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Actin is one of the most abundant proteins in nature. It is found in all eukaryotes and plays a fundamental role in many diverse and dynamic cellular processes. Also, actin is one of the most ubiquitous proteins because actin-like proteins have recently been identified in bacteria. | ễFEBS Journal REVIEW ARTICLE Thermal unfolding and aggregation of actin Stabilization and destabilization of actin filaments Dmitrii I. Levitsky1 2 Anastasiya V. Pivovarova1 3 Valeria V. Mikhailova1 and Olga P. Nikolaeva2 1 A. N. Bach Institute of Biochemistry Russian Academy of Sciences Moscow Russia 2 A. N. Belozersky Institute of Physico-ChemicalBiology Moscow State University Russia 3 Schoolof Bioengineering and Bioinformatics Moscow State University Russia Keywords actin actin filaments cofilin differential scanning calorimetry heat-induced aggregation inorganic phosphate analogs phalloidin small heat shock proteins thermal stability thermal unfolding Correspondence D. I. Levitsky A.N. Bach Institute of Biochemistry Russian Academy of Sciences Leninsky Prosp. 33 119071 Moscow Russia Fax 7 495 954 2732 Tel 7 495 952 1384 E-mail levitsky@inbi.ras.ru Received 14 April2008 revised 31 May 2008 accepted 24 June 2008 doi 10.1111 j.1742-4658.2008.06569.x Actin is one of the most abundant proteins in nature. It is found in all eukaryotes and plays a fundamental role in many diverse and dynamic cellular processes. Also actin is one of the most ubiquitous proteins because actin-like proteins have recently been identified in bacteria. Actin filament F-actin is a highly dynamic structure that can exist in different conformational states and transitions between these states may be important in cyto-skeletal dynamics and cell motility. These transitions can be modulated by various factors causing the stabilization or destabilization of actin filaments. In this review we look at actin stabilization and destabilization as expressed by changes in the thermal stability of actin specifically we summarize and analyze the existing data on the thermal unfolding of actin as measured by differential scanning calorimetry. We also analyze in vitro data on the heat-induced aggregation of actin the process that normally accompanies actin thermal denaturation. In this respect we focus on .
