Modulation of GSK‐3‐catalyzed phosphorylation of microtubule‐associated protein tau by non‐proline‐dependent protein kinases

FEBS Letters

Singh, Toolsee J.¹  Zaidi, Tanweer¹  Grundke-Iqbal, Inge¹  Iqbal, Khalid¹ 

[1] New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY 10314, USA

关键词: GSK-3;    Tau protein;    Protein kinase;    Alzheimer's disease;    Paired helical filament;    PHF;    paired helical filaments;    A-kinase;    cyclic AMP-dependent protein kinase;    CaM kinase II;    calcium/calmodulin-dependent protein kinase 11;    C-kinase;    calcium/phospholipid-dependent protein kinase;    CK-1;    casein kinase-1;    CK-2;    casein kinase-2;    Gr kinase;    calcium/calmodulin-dependent protein kinase from rat cerebellum;    GSK-3;    glycogen synthase kinase-3;    MAP kinase;    mitogen-activated protein kinase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    PDPK;    proline-dependent protein kinase;   

DOI  :  10.1016/0014-5793(94)01383-C

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The phosphorylation of bovine tau, either by GSK-3 alone or by a combination of GSK-3 and several non-proline-dependent protein kinases (non-PDPKs), was studied. GSK-3 alone catalyzed the incorporation of ∼ 3 mol ³²P/mot tau at a relatively slow rate. Prephosphorylation of tau by A-kinase, C-kinase, or CK-2 (but not by CK-1, CaM kinase II or Gr kinase) increased both the rate and extent of a subsequent phosphorylation catalyzed by GSK-3 by several-fold. These results suggest that the phosphorylation of tau by PDPKs such as GSK-3 (and possibly MAP kinase, cdk5) may be positively modulated at the substrate level by non-PDPK-catalyzed phosphorylations.

【 授权许可】

Unknown