ERK7是细胞外信号调节激酶家族中的新成员.尽管ERK7激酶的活化环上含有ERK家族成员共有的TEY基序,但是在活化上与其它ERK家族成员截然不同,ERK7无需典型活化ERK的细胞外刺激或JNK和p38激酶活化物而发生自磷酸化并足以使其在缺乏上游激酶时发生活化,且发现ERK7中非激酶结构域的C端区域调节其结构性活化、核定位、生长抑制.此外,N端的20个氨基酸作为ERK7降解的首要决定因素调节ERK7的表达.新近研究表明ERK7与乳腺肿瘤、神经元分化、胚胎发生密切相关.本文就ERK7的结构特性活化、调控及功能等作了综述.
ERK7 is a new member of the extracellular signal-regulated kinase(ERK) family. Although ERK7 shares a TEY motif in the activation loop of the kinase domain with other members of ERK family, its activation is completely different from other ERKs. Extracellular stimuli that typically activate ERK and common activators of both c-Jun N-terminal kinase (JNK) and p38 kinase are not necessary for ERK7 activation. In the absence of upstream kinases, ERK7 autophosphorylation is sufficient for its activation. And the C-terminal tail of ERK7, not the kinase domain, regulates its constitutive activation, nuclear location and growth inhibition. Moreover, N-terminal 20 amino acids of the kinase domain, as the primary determinant of ERK7 degradation, regulate ERK7 expression. Recent studies indicate that ERK7 is frequently associated with breast cancer, neuronal differentiation and embryogenesis. This review focuses on constitutive activation, activating regulation and functions of ERK7.