[HTML][HTML] Dual regulation of glycogen synthase kinase 3 (GSK3) α/β by protein kinase C (PKC) α and Akt promotes thrombin-mediated integrin αIIbβ3 activation and …
SF Moore, MTJ van den Bosch, RW Hunter… - Journal of Biological …, 2013 - ASBMB
Glycogen synthase kinase-3 is a Ser/Thr kinase, tonically active in resting cells but inhibited
by phosphorylation of an N-terminal Ser residue (Ser 21 in GSK3α and Ser 9 in GSK3β) in
response to varied external stimuli. Recent work suggests that GSK3 functions as a negative
regulator of platelet function, but how GSK3 is regulated in platelets has not been examined
in detail. Here, we show that early thrombin-mediated GSK3 phosphorylation (0–30 s) was
blocked by PKC inhibitors and largely absent in platelets from PKCα knock-out mice. In …
by phosphorylation of an N-terminal Ser residue (Ser 21 in GSK3α and Ser 9 in GSK3β) in
response to varied external stimuli. Recent work suggests that GSK3 functions as a negative
regulator of platelet function, but how GSK3 is regulated in platelets has not been examined
in detail. Here, we show that early thrombin-mediated GSK3 phosphorylation (0–30 s) was
blocked by PKC inhibitors and largely absent in platelets from PKCα knock-out mice. In …