Function Of FHL1 Acetylation In Tumor Development

Normal cells physiological functions depend on a certain level of protein acetylation modification. Abnormal protein acetylation modification can lead tumor development. Stable protein acetylation level is actually the dynamic balance between acetyltransferase HAT and deacetylase HDAC active competition. The imbanlance of HAT and HDAC will lead to the transformation of normal cells into cancer. The present study showed that there is a low acetylation modification in many tumor cells, and a growing body of evidence indicated that acetylation modification disorders are closely related to many diseases. As a result, reversing abnormal acetylation status is of vital significance.Tumor-suppressor protein FHL1 belongs to the family of FHL. Previous studies have found that FHL1 regulated transforming growth factor beta (TGF beta) Signaling pathway and estrogen receptor (ER) Signaling pathway to inhibit the growth of liver cancer cells and breast cancer cells. Previous study indicated that FHL1 was down-regulated in a variety of tumor tissues, but the mechanism still unknown.In this study, we found that FHL1 was acetylated at K157 and K278. We further identified that p300 is acetyltransferase and HDAC6 is deacetylase of FHL1. Acetylation of FHL1 inhibited its ubiquitination by E3 ligase E6AP, and FHL1 inhibited HCC growth depend on its acetylation. Acetylation of FHL1 is downregulated in HCC tumor. FHL1 Acetylation is negative correlated with HDAC6 and E6AP in HCC patients, and FHL1 Acetylation have a great prognostic evaluation in clinical staging.In conclusion, FHL1 acetylation plays an important role in inhibiting tumor progress. Therefore, further study of FHL1 acetylation modification will make mechanism of FHL1 regulating tumor development much more clear, and provide clue for the clinical treatment strategy.