Actin-Binding Proteins and Disease by Cris dos Remedios, Deepak Chhabra

By Cris dos Remedios, Deepak Chhabra

This quantity, written by way of specialists within the box, is the 1st to house the connection among human illness and the actin cytoskeleton. It presents overviews of actin and chosen actin-binding proteins, after which makes a speciality of illnesses that contain those proteins. particular chapters care for actin, cofilin, profilin, gelsolin and thymosin ¾4. different chapters talk about the jobs of a number of actin-binding proteins in melanoma and metastasis, leukocyte issues, and center failure, and there's a bankruptcy that describes how intracellular pathogens use the host actin cytoskeleton. This seminal quantity is meant for researchers, clinicians, physicians, and graduate scholars within the fields of biochemistry, cellphone biology, microbiology, immunology, and genetics.

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Laing probably many more, genes can cause this disease. Again, as with most actin diseases these are dominant mutations. The CFTD mutations were L221P, D292V, and P332S. The observations raise two major questions: (1) Since both fiber types express ACTA1 as the major actin in postnatal skeletal muscle why do type 1 fibers show hypotrophy but type 2 fibers do not? (2) Since these patients did not show the nemaline myopathy (see above) typical of the majority of ACTA1 mutations do the CFTD mutations affect a specific actin function?

Commun. 173, 120–126. , Popp, D. and Holmes, K. C. 1993. Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826–836. 2. Actin Genetic Diseases 33 Luther, P. and Squire, J. M. 2002. Muscle Z-band ultrastructure: Titin Z-repeats and Z-band periodicities do not match. J. Mol. Biol. 319, 1157–1164. Maron, B. J. 1997. Hypertrophic cardiomyopathy. Lancet, 350, 127–133. , Abdulrazzak, H. and Sewry, C. 2004. Functional characterisation of a mutant actin (Met132Val) from a patient with nemaline myopathy.

The histochemical differentiation of the two fiber types, usually on the basis of staining for ATPase activity, reflects the different myosin isoforms present in each fiber type. In the monomeric actin atomic structure (Kabsch et al. 1990; Otterbein, Graceffa and Dominguez 2001) the amino acid residues affected by the three mutations (Leu221Pro, Asp292Val and Pro332Ser) form part of the monomeric actin surface and will remain exposed in the F-actin polymer. By fitting the atomic structures of both actin and the myosin S1 fragment into EM reconstructions of rigorstate S1-decorated F-actin (Rayment et al.

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