肌小节组装研究进展

doi:10.3976/j.issn.1002-4026.2017.02.005

Abstract

Abstract:

As the basic contractile unit of striated muscles, sarcomere has a highly ordered structure, which was assembled by Actin, Myosin, and a variety of related proteins. During the assembling process, the correcting assembly of Z belt, M belt, and a series of associated proteins is essential for maintaining movement of muscles, so the study on the mechanism of folding and assembling of sarcomere composition protein is very important for understanding the causes of muscle disease and carrying out targeted therapy. In this paper, the research progress of sarcomere primary components and sarcomere assembling process was reviewed. It was considered that the present studies on sarcomere skeleton assembly, the function of the sarcomere contractile complex, and the relationship between the chaperones and muscle diseases were not deep enough. Therefore, in the future, more studies should be developed on the relationship between Myosin binding protein, Titin, molecular chaperones, and diseases, to find new ideas and solutions to the treatment of muscle related diseases.

Key words: sarcomere, assembling, molecular chaperones, assembling, molecular chaperones, muscle protein, sarcomere, muscle protein

CLC Number:

Q445

HOU Cai-ping, HAN Li-wen, HOU Hai-rong, WANG Xi-min, ZHANG Shan-shan,ZHANG Xuan-ming, WANG Xue, LI Xiao-bin, TIAN Qing-ping, HE Qiu-xia, LIU Ke-chun. The research progress of sarcomere assembly[J].SHANDONG SCIENCE, 2017, 30(2): 25-36.

References

［1］EHLER E, GAUTEL M. The sarcomere andsarcomerogenesis［M］// The Sarcomere and Skeletal Muscle Disease. New York :Springer, 2008.
［2］ AULD A L, FORKER E S. Nucleusdependent sarcomere assembly is mediated by the LINC complex［J］. Molecular biology of the cell, 2016, 27(15): 23512359.
［3］ LAING N G, NOWAK K J. When contractile proteins go bad: the sarcomere and skeletal muscle disease［J］.Bioessays, 2005, 27(8): 809822.
［4］ HELLERSCHMIED D, CLAUSEN T. Myosin chaperones［J］. Current Opinion Structural Biology, 2014, 25:915.
［5］ FUKUDA N, TERUI T, ISHIWATA S,et al. Titinbased regulations of diastolic and systolic functions of mammalian cardiac muscle［J］. Journal of Molecular and Cellular Cardiology, 2010, 48(5): 876881.
［6］柳睿殊，刘荣，刘书霞，等. 肌肉力量的微观起源［J］. 生命科学研究, 2014, 18（5）：453457.
［7］ MYHRE J L, HILLS J A,PRILL K, et al. The titin Aband rod domain is dispensable for initial thick filament assembly in zebrafish［J］. Developmental Biology, 2014, 387(1): 93108.
［8］ DAVULURI G, SEILER C, ABRAMS J, et al. Differential effects of thin and thick filament disruption on zebrafish smooth muscle regulatory proteins［J］. Neurogastroenterology and Motility, 2010, 22(10): 1100e285.
［9］ YAMAGUCHI M, IZUMIMOTO M, ROBSON R M, et al. Fine structure of wide and narrow vertebrate muscle Zlines: A proposed model and computer simulation of Zline architecture［J］. Journal of Molecular Biology, 1985, 184(4): 621643.
［10］ LUTHER P K, BARRY J S, SQUIRE J M. The threedimensional structure of a vertebrate wide (slow muscle) Zband: Lessons on Zband assembly［J］. Journal of Molecular Biology, 2002, 315(1): 920.
［11］ LUTHER P K. Threedimensional structure of a vertebrate muscle Zband: Implications for titin and alphaactinin binding［J］. Journal of Structure Biology, 2000, 129(1): 116.
［12］ SEILER C, DAVULURI G, ABRAMS J, et al. Smooth muscle tension induces invasive remodeling of the zebrafish intestine［J］. Plos Biology, 2012, 10(9):e1001386.
［13］ABRAMS J, EINHORN Z, SEILER C, et al. Graded effects of unregulated smooth muscle myosin on intestinal architecture, intestinal motility and vascular function in zebrafish［J］. Disease Models & Mechanisms, 2016, 9(5): 529540.
［14］ PRILL K, REID P W, WOHLGEMUTH S L, et al. Still heart encodes a structural HMT, SMYD1b, with chaperonelike function during fast muscle sarcomere assembly［J］.PloS One, 2015, 10(11): e0142528.
［15］ SCHIAFFINO S, REGGIANI C, et al. Fiber types in mammalian skeletal muscles［J］. Physiol Rev, 2011, 91(4): 14471531.
［16］ OFFER G,MOOS C, STARR R. A new protein of the thick filaments of vertebrate skeletal myofibrils: Extractions, purification and characterization［J］. Journal of Molecular Biology, 1973, 74(4):653676.
［17］ LI M, ANDERSSON LENDAHL M, SEJERSEN T, et al. Knockdown of fast skeletal myosinbinding protein C in zebrafish results in a severe skeletal myopathy［J］. Journal of General Physiology, 2016, 147(4): 309322.
［18］ RACCA A W, BECK A E, RAO V S,et al. Contractility and kinetics of human fetal and human adult skeletal muscle［J］. J Physiol. 2013, 591(12): 30493061.
［19］ DEACON J C, BLOEMINK M J, REZAVANDI H, et al. Identification of functional differences between recombinant human α and β cardiac myosin motors［J］. Cell Mol Life Sci, 2012, 69(13): 22612277.
［20］ BLOEMINK M, DEACON J, LANGER S, et al. The hypertrophic cardiomyopathy myosin mutation R453C alters ATPbinding and hydrolysis of human cardiac βmyosin［J］. J Biol Chem, 2014, 289: 51585167.
［21］ SOMMESE R F, SUNG J, NAG S, et al. Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human cardiac myosin motor function［J］. Proc Natl Acad Sci USA, 2013, 110(31): 1260712612.
［22］马兰芳，杨书红，王世宣. 肌动蛋白相关蛋白2/3复合体的研究进展［J］. 中国妇幼保健, 2014, 29(34)：57245726.
［23］ ROUILLER I, XU X P , AMANN K J , et al. The structural basis of actin filament branching by the Arp2/3 complex［J］. The Journal of Cell Biology, 2008, 180(5): 887895.
［24］ BAILEY K. Tropomyosin :a new asymmetric protein component of muscle［J］. Nature, 1946, 157: 368369.
［25］ JANCO M, BONELLO T T, BYUN A, et al. The impact of tropomyosins on actin filament assembly is isoform specific［J］. Bioarchitecture, 2016, 6(4):6175.
［26］ KHAITLINA S Y. Chaper sevenTropomyosin as a regulator of actin dynamics［J］. International Review of Cell and Molecular Biology, 2015, 318: 255291.
［27］ MUKHOPADHYAY S, LANGSETMO K, STAFFORD W F III, et al. Identification of a region of fast skeletal troponin T required for stabilization of the coiledcoil formation with troponin I［J］. Journal of Biological Chemistry, 2005, 280(1): 538547.
［28］ FERRANTE M I, KIFF R M, GOULDING D A, et al. Troponin T is essential for sarcomere assembly in zebrafish skeletal muscle［J］. Journal of Cell Science, 2011, 124(Pt 4): 565577.
［29］ GALIN′SKARAKOCZY A, ENGEL P, XU C, et al. Structural basis for the regulation of muscle contraction by troponin and tropomyosin［J］. Journal of Molecular Biology, 2008, 379(5): 929935.
［30］ VIKHLYANTSEV I M, PODLUBNAYA Z A. New titin (connectin) isoforms and their functional role in striated muscles of mammals: Facts and suppositions［J］. Biochemistry, 2012, 77(13): 15151535.
［31］ LINKE W A , HAMDANI N. Gigantic business: Titin properties and function through thick and thin［J］. Circ Res, 2014, 114(6): 10521068.
［32］ BOATENG S Y, GOLDSPINK P H. Assembly and maintenance of the sarcomere night and day［J］. Cardiovasc Res, 2008, 77(4): 667675.
［33］ LIVERSAGE A D, HOLMES D, KNIGHT P J, et al. Titin and the sarcomere symmetry paradox［J］. Journal of Molecular Biology, 2001, 305(3):401409.
［34］ SOMERVILLE L L, WANG K. Sarcomere matrix of striated muscle: In vivo phosphorylation of titin and nebulin in mouse diaphragm muscle［J］. Archives of Biochemistry and Biophysics, 1988, 262(1):118129.
［35］ SALMOVA N N, GRITSYNA Y V, ULANOVA A D, et al. On the role of titin phosphorylation in the development of muscular atrophy［J］. Biophysics, 2015, 60(4): 684686.
［36］ PINNIGER G J. Muscles as motors and muscles as brakes［J］. Leonardo, 2015, 48(2): 174175.
［37］ MUNGAL S U, DUBE S P, DHOLE A, et al. New hypothesis for mechanism of sliding filament theory of skeletal muscle contraction［J］. National Journal of Physiology, Pharmacy & Pharmacology, 2015, 5(1): 7275.
［38］ HUXLEY H E, HANSON J. Changes in the crossstriations of muscle during contraction and stretch and their structural interpretation［J］. Nature, 1954, 173(4412): 973976.
［39］ HUXLEY A F, NIEDERGERKE R. Structural changes in muscle during contraction: Interference microscopy of living muscle fibres［J］. Nature, 1954, 173(4412): 971973.
［40］邱华玲，于建兴，陈宏权. MyoG 基因结构与功能研究进展［J］. 生物信息学, 2007, 5（4）: 190192.
［41］ SANGER J W, WANG J S, FAN Y L, et al. Assembly and dynamics of myofibrils［J］.J Biomed Biotechnol, 2010, 2010: 858606.
［42］ EHLER E,ROTHEN B M, HAMMERLE S P, et al. Myofibrillogenesis in the developing chicken heart: Assembly of Zdisk, Mline and the thick filaments［J］. Journal of Cell Science, 1999, 112(10):15291539.
［43］ GREGORIO C C, ANTIN P B. To the heart of myofibril assembly［J］. Trends in Cell Biol, 2000, 10(9): 355362.
［44］ ROTTY J D，WU C，BEAR J E. New insights into the regulation and cellular functions of the Arp2 /3 complex［J］. Nat Rev Mol Cell Biol, 2013,14 (1): 712.
［45］张震华，薛良义. 鱼类肌节的组成及装配［J］. 中国细胞生物学学报, 2012, 34（12）: 12761281.
［46］ SCHNORRER F, SCHNBAUER C, LANGER C C, et al. Systematic genetic analysis of muscle morphogenesis and function in Drosophila［J］. Nature, 2010, 464(7286): 287291.
［47］ LASKY L A, NAKAMURA G, SMITH D H, et al. Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptor［J］. Cell, 1987, 50(6): 975985.
［48］ SRIKAKULAM R, WINKELMANN D A. Myosin II folding is mediated by a molecular chaperonin［J］. J Biol Chem, 1999, 274: 2726527273.
［49］ SRIKAKULAM R, WINKELMANN D A. Chaperonemediated folding and assembly of myosin in striated muscle［J］. J Cell Sci, 2004, 117(Pt 4): 641652.
［50］ ETARD C, ROOSTALU U, STRAHLE U. Shuttling of the chaperones Unc45b and Hsp90a between the A band and the Z line of the myofibril［J］. J Cell Biol, 2008,180(6): 11631175.
［51］ PRODROMOU C, PANARETOU B, CHOHAN S, et al. The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the Nterminal domains［J］. EMBO J, 2000, 19(16): 43834392.
［52］ ZHAO R, HOURY W A. Molecular interaction network of the Hsp90 chaperone system［J］. Adv Exp Med Biol, 2007, 594: 2736.
［53］ DU S J, LI H Q, BIAN Y H, et al. Heatshock protein 90α1 is required for organized myofibril assembly in skeletal muscles of zebrafish embryos［J］. Proc Natl Acad Sci USA, 2008, 105(2): 554559.
［54］ HAWKINS T A, HARAMIS A P, ETARD C, et al. The ATPasedependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis［J］. Development, 2008, 135(6): 11471156.
［55］ NI W, HUTAGALUNG A H, LI S, et al. The myosinbinding UCS domain but not the Hsp90binding TPR domain of the UNC45 chaperone is essential for function in Caenorhabditis elegans［J］. J Cell Sci, 2011, 124(Pt 18): 31643173.
［56］ CODINA M, LI J L, GUTIRREZ J, et al. Loss of Smyhc1 or Hsp90α1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos［J］. PloS One, 2010, 5: e8416.
［57］ YUN B G, MATTS R L. Differential effects of Hsp90 inhibition on protein kinases regulating signal transduction pathways required for myoblast differentiation［J］. Exp Cell Res, 2005, 307(1): 212223.
［58］ ETARD C, BEHRA M, FISCHER N, et al. The UCS factor Steif/Unc45b interacts with the heat shock protein Hsp90a during myofibrillogenesis［J］. Dev Biol, 2007, 308(1): 133143.
［59］ PRICE M G, LANDSVERK M L, BARRAL J M, et al. Two mammalian UNC45 isoforms are related to distinct cytoskeletal and musclespecific functions［J］. J Cell Sci, 2002, 115(Pt 21): 40134023.
［60］ WOHLGEMUTH S L, CRAWFORD B D, PILGRIM D B. The myosin cochaperone Unc45 is required for skeletal and cardiac muscle function in zebrafish［J］. Dev Biol, 2007, 303(2): 483492.
［61］ LANDSVERK M L, LI S, HUTAGALUNG A H, et al. The UNC45 chaperone mediates sarcomere assembly through myosin degradation in caenorhabditis elegans［J］. J Cell Biol, 2007, 177(2): 205210.
［62］ GAZDA L, POKRZYWA W, HELLERSCHMIED D, et al. The myosin chaperone Unc45 is organized in tandem modules to support myofilament formation in C. elegans［J］. Cell, 2013, 152(1/2): 183195.
［63］ WOHLGEMUTH S L, CRAWFORD B D, PILGRIM D B. The myosin cochaperone Unc45 is required for skeletal and cardiac muscle function in zebrafish［J］. Dev Biol. 2007, 303(2): 483492.
［64］ LEE CF, MELKANI G C, YU Q, et al. Drosophila UNC45 accumulates in embryonic blastoderm and in muscles, and is essential for muscle myosin stability［J］. J Cell Sci, 2011, 124(5): 699705.
［65］ MELKANI G C, LEE C F, CAMMARATO A, et al. Drosophila Unc45 prevents heatinduced aggregation of skeletal muscle myosin and facilitates refolding of citrate synthase［J］. Biochem Biophys Res Commun, 2010, 396(2): 317322.
［66］ BARRAL J M, BAUER C C, ORTIZ I, et al. Unc45 mutations in Caenorhabditis elegans implicate a CRO1/She4plike domain in myosin assembly［J］. J Cell Biol, 1998, 143(5): 12151225.
［67］ SRIKAKULAM R, LIU L, WINKELMANN D A. Unc45b forms a cytosolic complex with Hsp90 and targets the unfolded myosin motor domain［J］. PloS One, 2008, 3(5): e2137.
［68］ CHEN DS, LI SM, SINGH R, et al. Dual function of the Unc45b chaperone with myosin and GATA4 in cardiac development［J］. J Cell Sci, 2012, 125(16): 38933903.
［69］ LI H Q, ZHONG Y W, WANG Z F, et al. Smyd1b is required for skeletal and cardiac muscle function in zebrafish［J］. Mol Biol Cell, 2013, 24(22): 35113521.

The research progress of sarcomere assembly

PDF (PC)

Like

Knowledge

Abstract

Cite this article

share this article

References

Related Articles 0

Metrics

Comments

Recommended 0