The phytohormone abscisic acid (ABA) plays critical roles in abiotic stress responses and plant development.In germinating seeds,the phytochrome-associated protein phosphatase,FyPP3,negatively regulates ABA signaling by dephosphorylating the transcription factor ABI5.However,whether and how FyPP3 is regulated at the posttranscriptional level remains unclear.Here,we report that an asparagine-rich protein,NRP,interacts with FyPP3 and tethers FyPP3 to SYP41/61-positive endosomes for subsequent degradation in the vacuole.Upon ABA treatment,the expression of NRP was induced and NRP-mediated FyPP3 tuover was accelerated.Consistently,ABA-induced FyPP3 tuover was abolished in an nrp null mutant.On the other hand,FyPP3 can dephosphorylate NRP in vitro,and overexpression of FyPP3 reduced the half-life of NRP in vivo.Genetic analyses showed that NRP has a positive role in ABA-mediated seed germination and gene expression,and that NRP is epistatic to FyPP3.Taken together,our results identify a new regulatory circuit in the ABA signaling network,which links the intracellular trafficking with ABA signaling.