MEGF10 is a member of the multiple epidermal growth factor-like domains protein family. MEGF10 is a type I transmembrane protein that consists of 15 EGF-like domains in its extracellular region and is the mammalian homolog of Draper (a Drosophila phagocytosis apoptotic cell receptor)¹.

MEGF10 is a mediator for apoptotic cell phagocytosis by central nervous system (CNS) macrophages- microglia and astrocytes, through binding with high affinity to C1q, an eat-me signal, that binds phosphatidylserine expressed on the surface of apoptotic cells². Also necessary for astrocyte-dependent apoptotic neuron clearance in the developing cerebellum².  In this regard, MEGF10 works alongside other phagocytic receptors expressed in astrocytes or microglia such as the tyrosine kinase receptors MERTK and AXL, the G-protein coupled receptors Bai1 and GPR56 or the TREM2 receptor³.

MEGF10 is involved in the uptake of amyloid-β peptide (Aβ42) in the brain. Alzheimer's disease (AD) is characterized by extracellular accumulation of senile plaques, the major component of which is the amyloid-β peptide (Aβ), and the presence of neurofibrillary tangles. MEGF10 as a functional receptor that mediates the uptake of amyloid-β peptide will help elucidate the molecular mechanisms of amlyoid-β clearance in Alzheimer's disease^1,4.

MEGF10 is also an essential factor in the regulation of myogenesis. It controls the balance between skeletal muscle satellite cells proliferation and differentiation through regulation of the notch signaling pathway⁵. In fact, mutations in the MEGF10 gene are the underlying cause of Early-onset myopathy, areflexia, respiratory distress, and dysphagia (EMARDD), a lethal congenital myopathy characterized by hypotonia with respiratory distress ^5,6.