Huelsman D A, Gitz D L, Pennock D G
Department of Zoology, Miami University, Oxford, Ohio 45056.
Cytobios. 1992;71(284):37-50.
Previous work suggests that changes in the phosphorylation state of some centrosomal proteins regulate centrosomal activity. The hypothesis that changes in the phosphorylation state of one or more basal body microtubule organizing centre (MTOC) components regulate its ability to nucleate cilia assembly in Tetrahymena thermophila was tested. The MPM-2 antibody, which recognizes phosphorylated epitopes in MTOCs in a variety of organisms, was used to probe immunoblots of cytoskeletal frameworks prepared from starved Tetrahymena, from starved deciliated Tetrahymena, and from a starved deciliated mutant Tetrahymena which failed to initiate ciliogenesis following deciliation. The MPM-2 antibody recognized an identical array of proteins in all blots. These results suggest that, unlike centrosomes, basal body MTOC activity is not regulated by changes in the phosphorylation state of component proteins.
先前的研究表明,某些中心体蛋白磷酸化状态的变化会调节中心体活性。我们对以下假说进行了验证:一个或多个基体微管组织中心(MTOC)组分的磷酸化状态变化会调节嗜热四膜虫中其促使纤毛组装成核的能力。MPM-2抗体可识别多种生物体MTOC中的磷酸化表位,我们用它来探测由饥饿的嗜热四膜虫、饥饿的去纤毛嗜热四膜虫以及饥饿的去纤毛后无法启动纤毛再生的嗜热四膜虫突变体制备的细胞骨架框架的免疫印迹。MPM-2抗体在所有印迹中识别出相同的蛋白阵列。这些结果表明,与中心体不同,基体MTOC活性不受组分蛋白磷酸化状态变化的调节。