Symplekin scaffold protein (SYMPK)

Symplekin scaffold protein (SYMPK) is a ubiquitously expressed, evolutionarily conserved nuclear protein functioning as a scaffold for the assembly of polyadenylation machinery during pre-mRNA processing and histone mRNA 3'-end maturation. Structurally, symplekin harbors a HEAT repeat domain supporting protein-protein interactions, and contributes to both the regulation of gene expression and the maintenance of mitotic spindle integrity. While it impacts cellular responses to certain drugs such as paclitaxel via modulation of mitosis, symplekin is not a direct drug target and is chiefly classified as a scaffold/structural protein rather than as a receptor, enzyme, transporter, or transcription factor. It is also found at tight junction plaques in select cell types, supporting possible roles in cell-cell adhesion and signaling.

Other names

SymplekinSYMPKSPKSYMPta1

None established for drugs, as symplekin is not a known pharmacological target. Paclitaxel sensitivity is indirectly modulated through symplekin’s role in mitosis.