【 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
【 预 览 】
Files | Size | Format | View |
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RO201912020300561ZK.pdf | 524KB | download |