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New insights into the structural roles of nebulin in skeletal muscle Ottenheijm CA; Granzier HJ Biomed Biotechnol 2010[]; 2010 (ä): 968139One important feature of muscle structure and function that has remained relatively obscure is the mechanism that regulates thin filament length. Filament length is an important aspect of muscle function as force production is proportional to the amount of overlap between thick and thin filaments. Recent advances, due in part to the generation of nebulin KO models, reveal that nebulin plays an important role in the regulation of thin filament length. Another structural feature of skeletal muscle that is not well understood is the mechanism involved in maintaining the regular lateral alignment of adjacent sarcomeres, that is, myofibrillar connectivity. Recent studies indicate that nebulin is part of a protein complex that mechanically links adjacent myofibrils. Thus, novel structural roles of nebulin in skeletal muscle involve the regulation of thin filament length and maintaining myofibrillar connectivity. When these functions of nebulin are absent, muscle weakness ensues, as is the case in patients with nemaline myopathy with mutations in nebulin. Here we review these new insights in the role of nebulin in skeletal muscle structure.|*Muscle Proteins/chemistry/physiology[MESH]|Biomechanical Phenomena[MESH]|Humans[MESH]|Models, Molecular[MESH]|Muscle, Skeletal/*chemistry[MESH]|Protein Conformation[MESH] |
