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Pharmacological inhibition of GSK-3 is not strictly correlated with a decrease in tyrosine phosphorylation of residues 216/279

AuthorsSimón, David; Benítez, María José; Giménez-Cassina, Alfredo; Garrido Jurado, Juan José ; Bhat, R. V.; Díaz-Nido, Javier ; Wandosell, Francisco
Issue Date2008
PublisherJohn Wiley & Sons
CitationJournal of Neuroscience Research 86: 668- 674 (2008)
AbstractRecent evidence suggests that intramolecular autophosphorylation is responsible for the tyrosine phosphorylation (pY) of residues 279 or 216 of glycogen synthase kinase-3 (GSK-3α or β), an event that appears to play an important role in regulating this kinase. This provocative hypothesis was based on the capacity of certain nonselective GSK-3 inhibitors to alter both the activity of GSK-3 and its pY. Inhibitors of GSK-3 are not always capable of preventing this tyrosine phosphorylation, which may require an extended period of time. For example, although lithium chloride inhibits GSK-3 activity, this inhibition does not alter its pY content. Furthermore, even when GSK-3 activity is impaired, GSK-3 pY can still be modified by physiological or pharmacological agents. Taken together, these data indicate that GSK-3 kinase activity is not necessarily correlated with the extent of GSK-3 pY. We hypothesized that some as-yet-unidentified tyrosine kinases and phosphatases may also regulate this kinase. © 2007 Wiley-Liss, Inc.
Identifiersdoi: 10.1002/jnr.21523
issn: 0360-4012
Appears in Collections:(IC) Artículos
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