Toward understanding the glucose- -cells from analysis of glucose-responsive MafA kinase

我们发现GSK3和MaCK对MafA转录因子的多重磷酸化事件是通过增强dna结合和Beta2结合来实现其在β细胞中的功能所必需的。此外，我们证明了MafA磷酸化降低是II型糖尿病β细胞功能障碍的主要原因之一。我们还发现了一种小分子抑制剂，可以模拟β细胞中的内源性MafA去磷酸化。这些发现有助于了解β细胞功能和功能障碍的分子机制。

We have found that multiple phosphorylation events on MafA transcription factor by GSK3 and MaCK are required for its function in β-cells through enhancing DNA-binding and Beta2 association. Furthermore, We demonstrated that decreased MafA phosphorylation is one of the main causes of β-cell dysfunction in type II diabetes. We also identified a small molecule inhibitor that mimics endogenous MafA de-phosphorylation in β-cells. These findings led to understanding of molecular mechanisms of β-cell function and dysfunction.