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Updated: May 4, 2026

Tension Gauge Tether Probes for Quantifying Growth Factor Mediated Integrin Mechanics and Adhesion
Published on: February 11, 2022
Fibronectin at select sites binds multiple growth factors and enhances their activity: expansion of the collaborative
1Department of Biochemistry, Stony Brook University, Stony Brook, New York, USA.
Abstract:
Intensive research has demonstrated that extracellular matrix (ECM) molecules and growth factors (GF) collaborate at many different levels. The ability of ECM to modulate GF signals has important implications in tissue formation and homeostasis as well as novel therapies for acute and chronic wounds. Recently, a number of GF-binding sites was identified in fibronectin (FN) and was shown to provide another layer of regulation on GF signaling. Here, we review these new findings on FN interaction with GF in the context of general ways ECM molecules regulate GF signaling.
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