Src kinase activation by direct interaction with the integrin β cytoplasmic domain
By E. Arias-Salgado, S. Lizano, Sugata Sarkar, J. Brugge, M. Ginsberg, S. Shattil. Proceedings of the National Academy of Sciences of the United States of America, 2003
602 citations recorded by the source corpus.
Subfields: Immunology and Allergy, Molecular Biology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/f13101ffc1ac154553bd05e38eda39486ff750a8
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Immunology and Allergy
- Valerie M. Weaver
- M. Schwartz
- S. Mitra
- Daniel A. Hanson
- E. Danen
- K. Legate
- Matthew J. Paszek
- D. Schlaepfer
In Molecular Biology
- Valerie M. Weaver
- M. Schwartz
- S. Mitra
- Daniel A. Hanson
- E. Danen
- K. Legate
- D. Schlaepfer
- D. Calderwood
In Radiology, Nuclear Medicine and Imaging
Citations in the corpus
- Genetic and cell biological analysis of integrin outside-in signaling. (2009, background): “The activation of b1-, b2-, and b3-bound SFKs has also been shown to occur through transactivation of Src by itself or by competition from FAK for binding to the Src SH2 domain (Arias-Salgado et al. 2003; Mitra et al. 2005).”
- Focal adhesion kinase: in command and control of cell motility (2005, background): “As Src can also become activated through direct interaction with the cytoplasmic domains of β-integrin”
- Adhesion signaling – crosstalk between integrins, Src and Rho (2009, background): “Jo ur na l o f C el l S ci en ce 1062 residue in the activation loop of the Src kinase domain, probably resulting from enhanced cross-phosphorylation that is triggered by integrin clustering (Arias-Salgado et al., 2003; Huveneers et al., 2007).”
- PKD1/PKCμ promotes αvβ3 integrin recycling and delivery to nascent focal adhesions (2004, background): “domain has no effect on the interaction of b3 integrin with c-Src ( Arias-Salgado et al, 2003 ), indicating that the precise determinants for binding this tyrosine kinase differ from”
- Integrins and extracellular matrix in mechanotransduction. (2010, background): “SFKs can bind directly to β integrin tails which contributes to the activation of kinase activity.(40) Integrin-linked kinase has a major role as a signaling scaffold at integrin adhesions.”
- Tensional homeostasis and the malignant phenotype. (2005, background): “Indeed, MECs on soft BM gels had higher levels of total and activated LynpY507 and LckpY505 kinases than MECs on stiff gels (Figure 2G), and MECs grew and survived in 3D quite well, consistent with integrin activation, FAKpY861, and adhesion assembly (Arias-Salgado et al., 2003).”
- Integrin signalling at a glance (2009, background): “SFKs can bind directly to βintegrin tails in a tail- and SFK-specific manner, and this interaction contributes to activation of kinase activity and controls cell spreading ( Arias-Salgado et al., 2003; Reddy et al., 2008).”