Endoglycan (PODXL2) is proteolytically processed by ADAM10 (a disintegrin and metalloprotease 10) and controls neurite branching in primary neurons

Cell adhesion is tightly controlled in multicellular organisms, for example, through proteolytic ectodomain shedding of the adhesion-mediating cell surface transmembrane proteins. In brain, proteins required nervous system development and function, but only a few has been studied detail mammalian brain. One such protein endoglycan (PODXL2), which belongs to CD34-family highly glycosylated sialomucins. Here, we demonstrate that broadly expressed developing mouse brains proteolytically shed vitro neurons vivo brains. Endoglycan primary was mediated by protease disintegrin metalloprotease 10 (ADAM10), not its homolog ADAM17. Functionally, deficiency reduced branching neurites extending from vitro, whereas deletion ADAM10 had opposite effect increased neurite branching. Taken together, our study discovers function branching, establishes as an substrate suggests cleavage may contribute