Clathrin, made up of the heavy- and light-chains, constitutes one of the most abundant protein in vesicles involved in intracellular protein trafficking and endocytosis. YPR129W, which encodes RGG-motif containing translation repressor was identified as a part of multi-gene construct (SCD6) that suppressed clathrin deficiency. However, the contribution of YPR129W alone in suppressing clathrin deficiency has not been documented. In this study we identify YPR129W as a necessary and sufficient gene in a multigene construct SCD6 that suppresses clathrin deficiency. Importantly, we identify cytoplasmic RGG-motif protein encoding gene PSP2 as a novel suppressor of clathrin deficiency. Three other RGG-motif protein encoding genes SBP1, DED1 and GBP2 do not suppress clathrin deficiency. DHH1, a DEAD-box RNA helicase with translation repression activity also fails to rescue clathrin deficiency. α-factor secretion assay suggests that suppression of clathrin deficiency by SCD6 and PSP2 is not mediated by the rescue of the trans-Golgi network (TGN) protein sorting defect observed in the absence of CHC1. Detailed domain analysis of the two suppressors reveals that the RGG-motif of both Scd6 and Psp2 is important for suppressing clathrin deficiency. Additionally, the Lsm domain deletion as well as the arginine to alanine mutation in the arginine methylation defective (AMD) mutant render Scd6 defective in suppressing clathrin deficiency. Overall based on our results using SCD6 and PSP2 proteins, we identify a novel role of RGG-motif in suppressing clathrin deficiency. Since both the suppressors are RNA-binding granule-resident proteins, this study opens an exciting avenue for exploring the connection between clathrin function and cytoplasmic RNA metabolism.