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   <subfield code="a">Non-proline-dependent protein kinases phosphorylate several sites found in tau from Alzheimer disease brain</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Toolsee Singh, Tanweer Zaidi, Inge Grundke-Iqbal, Khalid Iqbal]</subfield>
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   <subfield code="a">Of 21 phosphorylation sites identified in PHF-tau 11 are on ser/thr-X motifs and are probably phosphorylated by non-proline-dependent protein kinases (non-PDPKs). The identities of the non-PDPKs and how they interact to hyperphosphorylate PHF-tau are still unclear. In a previous study we have shown that the rate of phosphorylation of human tau 39 by a PDPK (GSK-3) was increased several fold if tau were first prephosphorylated by non-PDPKs (Singh et al., FEBS Lett 358: 267-272, 1995). In this study we have examined how the specificity of a non-PDPK for different sites on human tau 39 is modulated when tau is prephosphorylated by other non-PDPKs (A-kinase, C-kinase, CK-1, CaM kinase II) as well as a PDPK (GSK-3). We found that the rate of phosphorylation of tau 39 by a non-PDPK can be stimulated if tau were first prephosphorylated by other non-PDPKs. Of the four non-PDPKs only CK-1 can phosphorylate sites (thr 231, ser 396, ser 404) known to be present in PHF-tau. Further, these sites were phosphorylated more rapidly and to a greater extent by CK-1 if tau 39 were first prephosphorylated by A-kinase, CaM kinase II or GSK-3. These results suggest that the site specificities of the non-PDPKs that participate in PHF-tau hyperphosphorylation can be modulated at the substrate level by the phosphorylation state of tau.</subfield>
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   <subfield code="a">Kluwer Academic Publishers, 1996</subfield>
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   <subfield code="a">GSK-3</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">tau protein</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">protein kinases</subfield>
   <subfield code="2">nationallicence</subfield>
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   <subfield code="a">Alzheimer disease</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">paired helical filaments</subfield>
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   <subfield code="a">microtubules</subfield>
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   <subfield code="a">PHF : paired helical filaments</subfield>
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   <subfield code="a">A-kinase : cyclic AMP-dependent protein kinase</subfield>
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   <subfield code="a">CaM kinase II : calcium/calmodulin-dependent protein kinase II</subfield>
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   <subfield code="a">C-kinase : calcium/phospholipid-dependent protein kinase</subfield>
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   <subfield code="a">CK-1 : casein kinase-1</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">CK-2 : casein kinase-2</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">GSK-3 : glycogen synthase kinase-3</subfield>
   <subfield code="2">nationallicence</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">MAP kinase : mitogen-activated protein kinase</subfield>
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  <datafield tag="690" ind1=" " ind2="7">
   <subfield code="a">PDPK : proline-dependent protein kinase</subfield>
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   <subfield code="a">Singh</subfield>
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   <subfield code="u">New York State Institute for Basic Research in Developmental Disabilities, 10314, Staten Island, New York, USA</subfield>
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   <subfield code="t">Molecular and Cellular Biochemistry</subfield>
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   <subfield code="a">Metadata rights reserved</subfield>
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