期刊
JOURNAL OF EXPERIMENTAL BIOLOGY
卷 219, 期 2, 页码 146-152出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jeb.126383
关键词
Actin filament; Sarcomere; Skeletal muscle
类别
资金
- National Institutes of Health [R01HL108625, R01HL123078]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL123078, R01HL108625] Funding Source: NIH RePORTER
Efficient muscle contraction in skeletal muscle is predicated on the regulation of actin filament lengths. In one long-standing model that was prominent for decades, the giant protein nebulin was proposed to function as a 'molecular ruler' to specify the lengths of the thin filaments. This theory was questioned by many observations, including experiments in which the length of nebulin was manipulated in skeletal myocytes; this approach revealed that nebulin functions to stabilize filamentous actin, allowing thin filaments to reach mature lengths. In addition, more recent data, mostly from in vivo models and identification of new interacting partners, have provided evidence that nebulin is not merely a structural protein. Nebulin plays a role in numerous cellular processes including regulation of muscle contraction, Z-disc formation, andmyofibril organization and assembly.
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