Mess1的结构分析和功能研究

Mess1是新近鉴定的 STE2 0家族的蛋白激酶 .对 Mess1的基因表达和蛋白功能进行研究 ,发现其 m RNA在鼠组织中广泛分布 ,但在不同细胞系中表达显著不同 ;结构分析表明 ,Mess1蛋白N端是保守的 STE2 0样激酶催化区 ,C端是高度亲水的酸性调节区 ,包含多个潜在的丝氨酸 /苏氨酸磷酸化调节位点 .哺乳动物细胞表达的 Mess1对 MBP显示出激酶活性 ,并发生自主磷酸化 .Mess1可被砷酸盐应激激活 ,但丝裂原 EGF刺激无活化效应 .表明 Mess1可能在蛋白磷酸化的早期过程中发挥作用 ,介导细胞对严重应激刺激引起的特异性反应 .

Structural Analysis and Functional Study of Mess1

Mess1 is a newly identified protein kinase of STE20 family.This study focused on the gene expression and protein function of Mess1.It was found that the messenger RNA of Mess1 was widely distributed in murine tissues but differentially expressed in various cell lines.A conserved STE20 like kinase catalytic domain located at the amino terminus of Mess1 and a hydrophilic acidic regulatory domain in the carboxyl terminal region of Mess1 contained many potential serine/threonine phosphorylation sites.The Mess1 expressed in mammalian cells showed kinase activity to MBP,as well as autophosphorylation.Mess1 was activated by the stress of arsenite but not activated by mitogenic stimulation of EGF.The similarity to STE20 and the specific activation of Mess1 suggest that Mess1 may function at early stage in phosphorylation events to mediate specific cellular response to extreme stresses.