Leucine-rich repeat and fibronectin type-III domain-containing protein 4 (LRFN4)

Leucine-rich repeat and fibronectin type-III domain-containing protein 4 (LRFN4) is a type I transmembrane glycoprotein primarily classified within the fibronectin type III domain-containing and immunoglobulin superfamily proteins. LRFN4 is expressed in neural tissues—where it modulates synapse formation and maturation—and in diverse cancer and hematopoietic cell lines, particularly upregulated during macrophage differentiation[1]. It plays a critical role in regulating cell motility by modulating transendothelial migration and actin cytoskeleton reorganization via complexes with proteins such as 14-3-3 and NCK1. In cancer biology, LRFN4 promotes proliferation, migration, and resistance to apoptosis, partly by influencing cyclin D1, CDK4, and caspase-3 activity. These functions implicate LRFN4 as a potential therapeutic target and putative biomarker for several cancers, with a notable role in modulating the tumor immune microenvironment by affecting immune cell infiltration and polarization[1][2][3][4].

Other names

SALM3FIGLER6MGC3103fibronectin type IIIimmunoglobulin and leucine rich repeat domains 6LRFN4Leucine-rich repeat and fibronectin type-III domain-containing protein 4

No established drugs known to target LRFN4 directly; potential mechanisms based on hypothetical inhibition may involve modulation of cell migration, reduction of cell proliferation, and increase of apoptosis in cancer cells via disruption of actin cytoskeleton reorganization and downregulation of cyclin D1/CDK4/caspase-3 pathways[2].