[HTML][HTML] Relationships between Rap1b, affinity modulation of integrin αIIbβ3, and the actin cytoskeleton
A Bertoni, S Tadokoro, K Eto, N Pampori… - Journal of Biological …, 2002 - ASBMB
The affinity of integrin α IIb β 3 for fibrinogen is controlled by inside-out signals that are
triggered by agonists like thrombin. Agonist treatment of platelets also activates Rap1b, a
small GTPase known to promote integrin-dependent adhesion of other cells. Therefore, we
investigated the role of Rap1b in α IIb β 3 function by viral transduction of GFP-Rap1
chimeras into murine megakaryocytes, which exhibit inside-out signaling similar to platelets.
Expression of constitutively active GFP-Rap1b (V12) had no effect on unstimulated …
triggered by agonists like thrombin. Agonist treatment of platelets also activates Rap1b, a
small GTPase known to promote integrin-dependent adhesion of other cells. Therefore, we
investigated the role of Rap1b in α IIb β 3 function by viral transduction of GFP-Rap1
chimeras into murine megakaryocytes, which exhibit inside-out signaling similar to platelets.
Expression of constitutively active GFP-Rap1b (V12) had no effect on unstimulated …