[HTML][HTML] Identification of Shc as the primary protein binding to the tyrosine-phosphorylated β3 subunit of αIIbβ3 during outside-in integrin platelet signaling
KJ Cowan, DA Law, DR Phillips - Journal of Biological Chemistry, 2000 - ASBMB
Outside-in signaling mediated by the integrin α IIb β 3 (GPIIbIIIa) is critical to platelet function
and has been shown to involve the phosphorylation of tyrosine residues on the cytoplasmic
tail of β 3. To identify proteins that bind directly to phosphorylated β 3, we utilized an affinity
column consisting of a peptide modeled on the tyrosine-phosphorylated cytoplasmic domain
of β 3. Tandem mass spectrometric sequencing and immunoblotting demonstrated that Shc
was the primary protein binding to phosphorylated β 3. To determine the involvement of Shc …
and has been shown to involve the phosphorylation of tyrosine residues on the cytoplasmic
tail of β 3. To identify proteins that bind directly to phosphorylated β 3, we utilized an affinity
column consisting of a peptide modeled on the tyrosine-phosphorylated cytoplasmic domain
of β 3. Tandem mass spectrometric sequencing and immunoblotting demonstrated that Shc
was the primary protein binding to phosphorylated β 3. To determine the involvement of Shc …