Shapiro P S, Vaisberg E, Hunt A J, Tolwinski N S, Whalen A M, McIntosh J R, Ahn N G
Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309, USA.
J Cell Biol. 1998 Sep 21;142(6):1533-45. doi: 10.1083/jcb.142.6.1533.
The mitogen-activated protein (MAP) kinase pathway, which includes extracellular signal-regulated protein kinases 1 and 2 (ERK1, ERK2) and MAP kinase kinases 1 and 2 (MKK1, MKK2), is well-known to be required for cell cycle progression from G1 to S phase, but its role in somatic cell mitosis has not been clearly established. We have examined the regulation of ERK and MKK in mammalian cells during mitosis using antibodies selective for active phosphorylated forms of these enzymes. In NIH 3T3 cells, both ERK and MKK are activated within the nucleus during early prophase; they localize to spindle poles between prophase and anaphase, and to the midbody during cytokinesis. During metaphase, active ERK is localized in the chromosome periphery, in contrast to active MKK, which shows clear chromosome exclusion. Prophase activation and spindle pole localization of active ERK and MKK are also observed in PtK1 cells. Discrete localization of active ERK at kinetochores is apparent by early prophase and during prometaphase with decreased staining on chromosomes aligned at the metaphase plate. The kinetochores of chromosomes displaced from the metaphase plate, or in microtubule-disrupted cells, still react strongly with the active ERK antibody. This pattern resembles that reported for the 3F3/2 monoclonal antibody, which recognizes a phosphoepitope that disappears with kinetochore attachment to the spindles, and has been implicated in the mitotic checkpoint for anaphase onset (Gorbsky and Ricketts, 1993. J. Cell Biol. 122:1311-1321). The 3F3/2 reactivity of kinetochores on isolated chromosomes decreases after dephosphorylation with protein phosphatase, and then increases after subsequent phosphorylation by purified active ERK or active MKK. These results suggest that the MAP kinase pathway has multiple functions during mitosis, helping to promote mitotic entry as well as targeting proteins that mediate mitotic progression in response to kinetochore attachment.
丝裂原活化蛋白(MAP)激酶途径,包括细胞外信号调节蛋白激酶1和2(ERK1、ERK2)以及MAP激酶激酶1和2(MKK1、MKK2),已知其对于细胞周期从G1期进展到S期是必需的,但其在体细胞有丝分裂中的作用尚未明确确立。我们使用对这些酶的活性磷酸化形式具有选择性的抗体,研究了有丝分裂期间哺乳动物细胞中ERK和MKK的调节。在NIH 3T3细胞中,ERK和MKK在前期早期均在细胞核内被激活;它们在前期到后期定位于纺锤体极,在胞质分裂期间定位于中间体。在中期,活性ERK定位于染色体周边,而活性MKK则明显被排除在染色体之外。在PtK1细胞中也观察到活性ERK和MKK在前期的激活以及纺锤体极定位。活性ERK在动粒处的离散定位在前期早期和前中期明显可见,而在排列在中期板上的染色体上染色减少。从中期板移位的染色体的动粒,或在微管破坏的细胞中的动粒,仍然与活性ERK抗体强烈反应。这种模式类似于针对3F3/2单克隆抗体报道的模式,该抗体识别一种磷酸表位,该表位在动粒与纺锤体附着时消失,并与后期开始的有丝分裂检查点有关(戈尔布斯基和里基茨,1993年。《细胞生物学杂志》122:1311 - 1321)。用蛋白磷酸酶去磷酸化后,分离染色体上动粒的3F3/2反应性降低,然后在用纯化的活性ERK或活性MKK随后磷酸化后增加。这些结果表明,MAP激酶途径在有丝分裂期间具有多种功能,有助于促进有丝分裂进入以及靶向响应动粒附着而介导有丝分裂进展的蛋白质。