p90‐RSK and Akt may promote rapid phosphorylation/inactivation of glycogen synthase kinase 3 in chemoattractant‐stimulated neutrophils

FEBS Letters

Badwey, John A.¹  De Mesquita, Dirson D.¹  Crossley, Lisa¹  Zhan, Qian¹ 

[1] Center for Experimental Therapeutics and Reperfusion Injury, Department of Anesthesiology, Perioperative and Pain Medicine, Brigham and Women's Hospital, Harvard Medical School, Thorn Building, Room 703, 75 Francis Street, Boston, MA 02115, USA

关键词: Neutrophil;    Cell signaling;    Chemoattractant;    p90-RSK;    Glycogen synthase kinase 3;    fMLP;    fMet-Leu-Phe;    GSK-3;    glycogen synthase kinase 3;    ERK;    extracellular signal-regulated kinase;    PI 3-K;    phosphoinositide 3-kinase;    PDK-1;    3-phosphoinositide-dependent protein kinase 1;    PKA;    protein kinase A;   

DOI  :  10.1016/S0014-5793(01)02669-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown