Korn E D
Proc Natl Acad Sci U S A. 1978 Feb;75(2):588-99. doi: 10.1073/pnas.75.2.588.
Actins and myosins similar to the major proteins of muscle are the major molecular components of intricate mechanochemical systems that perform numerous vital motility and structural functions in all eukaryotic cells. In this article, after a brief summary of the morphological distribution and ultrastructure of actin, myosin, and interrelated proteins of nonmuscle cells, our present knowledge of their biochemistry is critically appraised from the perspective that understanding complex cellular processes depends ultimately on the identification, purification, and biochemical characterization of the proteins involved. Although few conclusions are reached, possible molecular mechanisms for cellular regulation of actin polymerization, filament association, actomyosin ATPase activity, and mechanochemical coupling are discussed and a number of potentially fruitful directions for further research are suggested. These include comparative biochemical investigations and the study of the interaction of heterologous proteins, but particular emphasis is given to the need for quantitative studies at the molecular level of motility proteins purified from a single cellular source.
与肌肉主要蛋白质类似的肌动蛋白和肌球蛋白,是复杂的机械化学系统的主要分子成分,这些系统在所有真核细胞中执行众多重要的运动和结构功能。在本文中,在简要总结非肌肉细胞中肌动蛋白、肌球蛋白及相关蛋白的形态分布和超微结构之后,我们从这样的观点对它们的生物化学的现有知识进行了批判性评估,即理解复杂的细胞过程最终取决于对所涉及蛋白质的鉴定、纯化和生物化学特性分析。虽然得出的结论很少,但讨论了细胞调节肌动蛋白聚合、丝状体缔合、肌动球蛋白ATP酶活性和机械化学偶联的可能分子机制,并提出了一些有潜在成果的进一步研究方向。这些包括比较生物化学研究和异源蛋白质相互作用的研究,但特别强调需要在从单一细胞来源纯化的运动蛋白的分子水平上进行定量研究。