The LIM domain of PDLIM2 directly interacts with some important signalling molecules, including kinases, receptors, and phosphatases.19, 20 It also mediates the ubiquitination of nuclear p65.32 In addition, this domain is involved in regulating the cellular distribution of PDLIM2.33 Deletion of this domain results in increased accumulation of PDLIM2 in the cytoplasm and nucleoplasm, and reduced protein level in the nuclear matrix.33 These findings suggest that the expression of exon 1‐10 might be critical to maintaining the normal function of PDLIM2 in ESCC. This evidence concerns the gene PDLIM2 and esophageal squamous cell carcinoma.