Ma H, Gamper M, Parent C, Firtel R A
Department of Biology, Center for Molecular Genetics, University of California, San Diego, La Jolla 92093-0634, USA.
EMBO J. 1997 Jul 16;16(14):4317-32. doi: 10.1093/emboj/16.14.4317.
We have identified a MAP kinase kinase (DdMEK1) that is required for proper aggregation in Dictyostelium. Null mutations produce extremely small aggregate sizes, resulting in the formation of slugs and terminal fruiting bodies that are significantly smaller than those of wild-type cells. Time-lapse video microscopy and in vitro assays indicate that the cells are able to produce cAMP waves that move through the aggregation domains. However, these cells are unable to undergo chemotaxis properly during aggregation in response to the chemoattractant cAMP or activate guanylyl cyclase, a known regulator of chemotaxis in Dictyostelium. The activation of guanylyl cyclase in response to osmotic stress is, however, normal. Expression of putative constitutively active forms of DdMEK1 in a ddmek1 null background is capable, at least partially, of complementing the small aggregate size defect and the ability to activate guanylyl cyclase. However, this does not result in constitutive activation of guanylyl cyclase, suggesting that DdMEK1 activity is necessary, but not sufficient, for cAMP activation of guanylyl cyclase. Analysis of a temperature-sensitive DdMEK1 mutant suggests that DdMEK1 activity is required throughout aggregation at the time of guanylyl cyclase activation, but is not essential for proper morphogenesis during the later multicellular stages. The activation of the MAP kinase ERK2, which is essential for chemoattractant activation of adenylyl cyclase, is not affected in ddmek1 null strains, indicating that DdMEK1 does not regulate ERK2 and suggesting that at least two independent MAP kinase cascades control aggregation in Dictyostelium.
我们已经鉴定出一种在盘基网柄菌中正常聚集所必需的丝裂原活化蛋白激酶激酶(DdMEK1)。无效突变会产生极小的聚集体,导致蛞蝓体和终期子实体的形成,这些结构明显小于野生型细胞的。延时视频显微镜和体外实验表明,这些细胞能够产生穿过聚集区域的cAMP波。然而,在聚集过程中,这些细胞无法对趋化因子cAMP进行正常的趋化运动,也无法激活鸟苷酸环化酶,而鸟苷酸环化酶是盘基网柄菌中已知的趋化调节因子。不过,对渗透胁迫的响应中鸟苷酸环化酶的激活是正常的。在ddmek1无效背景中表达假定的组成型活性形式的DdMEK1,至少部分能够弥补聚集体尺寸小的缺陷以及激活鸟苷酸环化酶的能力。然而,这并不会导致鸟苷酸环化酶的组成型激活,这表明DdMEK1活性对于cAMP激活鸟苷酸环化酶是必要的,但不是充分的。对温度敏感的DdMEK1突变体的分析表明,在鸟苷酸环化酶激活时,整个聚集过程都需要DdMEK1活性,但在后期多细胞阶段的正常形态发生中并非必需。腺苷酸环化酶的趋化因子激活所必需的丝裂原活化蛋白激酶ERK2的激活,在ddmek1无效菌株中不受影响,这表明DdMEK1不调节ERK2,并暗示至少有两个独立的丝裂原活化蛋白激酶级联控制盘基网柄菌中的聚集。