SUMOylation is essential for Sirt2 tumor-suppressor function in neuroblastoma
Autor: | Renjie Cai, Ming Xu, Ci Xu, Qiang Fan, Haihua Yuan, Wenmei Lu, Danhong Wu, Biying Chen, Qian Wang |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
Cancer Research Cell signaling Original article Lysine SUMO protein Gene Expression SIRT2 medicine.disease_cause lcsh:RC254-282 p38 Mitogen-Activated Protein Kinases Cell Line 03 medical and health sciences Neuroblastoma Mice 0302 clinical medicine Sirtuin 2 Cell Signaling Cell Movement medicine Animals Humans Cell Proliferation Sirt2 Chemistry TOR Serine-Threonine Kinases Tumor Suppressor Proteins Sumoylation Acetylation lcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogens medicine.disease Prognosis Xenograft Model Antitumor Assays Cell biology Disease Models Animal 030104 developmental biology 030220 oncology & carcinogenesis Cancer cell Carcinogenesis Protein Processing Post-Translational Proto-Oncogene Proteins c-akt Signal Transduction |
Zdroj: | Neoplasia (New York, N.Y.) Neoplasia: An International Journal for Oncology Research, Vol 23, Iss 1, Pp 129-139 (2021) |
ISSN: | 1476-5586 1522-8002 |
Popis: | SUMOylation is an important post-translational modification that participates in a variety of cellular physiological and pathological processes in eukaryotic cells. Sirt2, a NAD+-dependent deacetylase, usually exerts a tumor-suppressor function. However, the role of SUMOylation in cancer cells is not fully known. In this study, we found that SUMOylation can occur in the Sirt2 protein at both lysine 183 and lysine 340 sites. SUMOylation did not affect Sirt2 localization or stability but was involved in P38-mTORC2-AKT cellular signal transduction via direct deacetylation on a new substrate MAPK/P38. SUMOylation-deficient Sirt2 lost the capability of suppressing tumor processes and showed resistance to the Sirt2-specific inhibitor AK-7 in neuroblastoma cells. Here, we revealed the important function of Sirt2-SUMOylation, which is closely associated with cellular signal transduction and is essential for suppressing tumorigenesis in neuroblastoma. |
Databáze: | OpenAIRE |
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