期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1978
卷号：75
期号：2
页码：588-599
DOI：10.1073/pnas.75.2.588
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
