Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors (1996)

Content Provider	CiteSeerX
Author	Miyamoto, Shingo Teramoto, Hidemi Gutkind, J. Silvio Yamada, Kenneth M.
Abstract	Abstract. Integrins mediate cell adhesion, migration, and a variety of signal transduction events. These integrin actions can overlap or even synergize with those of growth factors. We examined for mechanisms of collaboration or synergy between integrins and growth factors involving MAP kinases, which regulate many cellular functions. In cooperation with integrins, the growth factors EGF, PDGF-BB, and basic FGF each produced a marked, transient activation of the ERK (extracellular signal-regulated kinase) class of MAP kinase, but only if the integrins were both aggregated and occupied by ligand. Transmembrane accumulation of total tyrosine-phosphorylated proteins, as well as nonsynergistic MAP kinase activation, could be induced by simple integrin aggregation, whereas enhanced transient accumulation
File Format	PDF
Journal	J. Cell
Language	English
Publisher Date	1996-01-01
Access Restriction	Open
Subject Keyword	Growth Factor Integrin Aggregation Map Kinase Activation Receptor Tyrosine Kinase Map Kinase Transmembrane Accumulation Integrin Action Many Cellular Function Total Tyrosine-phosphorylated Protein Transient Activation Integrins Mediate Cell Adhesion Transient Accumulation Nonsynergistic Map Kinase Activation Extracellular Signal-regulated Kinase Basic Fgf Signal Transduction Event Growth Factor Egf Simple Integrin Aggregation
Content Type	Text
Resource Type	Article