Human Protein Tyrosine Phosphatase Receptor Type M (PTPRM) Protein

Background

PTPRM, also known as RPTPμ, is a receptor-like protein tyrosine phosphatase that regulates cell-cell adhesion, signaling, and growth suppression. Structurally, PTPRM contains extracellular Ig-like and fibronectin type III domains, a transmembrane domain, and two intracellular phosphatase domains. PTPRM mediates homophilic binding, meaning it interacts with other PTPRM molecules on adjacent cells to facilitate cell-cell adhesion. It plays essential roles in maintaining tissue architecture, especially in epithelial and endothelial cells. PTPRM interacts with cadherins and catenins to regulate cell adhesion and cytoskeletal organization. Loss or downregulation of PTPRM is associated with cancer progression and metastasis due to disrupted cell adhesion. Its regulatory role in neuronal guidance and tissue integrity also highlights its importance in development and cancer biology.