Dictyostelium myosin II is regulated during chemotaxis by a novel protein kinase C
Dictyostelium myosin II is regulated during chemotaxis by a novel protein kinase C
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DOI：
10.1074/jbc.271.2.977
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发表时间：
1996-01-12
影响因子：
4.8
通讯作者：
Ravid, S
中科院分区：
文献类型：
--
作者：
AbuElneel, K;Karchi, M;Ravid, S
从盘状Dictyostelium disideum中分离的肌球蛋白II重链（MHC）特异性蛋白激酶C （MHC- pkc）参与了肌球蛋白II对化学引诱剂cAMP的组装调节（Ravid， S., and Spudich， J. A. (1989) J. Biol.）。化学，264,15144-15150)。在这里，我们报道了MHC-PKC的消除导致MNC磷酸化的消除，以响应cAMP。缺乏MHC- pkc的细胞表现出大量的肌球蛋白II过组装，以及异常的细胞极化、趋化和形态分化，过度表达MHC- pkc的细胞含有高度磷酸化的MHC，表现出肌球蛋白II定位受损，没有明显的细胞极化和趋化。本研究结果提供了直接证据，证明MHC- pkc在cAMP作用下磷酸化MHC，并在趋化过程中调控肌球蛋白II的定位中发挥重要作用。
The myosin II heavy chain (MHC)-specific protein kinase C (MHC-PKC) isolated from Dictyostelium discoideum has been implicated in the regulation of myosin II assembly in response to the chemoattractant, cAMP (Ravid, S., and Spudich, J. A. (1989) J. Biol. Chem. 264, 15144-15150). Here we report that elimination of MHC-PKC results in the abolishment of MNC phosphorylation in response to cAMP. Cells devoid of MHC-PKC exhibit substantial myosin II overassembly, as well as aberrant cell polarization, chemotaxis, and morphological differentiation, Cells overexpressing the MHC-PKC contain highly phosphorylated MHC and exhibit impaired myosin II localization and no apparent cell polarization and chemotaxis. The results presented here provide direct evidence that MHC-PKC phosphorylates MHC in response to cAMP and plays an important role in the regulation of myosin II localization during chemotaxis.