CYTOSKELETAL INTEGRITY IN INTERPHASE CELLS REQUIRES PROTEIN PHOSPHATASE-ACTIVITY
CYTOSKELETAL INTEGRITY IN INTERPHASE CELLS REQUIRES PROTEIN PHOSPHATASE-ACTIVITY
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DOI：
10.1073/pnas.89.22.11093
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发表时间：
1992-11-15
影响因子：
11.1
通讯作者：
GOLDMAN, RD
中科院分区：
文献类型：
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作者：
ERIKSSON, JE;BRAUTIGAN, DL;GOLDMAN, RD
蛋白激酶的磷酸化已被确定为调节细胞骨架结构的关键因素。然而，很少有人知道蛋白磷酸酶在细胞骨架调节中的作用。为了评估蛋白磷酸酶在这方面的可能功能，我们研究了磷酸酶抑制剂calyculin A，冈田酸和甲藻毒素1（35-methylokadaic acid）对BHK-21成纤维细胞的影响。在与这些抑制剂孵育的几分钟内，可以看到中间丝的结构组织发生变化，随后通过免疫荧光法测定微管的损失。这些细胞骨架结构的变化伴随着间期特异性位点上波形蛋白磷酸化的快速和选择性增加，并且在去除calyculin A后它们是完全可逆的。结果表明，有一个快速的磷酸盐周转细胞骨架中间丝，并进一步表明，蛋白磷酸酶是必不可少的两个主要的细胞骨架成分的维护和结构完整性。
Phosphorylation by protein kinases has been established as a key factor in the regulation of cytoskeletal structure. However, little is known about the role of protein phosphatases in cytoskeletal regulation. To assess the possible functions of protein phosphatases in this respect, we studied the effects of the phosphatase inhibitors calyculin A, okadaic acid, and dinophysistoxin 1 (35-methylokadaic acid) on BHK-21 fibroblasts. Within minutes of incubation with these inhibitors, changes are seen in the structural organization of intermediate filaments, followed by a loss of microtubules, as assayed by immunofluorescence. These changes in cytoskeletal structure are accompanied by a rapid and selective increase in vimentin phosphorylation on interphase-specific sites, and they are fully reversible after removal of calyculin A. The results indicate that there is a rapid phosphate turnover on cytoskeletal intermediate filaments and further suggest that protein phosphatases are essential for the maintenance and structural integrity of two major cytoskeletal components.