In this study, a participation of all four KH-domains of the IGF2BP paralogues in the association with RNA-substrates ACTB and MYC was determined by comparative in vitro filter binding studies. Continuative analyses showed that all KH-domains of IGF2BP paralogues are important functional units regarding cytoplasmic localization, protein-association, oligomerization and organization of IGF2BP proteins in stress granules. Using the SELEX process, pyrimidine rich RNA-motifs could be selected for IGF2BP proteins. By analyses concerning protein composition of ZBP1-RNPs, further ZBP1 interactors in m- and YRNPs were identified. For IGF2BP2, a role in glucose metabolism was recently postulated. The hypothesis could be reinforced by this study, showing that overexpression of GFP-IGF2BP2 compared to GFP alone led to increased glucose uptake in U2OS cells and was accompanied by elevated glycogen levels.