SYNPO2 was initially identified as myopodin, a member of the synaptopodin family that contains one PPXY motif and multiple PXXP motifs. It colocalizes with alpha-actinin and is found at the Z-disc and during stress conditions will translocate to the nucleus, suggesting that it is part of signaling pathways in addition to its function as a structural protein. SYNPO2 has been shown to bind to calmodulin, alpha-actinin, and smooth muscle myosin and will stimulate actin polymerization in a calmodulin dependent manner, consistent with its proposed role in organizing the cytoskeleton. While deletion of SYNPO2 has been reported to be highly correlated with the invasiveness of prostate cancers, other reports suggest that down-regulation of SYNPO2 reduces the invasiveness and motility of prostate cancer cells.