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High External Potassium Induces an Increase in the Phosphorylation of the Cytoskeletal Protein MAP2 in Rat Hippocampal Slices
Author(s) -
DíazNido Javier,
Montoro Rafael J.,
LópezBarneo José,
Avila Jesús
Publication year - 1993
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.1993.tb00933.x
Subject(s) - phosphorylation , hippocampal formation , microbiology and biotechnology , cytoskeleton , chemistry , protein phosphorylation , kinase , calmodulin , protein kinase a , biology , biochemistry , neuroscience , cell , enzyme
Depolarization induced in rat hippocampal slices by a high concentration of extracellular K + leads to an increase in the phosphorylation of microtubule‐associated protein MAP2. The comparison of the major phosphopeptides derived from in situ and in vitro phosphorylated MAP2 suggests the implication of calcium‐dependent protein kinases, including calcium/calmodulin‐dependent protein kinase type II and protein kinase C, in the up‐phosphorylation of MAP2. In particular, a peptide containing the tubulin‐binding domain of the MAP2 molecule may be phosphorylated by protein kinase C. As the association of MAP2 with the cytoskeleton may be regulated by phosphorylation, we suggest that changes in the phosphorylation level bf MAP2 might be involved in synaptic remodelling in hippocampal neurons.