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β‐synemin localizes to regions of high stress in human skeletal myofibers

Synemin is an intermediate filament protein shown previously to interact with α‐dystrobrevin and desmin. Immunoblot analysis detects a β‐synemin protein of 170 kDa in human skeletal muscle and an α‐synemin protein of 225 kDa in monkey brain. Low‐resolution immunohistochemical analysis localizes β‐synemin within muscle along the sarcolemma, whereas confocal microscopic analysis further refines localization to the costamere and muscle Z‐lines. In addition to these locations, β‐synemin is also enriched at the neuromuscular and myotendinous junctions, other regions that undergo high stress during myofiber contraction. Based on its localization and its expression pattern, it is proposed that β‐synemin functions as a structural protein involved in maintaining muscle integrity through its interactions with α‐dystrobrevin, desmin, and other structural proteins. Muscle Nerve 30: 337–346, 2004