mProX™ Human MAP3K20 Stable Cell Line

Yang, Youzhualamu. et al. "Epigenomics Analysis of the Suppression Role of SIRT1 via H3K9 Deacetylation in Preadipocyte Differentiation" International journal of molecular sciences, 2023.
Sirtuin 1 (SIRT1) is a deacetylase enzyme that plays a crucial role in regulating cellular functions such as metabolism, DNA repair, and stress response. This enzyme has been linked to various age-related diseases and has shown potential as a therapeutic target. Recent studies have also found that SIRT1 activity can be modulated by small molecule activators, making it a promising avenue for drug development. Understanding the mechanisms and implications of SIRT1 deacetylase activity could provide valuable insights into disease prevention and treatment.
Yang, Youzhualamu. et al. "Epigenomics Analysis of the Suppression Role of SIRT1 via H3K9 Deacetylation in Preadipocyte Differentiation" International journal of molecular sciences, 2023.
Pubmed: 37511041   DOI: 10.3390/ijms241411281

Stonadge, Amy. et al. "Myofibrillar myopathy hallmarks associated with ZAK deficiency." Human molecular genetics, 2023.
The ZAK gene encodes two distinct kinases, ZAKα and ZAKβ, and their homozygous loss-of-function mutations lead to congenital muscle disease. ZAKβ is the only isoform expressed in skeletal muscle and is activated by muscular contraction and cell compression. However, the specific substrates and mechanism by which ZAKβ responds to mechanical stress in skeletal muscle have yet to be determined. To better understand the underlying pathology, ZAK-deficient cell lines, zebrafish, mice, and a human biopsy were utilized. The ZAK-deficient mice and zebrafish showed only mild symptoms. Further analysis of comparative histopathology data in these mice suggests that aging and physical activity are major factors driving the pathology, with ZAKβ playing a relatively minor role in myoblast fusion and muscle regeneration. A phosphoproteomics assay, along with immunofluorescence analysis of muscle sections from both mice and the human biopsy, revealed the presence of SYNPO2, BAG3, and Filamin C (FLNC) as potential ZAKβ substrates. Further investigation showed that ZAKβ may play a critical role in the turnover of FLNC, as evidenced by abnormal accumulations of FLNC and BAG3 in highly reactive muscle fibers. Additionally, mice subjected to increased mechanical stress showed exacerbated accumulations of FLNC, highlighting the importance of ZAKβ signaling in regulating FLNC turnover and maintaining normal physiological response to mechanical stress. The authors propose that the accumulation of mislocalized FLNC and BAG3 in highly active fibers contributes to the pathogenic mechanism of ZAK deficiency.
Stonadge, Amy. et al. "Myofibrillar myopathy hallmarks associated with ZAK deficiency." Human molecular genetics, 2023.
Pubmed: 37427997   DOI: 10.1093/hmg/ddad113