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PDZ and LIM domain protein 2 (PDLIM2) is a cytoskeletal adapter protein containing an N-terminal PDZ domain and a C-terminal LIM domain, encoded by the *PDLIM2* gene on chromosome 8p21 in humans[1][2][3]. PDLIM2 localizes to the nucleus and cytoplasm, where it links cytoskeletal actin networks with diverse intracellular signaling pathways, particularly by regulating the activity and stability of transcription factors such as NF-κB, STATs, and β-catenin[1][2]. Its functions include organizing the cytoskeleton, controlling cell polarization, modulating cell adhesion and migration, and tuning immune responses. PDLIM2 acts largely as a tumor suppressor by promoting degradation of pro-oncogenic transcription factors via a ubiquitin-like mechanism, but in certain cancers, it may support tumor growth and metastasis. Its expression levels and localization are tightly regulated, and aberrant PDLIM2 function from genetic or epigenetic alterations has been linked to cancer and inflammation, making it an emerging target and biomarker in oncology[1][2][3].
For hypothesized or future drugs: modulation of transcription factor turnover (e.g., NF-κB/STAT3 degradation via ubiquitination), restoration or inhibition of PDLIM2 function to influence tumor cell sensitivity to immune surveillance[1].
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