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The Tek/Tie2 receptor tyrosine kinase plays a pivotal role in vascular and hematopoietic development. To study the signal transduction pathways that are mediated by this receptor, we have used the yeast two-hybrid system to identify signaling molecules that associate with the phosphorylated Tek receptor. Using this approach, we demonstrate that five(More)
Several peptides found in insect venom, including melittin, apamin and mastoparan, inhibited the activity of calmodulin-stimulated phosphodiesterase at concentrations that had no appreciable effect on basal phosphodiesterase activity; the Ki value of melittin for inhibiting calmodulin activity was 30 nM. Acetylation of the peptides reduced their inhibitory(More)
In vertebrates, Grb2-associated binder (Gab)1–3 constitute a family of conserved docking proteins. Gab2 is tyrosine-phosphorylated upon activation of a variety of growth factor, hormone, antigen, cytokine and cell matrix receptors, leading to the recruitment of specific src homology (SH)2 domain-containing effectors, which include the p85 subunit of(More)
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