Regulation of muscle contraction by Drebrin-like protein 1 probed by atomic force microscopy.

Sarcomeres are the fundamental contractile units of striated muscle cells. They are composed of a variety of structural and regulatory proteins functioning in a precisely orchestrated fashion to enable coordinated force generation in striated muscles. Recently, we have identified a \textit{C. elegans} drebrin-like protein 1 (DBN-1) as a novel sarcomere component, which stabilizes actin filaments during muscle contraction. To further characterize the function of DBN-1 in muscle cells, we generated a new \textit{dbn-1} loss-of-function allele. Absence of DBN-1 resulted in a unique worm movement phenotype, characterized by hyper-bending. It is not clear yet if DBN-1 acts to enhance or reduce the capacity for contraction. We present here an experimental mechanical study on \textit{C. elegans} muscle mechanics. We measured the stiffness of the worm by indenting living \textit{C. elegans }with a micron-sized sphere adhered to the cantilever of an atomic force microscope (AFM). Modeling the worm as a pressurized elastic shell allows us to monitor the axial tension in the muscle through the measured stiffness. We compared responses of wild-type and mutant \textit{C. elegans} in which DBN-1 is not expressed..