Objective： To study the interaction between RET （GDNF receptor） with sucl-bingding neurotrophic target （SNT1） and search for the possible downstream substrates or regulatory proteins of RET, so as to reveal the mechanism of downstream signal transduction of RET. Methods： The RET^IC （intracellular domain of RET） was fused to LexA and the product was used as a DNA-binding domain protein. SNT1, SNT1PTB or SNT1APTB （SNT1 without PTB） was separately fused to B42AD and their ptoducts were used as an activation domain protein. The cotransformants were tested by β-galactosidase activity analysis and leucine medium growth analysis was used to study the interaction between SNT1 and RET. Results： Interaction between RET and SNT1 or SNT1PTB was found in yeast, but that between SNT1APTB and RET was not observed. Conclusion： It is confirmed that RET can interact with SNT1 in yeast, and the interaction may be mediated by PTB domain of SNT1.