SIRT2 is a mammalian member of the Sirtuin family of NAD(+)-dependent protein deacetylases. The tyrosine kinase Src is involved in a variety of cellular signaling pathways, leading to the induction of DNA synthesis, cell proliferation, and cytoskeletal reorganization. The function of SIRT2 is modulated by post-translational modifications; however, the precise molecular signaling mechanism of SIRT2 through interactions with c-Src has not yet been established. In this study, we investigated the potential regulation of SIRT2 function by c-Src. We found that the protein levels of SIRT2 were decreased by c-Src, and subsequently rescued by the addition of a Src specific inhibitor, SU6656, or by siRNA-mediated knockdown of c-Src. The c-Src interacts with and phosphorylates SIRT2 at Tyr104. c-Src also showed the ability to regulate the deacetylation activity of SIRT2. Investigation on the phosphorylation of SIRT2 suggested that this was the method of c-Src-mediated SIRT2 regulation.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.bbrc.2014.06.117 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
High cumulative glucocorticoid dose is associated with increased levels of inflammation-related mediators in active rheumatoid arthritis.
Front Immunol
January 2025
Department of Immunology, Faculty of Medicine and Dentistry, Palacký University Olomouc and University Hospital, Olomouc, Czechia.
Introduction: Glucocorticoids (GCs) are widely used as a treatment for rheumatoid arthritis (RA), leading to high cumulative doses in long-term treated patients. The impact of a high cumulative GC dose on the systemic inflammatory response in RA remains poorly understood.
Methods: We investigated long-treated patients with RA (n = 72, median disease duration 14 years) through blood counts and the serum levels of 92 inflammation-related proteins, and disease activity was assessed using the Simple Disease Activity Index (SDAI).
SIRT2 Promotes NLRP3-Mediated Microglia Pyroptosis and Neuroinflammation via FOXO3a Pathway After Subarachnoid Hemorrhage.
J Inflamm Res
December 2024
Department of Neurosurgery, Nanjing Drum Tower Hospital, Affiliated Hospital of Medical School, Nanjing University, Nanjing, People's Republic of China.
Purpose: This study primarily elucidating the specific mechanism of SIRT2 on neuroinflammation and microglial pyroptosis in a mouse model of SAH.
Patients And Methods: CSF were collected from 57 SAH patients and 11 healthy individuals. C57BL/6 mouse SAH model was established using prechiasmatic cistern blood injection and the in vitro hemoglobin (Hb) stimulation microglia model.
Ribose-induced advanced glycation end products reduce the lifespan in Drosophila melanogaster by changing the redox state and down-regulating the Sirtuin genes.
Biogerontology
December 2024
Neural Developmental Biology Lab, Department of Life Science, NIT Rourkela, Rourkela, 69008, India.
Advanced Glycation End (AGE) products are one such factor that accumulates during aging and age-related diseases. However, how exogenous AGE compounds cause aging is an area that needs to be explored. Specifically, how an organ undergoes aging and aging-related phenomena that need further investigation.
View Article and Find Full Text PDFDoxorubicin inhibits SIRT2 and NF-kB p65 phosphorylation in Brest cell-line cancer.
Biochem Biophys Res Commun
January 2025
Biotechnology Research Center (CRBt), Ali Mendjli, Constantine, 25000, Algeria. Electronic address:
Doxorubicin (DOXO) is a widely used anti-cancer agent, yet the precise mechanism underlying the induction of tumor cell death remains unclear. This study aimed to elucidate new mechanisms by which doxorubicin induces apoptosis in the EMT6 mouse breast carcinoma cell line. The role of doxorubicin was assessed using the XTT assay.
View Article and Find Full Text PDFSIRT2 Inhibition by AGK2 Promotes Perinuclear Cytoskeletal Organisation and Reduces Invasiveness of MDA-MB-231 Triple-Negative Breast Cancer Cells in Confined In Vitro Models.
Cells
December 2024
Department of Biosciences, Durham University, Durham DH1 3LE, UK.
Triple-negative breast cancer (TNBC) is a highly aggressive breast cancer subtype characterised by the absence of targetable hormone receptors and increased metastatic rates. As nuclear softening strongly contributes to TNBC's enhanced metastatic capacity, increasing the nuclear stiffness of TNBC cells may present a promising therapeutic avenue. Previous evidence has demonstrated the ability of Sirtuin 2 (SIRT2) inhibition to induce cytoskeletal reorganisation, a key factor in regulating nuclear mechanics.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!