Persephin has been found to be less potent than other members of the GDNF family. It has been found to support the survival and morphological differentiation of tyrosine hydroxylase immunoreactive neurons, although less so than both GDNF and neurturin. The mRNA levels of persephin in developing neurons has been low compared to other neurotrophic factors, but relatively higher levels of persephin mRNA have been found in embryonic neurons.
Similarly to the other members of the GDNF family of ligands, persephin uses a receptor that consists of the tyrosine kinase signaling component Ret and a unit of glycosylphosphatidylinsitol (GPI)-anchored receptor (GFRα). Persephin specifically binds to GFRα4.
Persephin acts on both neurons in the CNS and PNS, but also has the ability to act as a renal ramogen.