원문정보
초록
영어
O-GlcNAc modification is glycosylation that occurs on Serine and Threonine residues of proteins located in nucleus and cytoplasm. O-GlcNAcylation regulates various cellular events including transcription, translation, cell death and cell proliferation as cellular nutrient sensor. It also has important roles in development processes such as neurogenesis, osteogenesis, adipogenesis and myogenesis. Although some roles and molecular mechanism of O-GlcNAcylation in various development process has been studied, the relationship between O-GlcNAcylation and muscle differentiation is not clearly established. We confirm that physiological conditions to regulate cellular O-GlcNAc level as well as O-GlcNAcase inhibitor treatment influenced the myogenin expression and myogenesis. We also confirm that this results was shown in mouse model system. We demonstrate that these phenomenons result from O-GlcNAc of Mef2c. Furthermore, we identify the 3 O-GlcNAc sites in Mef2c and find that one of these site has role regulating the DNA binding affinity with promoter of myogenin. Our results suggest that one specific O-GlcNAc site of Mef2c is closely associated with muscle differentiation through the regulation of myogenin transcription.