TRAF4 directs oxidants to focal complexes

Subcellular targeting of oxidants during endothelial cell migration

Endogenous oxidants participate in endothelial cell migration, suggesting that the enzymatic source of oxidants, like other proteins controlling cell migration, requires precise subcellular localization for spatial confinement of signaling effects. We found that the nicotinamide adenine dinucleotide phosphate reduced (NADPH) oxidase adaptor p47(phox) and its binding partner TRAF4 were sequester...

Focal adhesion kinase-dependent focal adhesion recruitment of SH2 domains directs SRC into focal adhesions to regulate cell adhesion and migration

Directed cell migration requires dynamical control of the protein complex within focal adhesions (FAs) and this control is regulated by signaling events involving tyrosine phosphorylation. We screened the SH2 domains present in tyrosine-specific kinases and phosphatases found within FAs, including SRC, SHP1 and SHP2, and examined whether these enzymes transiently target FAs via their SH2 domain...

Stretch-induced phosphorylation of focal adhesion kinase in endothelial cells: role of mitochondrial oxidants.

Mechanical stretch activates a number of signaling pathways in endothelial cells, and it elicits a variety of functional responses including increases in the phosphorylation of focal adhesion kinase (FAK), a nonreceptor tyrosine kinase involved in integrin-mediated signal transduction. Stretch also triggers an increase in the generation of reactive oxygen species (ROS), which may function as se...

FOCAL POINT AND FOCAL K-PLANE

This paper deals with the basic notions of k-tautimmersions . These notions come from two special cases; that is, tight and taut immersions. Tight and taut based on high and distance functions respectively and their basic notions are normal bundle, endpoint map, focal point, critical normal. We generalize hight and distance functions to cylindrical function and define basic notions of k-taut ...

pp 60 src . kinase , pp 125 FAK , directs SH 2 - dependent Autophosphorylation of the focal adhesion