Skeletal Muscle Structure and Function

This chapter summarizes the basic organization of skeletal muscle. Skeletal muscle is responsible for all voluntary movement, and its unique organization is optimized for this function. The sarcomere is the unit of muscle contraction and the sarcomere is linked to the plasma membrane through the Z band. Skeletal muscle is also unique in that mature myofibers are a multinucleate syncytium. Efficient delivery of calcium is necessary for coordinated muscle contraction. Neuronal control is also a key contributor to muscle function. Mutations in the genes encoding many “structural” proteins of muscle lead to muscle weakness and degeneration.

[1]  G. Lanfranchi,et al.  Telethonin and Other New Proteins of the Z‐Disc of Skeletal Muscle , 2001, IUBMB life.

[2]  H. Sweeney,et al.  Dystrophin protects the sarcolemma from stresses developed during muscle contraction. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[3]  J. Barral,et al.  Protein machines and self assembly in muscle organization. , 1999, BioEssays : news and reviews in molecular, cellular and developmental biology.

[4]  A. Emery Emery–Dreifuss muscular dystrophy – a 40 year retrospective , 2000, Neuromuscular Disorders.

[5]  J. Spudich,et al.  Fluorescent actin filaments move on myosin fixed to a glass surface. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[6]  T. Yanagida,et al.  Single molecule analysis of the actomyosin motor. , 2000, Current opinion in cell biology.

[7]  M. Beckerle,et al.  Striated muscle cytoarchitecture: an intricate web of form and function. , 2002, Annual review of cell and developmental biology.

[8]  H. Sweeney,et al.  Myosin motors: missing structures and hidden springs. , 2001, Current opinion in structural biology.

[9]  J. Ervasti,et al.  The Dystrophin Complex Forms a Mechanically Strong Link between the Sarcolemma and Costameric Actin , 2000, The Journal of cell biology.

[10]  L. Kunkel,et al.  The structural and functional diversity of dystrophin , 1993, Nature Genetics.

[11]  C. Gregorio,et al.  To the heart of myofibril assembly. , 2000, Trends in cell biology.

[12]  H. Sweeney,et al.  Muscle degeneration without mechanical injury in sarcoglycan deficiency. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[13]  A. Goldberg,et al.  Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[14]  D J Glass,et al.  Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy , 2001, Science.

[15]  K. Campbell,et al.  Dystroglycan inside and out. , 1999, Current opinion in cell biology.

[16]  C. Kang,et al.  Structure–Function Relationships in Ca2+ Cycling Proteins , 2002 .

[17]  James A. Spudich,et al.  The myosin swinging cross-bridge model , 2001, Nature Reviews Molecular Cell Biology.

[18]  John Trinick,et al.  Two-headed binding of a processive myosin to F-actin , 2000, Nature.

[19]  J. Siliciano,et al.  A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. , 1983, Proceedings of the National Academy of Sciences of the United States of America.

[20]  B. Hainque,et al.  Familial hypertrophic cardiomyopathy: from mutations to functional defects. , 1998, Circulation research.

[21]  Daniel Safer,et al.  Myosin VI is an actin-based motor that moves backwards , 1999, Nature.

[22]  F. Müller,et al.  Junctional sarcoplasmic reticulum transmembrane proteins in the heart , 2002, Basic Research in Cardiology.

[23]  Amber L. Wells,et al.  Myosin VI is a processive motor with a large step size , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[24]  J. Ervasti Costameres: the Achilles' Heel of Herculean Muscle* 210 , 2003, The Journal of Biological Chemistry.

[25]  K. Campbell,et al.  Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. , 2002, Current opinion in genetics & development.

[26]  U. Mayer Integrins: Redundant or Important Players in Skeletal Muscle?* , 2003, The Journal of Biological Chemistry.

[27]  Min Han,et al.  Role of ANC-1 in Tethering Nuclei to the Actin Cytoskeleton , 2002, Science.

[28]  A. Huxley,et al.  Cross-bridge action: present views, prospects, and unknowns. , 2000, Journal of biomechanics.

[29]  Min Han,et al.  ANChors away: an actin based mechanism of nuclear positioning , 2003, Journal of Cell Science.

[30]  J. Trinick,et al.  Titin: a molecular control freak. , 1999, Trends in cell biology.

[31]  Se-Jin Lee,et al.  Myostatin and the control of skeletal muscle mass. , 1999, Current opinion in genetics & development.

[32]  T. Rando The dystrophin–glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies , 2001, Muscle & nerve.

[33]  Denise M O'Hara,et al.  Inhibition of myostatin in adult mice increases skeletal muscle mass and strength. , 2003, Biochemical and biophysical research communications.

[34]  H. Worman,et al.  How do mutations in lamins A and C cause disease? , 2004, The Journal of clinical investigation.

[35]  Susan C. Brown,et al.  Dystrophin and utrophin: Genetic analyses of their role in skeletal muscle , 2000, Microscopy research and technique.

[36]  Jianjie Ma,et al.  Junctional membrane structure and store operated calcium entry in muscle cells. , 2003, Frontiers in bioscience : a journal and virtual library.

[37]  E. McNally,et al.  Sarcoglycans in muscular dystrophy , 2000, Microscopy research and technique.

[38]  F. Protasi,et al.  Ryanodine receptors of striated muscles: a complex channel capable of multiple interactions. , 1997, Physiological reviews.