Decorin-binding receptors and partners (DCN-BRP)

Decorin-binding receptors and partners comprise a diverse array of cell surface signaling molecules and extracellular matrix (ECM) components that interact with the small leucine-rich proteoglycan (SLRP) decorin. This interactome is primarily defined by decorin's role as a "pan-receptor tyrosine kinase (RTK) inhibitor," where it binds to and antagonizes key receptors such as the epidermal growth factor receptor (EGFR), hepatocyte growth factor receptor (Met), and vascular endothelial growth factor receptor 2 (VEGFR2) [1.3.1, 1.5.1]. Upon binding, decorin triggers receptor dimerization, internalization via caveolae, and subsequent lysosomal degradation, thereby suppressing oncogenic signaling pathways [1.3.4, 1.5.1]. Furthermore, decorin acts as a biological reservoir or "sink" for various growth factors, most notably transforming growth factor-beta (TGF-beta), which allows it to modulate fibrotic responses and immune signaling [1.2.1, 1.3.4]. In the tumor microenvironment, these interactions collectively inhibit cell proliferation, angiogenesis, and metastasis while promoting tumor cell mitophagy and endothelial cell autophagy [1.1.3, 1.2.3]. Therapeutic strategies targeting this network include recombinant human decorin and targeted fusion proteins like CAR-decorin, which are being investigated for their potential to treat solid tumors and chronic fibrotic conditions [1.1.3, 1.2.1]. However, the broad nature of these interactions presents challenges, including potential pro-inflammatory effects through Toll-like receptors (TLR2/4) and the risk of interfering with normal tissue repair and growth factor homeostasis [1.2.2, 1.4.1].

Other names

Decorin interactomeDecorin-binding partnersPan-receptor tyrosine kinase inhibitor targetsDCN-binding receptorsDecorin-binding proteins

Competitive inhibition of growth factor binding, induction of receptor internalization and degradation, sequestration of growth factors (e.g., TGF-beta), and induction of Peg3-dependent autophagy.