p38分子与TAB1分子的相互作用及其自我磷酸化研究进展

Interaction between p38 and TAB1 and p38 autophosphorylation:research advances

一直以来,炎症的发生、发展受到人们的广泛关注。自1994年MAPK家族的p38分子被首次报道以来,大量相应的研究逐渐确立了p38分子在炎症调控中的重要作用。TAB1是MAP3K家族成员TAK1的结合蛋白,近来发现它能与p38发生相互作用并使p38自我磷酸化。最近,关于TAB1与p38相互作用的研究越来越多,在分子、细胞和组织器官层面都有新的发现,而且以TAB1和p38相互作用为靶向也成为新型p38抑制剂研究的新策略。

The mechanisms underlying the initiation and development of inflammation have been the focus of intensive studies. Since its initial identification in 1994, p38 MAPK has been gradually established to be a central regulator of inflammation, TAB1 was originally identified as a binding protein of TAK1, which belongs to MAP3Ks. Recently, TAB1 was found to be able to interact with p38, resulting in the autophosphorylation of p38. More and more publications have revealed that the interaction between p38 and TAB1 is of physiological or pathological significance at the level of molecules, cells or tissue. Consequently, p38 autophosphorylation has become a potential target for designing novel inhibitors of the p38 MAPK pathway.