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p90‐RSK and Akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant‐stimulated neutrophils
Author(s) -
De Mesquita Dirson D.,
Zhan Qian,
Crossley Lisa,
Badwey John A.
Publication year - 2001
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/s0014-5793(01)02669-2
Subject(s) - phosphorylation , gsk 3 , glycogen synthase , chemotaxis , serine , chemistry , gsk3b , gene isoform , protein kinase b , microbiology and biotechnology , biochemistry , kinase , receptor , biology , gene
Stimulation of neutrophils with the chemoattractant fMet‐Leu‐Phe (fMLP) triggers phosphorylation/inactivation of the α‐ and β‐isoforms of glycogen synthase kinase 3 (GSK‐3) with phosphorylation of the α‐isoform predominating. These reactions were monitored with a phosphospecific antibody that only recognized the α‐ or β‐isoforms of GSK‐3 when these proteins were phosphorylated on serine residues 21 and 9, respectively. Inhibitor studies indicated that phosphorylation of GSK‐3α may be catalyzed by the combined action of p90‐RSK and Akt and may represent a new strategy by which G protein‐coupled receptors inactivate GSK‐3. Inactivation of GSK‐3 may be one of the mechanisms that delay apoptosis in fMLP‐stimulated neutrophils.