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Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein

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Bibliographische Detailangaben
Zeitschriftentitel: Journal of Neurochemistry
Personen und Körperschaften: Dosemeci, Ayse, Reese, Thomas S.
In: Journal of Neurochemistry, 61, 1993, 2, S. 550-555
Medientyp: E-Article
Sprache: Englisch
veröffentlicht:
Wiley
Schlagwörter:
author_facet Dosemeci, Ayse
Reese, Thomas S.
Dosemeci, Ayse
Reese, Thomas S.
author Dosemeci, Ayse
Reese, Thomas S.
spellingShingle Dosemeci, Ayse
Reese, Thomas S.
Journal of Neurochemistry
Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
Cellular and Molecular Neuroscience
Biochemistry
author_sort dosemeci, ayse
spelling Dosemeci, Ayse Reese, Thomas S. 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.1993.tb02158.x <jats:p><jats:bold>Abstract: </jats:bold> The major postsynaptic density protein, proposed to be a calcium/calmodulin‐dependent protein kinase, becomes phosphorylated when a postsynaptic density preparation from rat cerebral cortex is incubated in medium containing calcium and calmodulin. Upon longer incubation, however, the level of phosphorylation declines, suggesting the presence of a phosphatase activity. When Microcystin‐LR, a phosphatase inhibitor, is included in the phosphorylation medium, the decline in phosphorylation is prevented and a higher maximal level of phosphorylation can be achieved. Under these conditions, the maximal phosphorylation of major postsynaptic density protein is accompanied by a nearly complete shift in its electrophoretic mobility from 50 kDa to 54 kDa, similar to that described for the a subunit of the soluble calcium/calmodulin‐dependent protein kinase II. Of the four major groups of serine/threonine protein phosphatases, the enzyme responsible for the dephosphorylation of major postsynaptic density protein is neither type 2C, which is insensitive to Microcystin‐LR, nor type 2B, which is calcium‐dependent. As Microcystin‐LR is much more potent than okadaic acid in inhibiting the dephosphorylation of major postsynaptic density protein, it is likely that the postsynaptic density‐associated phosphatase is a type 1. The above results indicate that the relatively low level of phosphorylation of the major postsynaptic density protein observed in preparations containing postsynaptic densities is not due to a difference between the cytoplasmic and postsynaptic density‐associated calcium/calmodulin‐dependent kinases as previously proposed, but to a phosphatase activity, presumably belonging to the type 1 group.</jats:p> Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein Journal of Neurochemistry
doi_str_mv 10.1111/j.1471-4159.1993.tb02158.x
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series Journal of Neurochemistry
source_id 49
title Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_unstemmed Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_full Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_fullStr Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_full_unstemmed Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_short Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_sort inhibition of endogenous phosphatase in a postsynaptic density fraction allows extensive phosphorylation of the major postsynaptic density protein
topic Cellular and Molecular Neuroscience
Biochemistry
url http://dx.doi.org/10.1111/j.1471-4159.1993.tb02158.x
publishDate 1993
physical 550-555
description <jats:p><jats:bold>Abstract: </jats:bold> The major postsynaptic density protein, proposed to be a calcium/calmodulin‐dependent protein kinase, becomes phosphorylated when a postsynaptic density preparation from rat cerebral cortex is incubated in medium containing calcium and calmodulin. Upon longer incubation, however, the level of phosphorylation declines, suggesting the presence of a phosphatase activity. When Microcystin‐LR, a phosphatase inhibitor, is included in the phosphorylation medium, the decline in phosphorylation is prevented and a higher maximal level of phosphorylation can be achieved. Under these conditions, the maximal phosphorylation of major postsynaptic density protein is accompanied by a nearly complete shift in its electrophoretic mobility from 50 kDa to 54 kDa, similar to that described for the a subunit of the soluble calcium/calmodulin‐dependent protein kinase II. Of the four major groups of serine/threonine protein phosphatases, the enzyme responsible for the dephosphorylation of major postsynaptic density protein is neither type 2C, which is insensitive to Microcystin‐LR, nor type 2B, which is calcium‐dependent. As Microcystin‐LR is much more potent than okadaic acid in inhibiting the dephosphorylation of major postsynaptic density protein, it is likely that the postsynaptic density‐associated phosphatase is a type 1. The above results indicate that the relatively low level of phosphorylation of the major postsynaptic density protein observed in preparations containing postsynaptic densities is not due to a difference between the cytoplasmic and postsynaptic density‐associated calcium/calmodulin‐dependent kinases as previously proposed, but to a phosphatase activity, presumably belonging to the type 1 group.</jats:p>
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author Dosemeci, Ayse, Reese, Thomas S.
author_facet Dosemeci, Ayse, Reese, Thomas S., Dosemeci, Ayse, Reese, Thomas S.
author_sort dosemeci, ayse
container_issue 2
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container_title Journal of Neurochemistry
container_volume 61
description <jats:p><jats:bold>Abstract: </jats:bold> The major postsynaptic density protein, proposed to be a calcium/calmodulin‐dependent protein kinase, becomes phosphorylated when a postsynaptic density preparation from rat cerebral cortex is incubated in medium containing calcium and calmodulin. Upon longer incubation, however, the level of phosphorylation declines, suggesting the presence of a phosphatase activity. When Microcystin‐LR, a phosphatase inhibitor, is included in the phosphorylation medium, the decline in phosphorylation is prevented and a higher maximal level of phosphorylation can be achieved. Under these conditions, the maximal phosphorylation of major postsynaptic density protein is accompanied by a nearly complete shift in its electrophoretic mobility from 50 kDa to 54 kDa, similar to that described for the a subunit of the soluble calcium/calmodulin‐dependent protein kinase II. Of the four major groups of serine/threonine protein phosphatases, the enzyme responsible for the dephosphorylation of major postsynaptic density protein is neither type 2C, which is insensitive to Microcystin‐LR, nor type 2B, which is calcium‐dependent. As Microcystin‐LR is much more potent than okadaic acid in inhibiting the dephosphorylation of major postsynaptic density protein, it is likely that the postsynaptic density‐associated phosphatase is a type 1. The above results indicate that the relatively low level of phosphorylation of the major postsynaptic density protein observed in preparations containing postsynaptic densities is not due to a difference between the cytoplasmic and postsynaptic density‐associated calcium/calmodulin‐dependent kinases as previously proposed, but to a phosphatase activity, presumably belonging to the type 1 group.</jats:p>
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spelling Dosemeci, Ayse Reese, Thomas S. 0022-3042 1471-4159 Wiley Cellular and Molecular Neuroscience Biochemistry http://dx.doi.org/10.1111/j.1471-4159.1993.tb02158.x <jats:p><jats:bold>Abstract: </jats:bold> The major postsynaptic density protein, proposed to be a calcium/calmodulin‐dependent protein kinase, becomes phosphorylated when a postsynaptic density preparation from rat cerebral cortex is incubated in medium containing calcium and calmodulin. Upon longer incubation, however, the level of phosphorylation declines, suggesting the presence of a phosphatase activity. When Microcystin‐LR, a phosphatase inhibitor, is included in the phosphorylation medium, the decline in phosphorylation is prevented and a higher maximal level of phosphorylation can be achieved. Under these conditions, the maximal phosphorylation of major postsynaptic density protein is accompanied by a nearly complete shift in its electrophoretic mobility from 50 kDa to 54 kDa, similar to that described for the a subunit of the soluble calcium/calmodulin‐dependent protein kinase II. Of the four major groups of serine/threonine protein phosphatases, the enzyme responsible for the dephosphorylation of major postsynaptic density protein is neither type 2C, which is insensitive to Microcystin‐LR, nor type 2B, which is calcium‐dependent. As Microcystin‐LR is much more potent than okadaic acid in inhibiting the dephosphorylation of major postsynaptic density protein, it is likely that the postsynaptic density‐associated phosphatase is a type 1. The above results indicate that the relatively low level of phosphorylation of the major postsynaptic density protein observed in preparations containing postsynaptic densities is not due to a difference between the cytoplasmic and postsynaptic density‐associated calcium/calmodulin‐dependent kinases as previously proposed, but to a phosphatase activity, presumably belonging to the type 1 group.</jats:p> Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein Journal of Neurochemistry
spellingShingle Dosemeci, Ayse, Reese, Thomas S., Journal of Neurochemistry, Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein, Cellular and Molecular Neuroscience, Biochemistry
title Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_full Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_fullStr Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_full_unstemmed Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_short Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
title_sort inhibition of endogenous phosphatase in a postsynaptic density fraction allows extensive phosphorylation of the major postsynaptic density protein
title_unstemmed Inhibition of Endogenous Phosphatase in a Postsynaptic Density Fraction Allows Extensive Phosphorylation of the Major Postsynaptic Density Protein
topic Cellular and Molecular Neuroscience, Biochemistry
url http://dx.doi.org/10.1111/j.1471-4159.1993.tb02158.x