The phosphorylation status of IGF2BP2 is crucial for its function as an RNA-binding protein and its interactions with various cellular partners. Zika virus (ZIKV) infection has been shown to decrease the phosphorylation of specific serine residues (Ser162) on IGF2BP2, which may alter its affinity for certain mRNA ligands and protein partners. This reduction in phosphorylation could lead to a decreased interaction with mRNAs that are typically bound by IGF2BP2, such as TNRC6A and PUM2, which are known to be involved in post-transcriptional regulation. Consequently, the remodeling of IGF2BP2's RNA interactome may result in a shift in the stability and translation of these mRNAs, potentially affecting cellular processes that are critical for viral replication. Additionally, the altered phosphorylation state may influence the protein interactome of IGF2BP2, leading to changes in its association with splicing factors and other proteins involved in RNA metabolism. This dynamic interplay between phosphorylation and protein interactions underscores the complexity of host-virus interactions and highlights how ZIKV can manipulate host cellular machinery to favor its replication.