Syntrophins are scaffold proteins that can bind several signaling molecules and localize them to the plasma membrane. We demonstrate here that in neuroblastoma SH-SY5Y cells, brain-specific ...gamma1-syntrophin binds the neurotrophic factor gamma-enolase through its PDZ domain, and translocates it to the plasma membrane, as shown by immunoprecipitation, surface plasmon resonance, fluorescence colocalization and flow cytometry. Extensive colocalization of gamma1-syntrophin and gamma-enolase was observed in neurite growth cones in differentiated SH-SY5Y cells. Silencing of the gamma1-syntrophin gene by RNA interference significantly reduced the re-distribution of gamma-enolase to theplasma membrane and impaired its neurotrophic effects. We demonstrated thatan intact C-terminal end of gamma-enolase is essential for its gamma1-syntrophin-assisted trafficking. The cleavage of two amino acids at C-terminal end of gamma-enolase by the carboxypeptidase cathepsin X prevents binding with the gamma1-syntrophin PDZ domain. Collectively, these data demonstrate that gamma1-syntrophin participates in gamma-enolase translocation towardsthe plasma membrane, a pre-requisite for its neurotrophic activity. By disrupting this gamma1-syntrophin-guided subcellular distribution, cathepsin X reduces gamma-enolase-induced neurotrophic signaling.
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