Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2 (ELFN2)

Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2 (ELFN2) is a multifunctional, extracellularly located protein involved in synaptic membrane adhesion, and modulation of protein phosphatase 1 activity. In the nervous system, ELFN2 regulates the formation and specialization of synapses in the retina, specifically facilitating interactions between photoreceptors and ON bipolar cells through transsynaptic recruitment of key neurotransmitter receptors (such as mGluR6). In oncogenic settings, ELFN2 shows context-dependent roles: its overexpression, often resulting from promoter hypomethylation or epigenetic regulation (involving lncRNA LINC00470 or miRNAs such as miR-101), is associated with increased tumor cell autophagy, proliferation, and potential for cancer progression in glioblastoma, gastric cancer, and endometrial carcinoma. ELFN2 may serve as a prognostic marker in these cancers and has been linked to stress fracture risk in genetic studies. It is classified as a regulatory subunit of protein phosphatase 1 (PPP1R), with additional fibronectin type III domains, and is considered a potential therapeutic target in both neurology and oncology.

Other names

Protein phosphatase 1 regulatory subunit 29ELFN2KIAA1904LRRC62PPP1R29dJ63G5.3Leucine-rich repeat-containing protein 62Extracellular leucine-rich repeat and fibronectin type III containing 2DJ63G5.3 (putative Leucine rich protein)

Inhibition of protein phosphatase 1 (PP1) activity; Interaction with Aurora kinase A (AurkA) and eukaryotic translation initiation factor 2 alpha (eIF2α), modulating autophagy and cell proliferation pathways