@article {832656,
	title = {SALS, a WH2-domain-containing protein, promotes sarcomeric actin filament elongation from pointed ends during Drosophila muscle growth.},
	journal = {Dev Cell},
	volume = {13},
	number = {6},
	year = {2007},
	month = {2007 Dec},
	pages = {828-42},
	abstract = {
	Organization of actin filaments into a well-organized sarcomere structure is critical for muscle development and function. However, it is not completely understood how sarcomeric actin/thin filaments attain their stereotyped lengths. In an RNAi screen in Drosophila primary muscle cells, we identified a gene, sarcomere length short (sals), which encodes an actin-binding, WH2 domain-containing protein, required for proper sarcomere size. When sals is knocked down by RNAi, primary muscles display thin myofibrils with shortened sarcomeres and increased sarcomere number. Both loss- and gain-of-function analyses indicate that SALS may influence sarcomere lengths by promoting thin-filament lengthening from pointed ends. Furthermore, the complex localization of SALS and other sarcomeric proteins in myofibrils reveals that the full length of thin filaments is achieved in a two-step process, and that SALS is required for the second elongation phase, most likely because it antagonizes the pointed-end capping protein Tropomodulin.

},
	keywords = {Actin Cytoskeleton, Amino Acid Sequence, Animals, Animals, Genetically Modified, Cells, Cultured, Drosophila, Drosophila Proteins, Fluorescent Antibody Technique, Microfilament Proteins, Molecular Sequence Data, Muscle, Striated, Myofibrils, Phenotype, RNA, Small Interfering, Sarcomeres, Sequence Homology, Amino Acid},
	issn = {1534-5807},
	doi = {10.1016/j.devcel.2007.10.003},
	author = {Bai, Jianwu and Hartwig, John H and Perrimon, Norbert}
}
