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Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
Author(s) -
Mandelkow E.-M.,
Drewes G.,
Biernat J.,
Gustke N.,
Van Lint J.,
Vandenheede J.R.,
Mandelkow E.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81496-9
Subject(s) - gsk 3 , kinase , microbiology and biotechnology , phosphorylation , glycogen synthase , microtubule , integrin linked kinase , ask1 , cyclin dependent kinase 9 , biochemistry , protein kinase a , biology , chemistry , mitogen activated protein kinase kinase , microtubule associated protein , tau protein , cyclin dependent kinase 2 , alzheimer's disease , medicine , disease
The Alzheimer‐like state of tau protein includes phosphorylation by a proline‐directed Ser/Thr kinase present in normal or pathological human brain. Extending earlier results on MAP kinase, we show here that the proline‐directed kinase, GSK3, can induce an Alzheimer‐like immune response involving several distinct and phoshorylatable epitopes at Ser—Pro motifs, as well as gel mobility shift, similar to MAP kinase. Both kinases behave like microtubule‐associated proteins in that they co‐purify through cycles of assembly and disassembly, and both kinases are directly associated with paired helical filaments.