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Much similar to workhorses, actin filaments are the laborious workers of a muscle. They push cell membranes to bring about cellular movements within tissues. Actin filaments work in order to keep all the cell organelles in their respective positions by applying pressure from within. The whole task of movement and keeping the respective positions for organelles is performed through continual splitting and reassembly of actin filaments. A complex series of molecular events determine the assembly and disassembly of actin filaments. This disassembly of actin filaments is influenced by a protein called cofilin which belongs to the family of actin binding proteins. The exact site of breakage of these actin filaments composed of actin monomers was unknown until now. It has also been observed that these filaments imitate the strength of commercial plastic. This molecular disassembly was captured by the scientists of Yale University led by Enrique De La Cruz, an Associate Professor of Molecular Biophysics and Biochemistry. His French colleagues also took part in this endeavour. Fluorescent stains of cofilin were used with the underlying basis of a phenomenon called total internal reflection fluorescence. This kind of microscopy helped them in studying the smallest of details in a cells working. This study has been published in the Journal of Current Biology. Cristian Suarez, Jérémy Roland, Rajaa Boujemaa-Paterski, Hyeran Kang, Brannon R. McCullough, Anne-Cécile Reymann, Christophe Guérin, Jean-Louis Martiel, Enrique M. De La Cruz, Laurent Blanchoin. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology, 28 April 2011 DOI: 10.1016/j.cub.2011.03.064 published: 30 Nov 2011 (12:06) Other news pages: 1 | ||||||
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