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Microtubule affinity‐regulating kinase 1 (MARK1) is activated by electroconvulsive shock in the rat hippocampus
Author(s) -
Jeon Songhee,
Kim YongSik,
Park Joobae,
Bae ChangDae
Publication year - 2005
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2005.03505.x
Subject(s) - phosphorylation , dephosphorylation , kinase , protein kinase a , electroconvulsive shock , hippocampus , microtubule , microbiology and biotechnology , neurotrophic factors , chemistry , biology , biochemistry , neuroscience , phosphatase , endocrinology , receptor
Electroconvulsive shock (ECS) induces phosphorylation and dephosphorylation of many signaling molecules in the rat brain. While studying phosphorylated proteins in the rat brain after ECS, we observed a 100‐kDa protein that cross‐reacted with anti‐phospho‐p70 S6 kinase antibody, which was subsequently purified and identified as microtubule affinity‐regulating kinase 1 (MARK1). Purified MARK1 was phosphorylated at the Ser and Thr residues. MARK1 activation and subsequent Tau phosphorylation in the hippocampus after ECS was confirmed by an in‐gel kinase assay using tau protein as a substrate. MARK1 was maximally activated between 2 and 5 min after ECS, and Tau phosphorylation at Ser262 was also increased at 2 min and lasted to 1 h after ECS. Taken together, we concluded that ECS activated MARK1 and subsequently phosphorylated Tau at Ser262. Both MARK1 activity and Tau phosphorylation were increased in the rat hippocampus after chronic ECS where axonal remodeling was apparent. In order to investigate the physiologic stimuli which are involved in the activation of MARK1, SH‐SY 5Y cells were treated with brain‐derived neurotrophic factor or 60 m m KCl. Both stimuli were capable of inducing MARK activation.