β1,6 GlcNAc branches-modified PTPRT attenuates its activity and promotes cell migration by STAT3 pathway.

摘要: Receptor-like protein tyrosine phosphatases (RPTPs) are type I transmembrane glycoproteins with N-glycans whose catalytic activities regulated by dimerization. However, the intrinsic mechanism involved in dimerizing processes remains obscure. In this study, receptor phosphatase rho (PTPRT) is identified as a novel substrate of N-Acetylglucosaminyltransferase V (GnT-V). We show that addition β1,6 GlcNAc branches on PTPRT prolongs PTPRT's cell-surface retention time. GnT-V overexpression enhances galectin-3's and promotes dimerization mediated galectin-3. Increased subsequently reduces activity dephosphorylation signal transducer activator transcription 3 (STAT3) at residue 705 (pY705 STAT3), then accumulated pY705 STAT3 translocates into nucleus. Collectively, these findings provide an insight molecular which cell migration, suggesting accumulation branched decreases its activity, resulting enhanced migratory capacity.