Structure and elasticity of desmin protofibrils explored with scanning force microscopy

Abstract

Desmin filaments form the intermediate filament system of muscle cells where they play important role in maintaining mechanical integrity and elasticity. Although the importance of desmin elasticity and assembly-disassembly dynamics in cellular mechanics is being increasingly recognized, the molecular basis of neither desmin's elasticity nor its disassembly pathway is well understood. In the present work, we explored the topographical structure of purified and reconstituted desmin filaments by using scanning force microscopy. With the addition of divalent cation chelators ethyleneglycoltetraacetic acid or ethylenediaminetetraacetic acid, the filaments disassembled on a time scale of hours to days into stable, thin fibrillar components with variable (up to micrometer) length, smooth surface and uniform thickness, which are identified as protofibrils. Desmin protofibrils appear as elastic structures with a persistence length of 51.5 nm, and their Young's modulus (10.6 MPa) far exceeds that of the mature filament (3.7 MPa). Protofibrillar bundling within the desmin filament results in high longitudinal tensile strength at a large bending flexibility. The stability of protofibrils suggests that desmin may disassemble along a pathway quite distinct from its assembly.