Zu Y L, Wu F, Gilchrist A, Ai Y, Labadia M E, Huang C K
Department of Pathology, University of Connecticut Health Center, Farmington 06030.
Biochem Biophys Res Commun. 1994 Apr 29;200(2):1118-24. doi: 10.1006/bbrc.1994.1566.
Mitogen-activated protein (MAP) kinase is of central importance in mediating intracellular actions in response to a variety of extracellular stimuli. MAP kinase activated protein (MAPKAP) kinase 2 is one of the two known protein kinases that can be phosphorylated and activated by MAP kinase. Here we present the first complete primary structure of MAPKAP kinase 2 elucidated from a human cDNA sequence. Sequence analysis reveals that MAPKAP kinase 2 is a 370 amino acid protein containing a proline-rich N-terminal region and a well conserved catalytic domain. Northern blot analysis of MAPKAP kinase 2 showed a 4.8 kb mRNA species in HL-60 cells. In addition, we also show the first evidence that recombinant MAPKAP kinase 2 is phosphorylated and activated by MAP kinase in vitro.
丝裂原活化蛋白（MAP）激酶在介导细胞对多种细胞外刺激的细胞内反应中至关重要。MAP激酶活化蛋白（MAPKAP）激酶2是已知的两种可被MAP激酶磷酸化并激活的蛋白激酶之一。在此，我们展示了从人cDNA序列阐明的MAPKAP激酶2的首个完整一级结构。序列分析表明，MAPKAP激酶2是一种由370个氨基酸组成的蛋白质，包含一个富含脯氨酸的N端区域和一个高度保守的催化结构域。对MAPKAP激酶2的Northern印迹分析显示，HL-60细胞中有一个4.8 kb的mRNA种类。此外，我们还首次证明了重组MAPKAP激酶2在体外可被MAP激酶磷酸化并激活。
