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It has been reported that the dynamic interplay between O-GlcNAcylationand O-phosphorylation is responsible for altering the activity or localizationof heat-shock proteins. The aim of this study was to determine whether dynamicinterplay between O-GlcNAcylation and O-phosphorylation of HSP27 in hepatocellularcancer (HCC) cells affect its entry into the nucleus. We demonstrate that theentry of HSP27 into the nucleus correlated with its phosphorylation through transfectingHCC cells with plasmids coding for wild-type HSP27 (HSP27-WT), its non-phosphorylatable(HSP27-3A) and pseudophosphorylated (HSP27-3D) mutants, however, not all of theendogenous or exogenous nuclear HSP27 was modified by phosphorylation. We observedthat HSP27 was modified with O-GlcNAc glycosylation in HCC cells and report thatat conserved Ser residues of HSP27, alternative phosphorylation and O-GlcNAc modificationcan be predicted by the YinOYang 1.2 method. Furthermore, after P79350 or combinedSB203580 and PUGNAc treatment, increased nuclear import of HSP27-WT and HSP27-3Dimplied that the entry of HSP27 into the nucleus was not only correlated withphosphorylation, but also with O-GlcNAc glycosylation. Collectively, O-GlcNAcylationof HSP27 in HCC cells may be a novel regulatory mode of HSP27 function, particularlyfor its entry into the nucleus. Crosstalk or interplay between glycosylation andphosphorylation of HSP27 could regulate its subcellular localization and biologicalfunctions in liver cancer.

Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation