Crosstalk between integrin and receptor tyrosine kinase signaling in breast carcinoma progression

Abstract

This review explored the mechanism of breast carcinoma progression by focusing on integrins and receptor tyrosine kinases (or growth factor receptors). While the primary role of integrins was previously thought to be solely as mediators of adhesive interactions between cells and extracellular matrices, it is now believed that integrins also regulate signaling pathways that control cancer cell growth, survival, and invasion. A large body of evidence suggests that the cooperation between integrin and receptor tyrosine kinase signaling regulates certain signaling functions that are important for cancer progression. Recent developments on the crosstalk between integrins and receptor tyrosine kinases, and its implication in mammary tumor progression, are discussed. [BMB reports 2010; 43(5): 311-318]

Tenascin-C-derived Peptide TNIIIA2 Highly Enhances Cell Survival and Platelet-derived Growth Factor (PDGF)-dependent Cell Proliferation through Potentiated and Sustained Activation of Integrin α5β1

“…Increasing evidence indicates that the signaling association between RTKs and integrins induces enhanced activation of intracellular signaling (50,51). Because this synergistic amplification of RTK-mediated signaling events by integrin could maximize cellular responses, the effect of integrins might be especially important in the active proliferation, migration, and invasion of tumor cells (50,51).…”

“…Because this synergistic amplification of RTK-mediated signaling events by integrin could maximize cellular responses, the effect of integrins might be especially important in the active proliferation, migration, and invasion of tumor cells (50,51). Considering the high expression of TN-C in tumor cells and tumor stroma, enhanced RTK signaling by TN-C needs to be investigated in relation to the role it plays in tumor initiation and progression.…”

SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration

“…As such, an accumulation of evidence correlates an invasive and metastatic state with the dysregulation of signals involved in cell migration [5,7,9,15,19,35,37]. For example, interactions between αvβ3, α5β1 and α6β4 and receptor tyrosine kinases (RTKs) such as ErbB2 and EGFR have been shown to facilitate the proliferation and migration of tumor cells independently of positional constraints in breast cancer [38,39]. Additionally, aberrant trafficking of integrins to the leading edge has been documented to activate the matrix-degrading proteases such as matrix metalloproteinases (MMPs) and plasmin, required for degradation of the ECM and subsequent cell invasion [38,40].…”

Fungal adhesion protein guides community behaviors and autoinduction in a paracrine manner

“…The multifunctionalities of Cfl1 resemble those of matrix proteins found in higher multicellular eukaryotes. These matrix proteins regulate intercellular communication via a crosstalk through growth factors that bind to receptors with intrinsic tyrosine kinase activity, or through their direct interactions with some members of this receptors family (8,(29)(30)(31)(32). The coexistence of SIGC and the receptor tyrosine kinase domain (Pfam accession no.…”