[1.] Sng/Fragment 023 17 - Diskussion
Zuletzt bearbeitet: 2016-05-22 22:04:19 Schumann
Blitzer et al 2005, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Sng

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Seite: 23, Zeilen: 17-22
Quelle: Blitzer et al 2005
Seite(n): 114, Zeilen: re.Sp. 39-47
A major target for Ca2+ is CaMKII, and among its many actions are the phosphorylation of GluR1 at serine 831 (which increases the channel conductance of the AMPA receptor; (Lee et al., 2000)), and the insertion of the receptor into the postsynaptic membrane through an indirect mechanism; (Hayashi et al., 2000). From a network perspective, the multiple effects of activated CaMKII define it as a ´node´, a point where a signal is split and directed to multiple targets (Schmitt et al., 2005).

66. Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, Malinow R (2000) Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction. Science 287: 2262-2267.

92. Lee HK, Barbarosie M, Kameyama K, Bear MF, Huganir RL (2000) Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405: 955-959.

141. Schmitt JM, Guire ES, Saneyoshi T, Soderling TR (2005) Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellular-regulated kinase-dependent long-term potentiation. J Neurosci 25: 1281-1290.

A major target for Ca2+ is Ca2+/calmodulin-dependent kinase type II (CaMKII), a major component of the postsynaptic density. Among its many actions are the phosphorylation of GluR1 at serine 831 (which increases the channel conductance of the AMPA receptor; Lee et al 2000), and the insertion of the receptor into the postsynaptic membrane (through an indirect mechanism; Hayashi et al 2000). From a network perspective, the multiple effects of activated CaMKII define it as a “node,” a point where a signal is split and directed to multiple targets.

Hayashi Y, Shi SH, Esteban JA, Piccini A, Poncer JC, Malinow R (2000): Driving AMPA receptors into synapses by LTP and CaMKII: Requirement for GluR1 and PDZ domain interaction. Science 287:2262–2267.

Lee HK, Barbarosie M, Kameyama K, Bear MF, Huganir RL (2000): Regulation of distinct AMPA receptor phosphorylation sites during bidirectional synaptic plasticity. Nature 405:955–959.

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[2.] Sng/Fragment 024 01 - Diskussion
Zuletzt bearbeitet: 2016-05-22 22:06:20 Schumann
Blitzer et al 2005, Fragment, Gesichtet, SMWFragment, Schutzlevel sysop, Sng, Verschleierung

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Seite: 24, Zeilen: 1-12
Quelle: Blitzer et al 2005
Seite(n): 115, Zeilen: Legende zu Figure 2
1.6.3. The interaction of three major postsynaptic signaling pathways in LTP

Ca2+/calmodulin protein kinase II (CaMKII), mitogen-activated protein kinase (MAPK), and adenosine 3′,5′-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) are all required for the induction of LTP (Frey et al., 1993;English and Sweatt, 1997;Bortolotto and Collingridge, 1998). The influx of Ca2+ through N-methyl-D-aspartate-type receptors (NMDA-R) or voltage-dependent Ca2+ channels (VDCC) can engage signaling cascades that activate these kinases. MAPK and CaMKII can promote the phosphorylation of each other, and MAPK is required for an increase in CaMKII levels produced by LTP-inducing stimulation (Giovannini et al., 2001). PKA activity promotes CaMKII phosphorylation by indirectly inhibiting the protein phosphatase PP1, which would otherwise limit the degree or persistence of CaMKII activation by dephosphorylating the kinase (Atkins et al., 2005).


15. Atkins CM, Davare MA, Oh MC, Derkach V, Soderling TR (2005) Bidirectional regulation of cytoplasmic polyadenylation element-binding protein phosphorylation by Ca2+/calmodulin-dependent protein kinase II and protein phosphatase 1 during hippocampal long-term potentiation. J Neurosci 25: 5604-5610.

26. Bortolotto ZA, Collingridge GL (1998) Involvement of calcium/calmodulin-dependent protein kinases in the setting of a molecular switch involved in hippocampal LTP. Neuropharmacology 37: 535-544.

47. English JD, Sweatt JD (1997) A requirement for the mitogen-activated protein kinase cascade in hippocampal long term potentiation. J Biol Chem 272: 19103-19106.

54. Frey U, Huang YY, Kandel ER (1993) Effects of cAMP simulate a late stage of LTP in hippocampal CA1 neurons. Science 260: 1661-1664.

64. Giovannini MG, Blitzer RD, Wong T, Asoma K, Tsokas P, Morrison JH, Iyengar R, Landau EM (2001) Mitogen-activated protein kinase regulates early phosphorylation and delayed expression of Ca2+/calmodulin-dependent protein kinase II in long-term potentiation. J Neurosci 21: 7053-7062.

Figure 2. The interaction of three major postsynaptic signaling pathways in LTP. Ca2+/calmodulin protein kinase II (CaMKII), mitogen-activated protein kinase (MAPK), and adenosine 3’,5’-cyclic monophosphate (cAMP)-dependent protein kinase (PKA) are all required for the induction of LTP. The influx of Ca2+ through N-methyl-D-aspartate-type receptors (NMDA-R) or voltage-dependent Ca2+ channels (VDCC) can engage signaling cascades that activate these kinases, and PKA can additionally be activated by β-adrenergic receptors (β-AR) and other G protein-coupled receptors. MAPK and CaMKII can promote the phosphorylation of each other, and MAPK is required for an increase in CaMKII levels produced by LTP-inducing stimulation. PKA activity promotes CaMKII phosphorylation by indirectly inhibiting the protein phosphatase PP1, which would otherwise limit the degree or persistence of CaMKII activation by dephosphorylating the kinase.
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Sichter
(Graf Isolan) Schumann

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