Assembly and Dynamics of Myofibrils

Sanger, Joseph W.; Wang, Jushuo; Fan, Yingli; White, Jennifer; Sanger, Jean M.

doi:10.1155/2010/858606

Cited by 139 publications

(151 citation statements)

References 65 publications

(115 reference statements)

Supporting

Mentioning

140

Contrasting

Unclassified

Order By: Relevance

“…Thus, the organization of actin filaments in premyofibrils resembles that of stress fibers in non-muscle cells (Sanger et al, 2005, Sanger et al, 2009. Although many sarcomeric proteins are present in premyofibrils, they contain non-muscle myosin II instead of the muscle-specific myosin II isoform (Handel et al, 1991;Sanger et al, 2010). Premyofibrils thus display some similarities to the transverse arcs of nonmuscle cells and might also utilize similar pathways for their assembly (Sanger et al, 2009;Sparrow and Schöck, 2009).…”

Section: Regulation Of Stress Fiber Contractionmentioning

confidence: 99%

Actin stress fibers – assembly, dynamics and biological roles

Tojkander

Gateva

Lappalainen

2012

Journal of Cell Science

731

743

View full text Add to dashboard Cite

SummaryActin filaments assemble into diverse protrusive and contractile structures to provide force for a number of vital cellular processes. Stress fibers are contractile actomyosin bundles found in many cultured non-muscle cells, where they have a central role in cell adhesion and morphogenesis. Focal-adhesion-anchored stress fibers also have an important role in mechanotransduction. In animal tissues, stress fibers are especially abundant in endothelial cells, myofibroblasts and epithelial cells. Importantly, recent live-cell imaging studies have provided new information regarding the mechanisms of stress fiber assembly and how their contractility is regulated in cells. In addition, these studies might elucidate the general mechanisms by which contractile actomyosin arrays, including muscle cell myofibrils and cytokinetic contractile ring, can be generated in cells. In this Commentary, we discuss recent findings concerning the physiological roles of stress fibers and the mechanism by which these structures are generated in cells.

show abstract

Section: Regulation Of Stress Fiber Contractionmentioning

confidence: 99%

Actin stress fibers – assembly, dynamics and biological roles

Tojkander

Gateva

Lappalainen

2012

Journal of Cell Science

731

743

View full text Add to dashboard Cite

show abstract

“…Myofibril assembly begins at the Z-disk (reviewed in Ehler and Gautel, 2008;Sanger et al, 2010). Here, antiparallel actin filaments are crosslinked and capped at their barbed ends, leading to tetragonal arrays of precisely tailored thickness (Figs 1-3).…”

Section: Z-disk Cytoskeleton: Form Follows Function?mentioning

confidence: 99%

“…There appears to be no change in Z-disk thickness, however. Whether the sprint performance advantage of wild-type ACTN3 carriers is due to subtle differences in molecular mechanical properties or in the interaction with any of the many α-actinin interacting proteins that link to cellular signalling and metabolic pathways (Djinovic-Carugo et al, 2002;Lange et al, 2006;Linke and Kruger, 2010;Sanger et al, 2010) is currently unclear. However, these observations underscore the role of the sarcomeric cytoskeleton as not only a passive scaffold but also a determinant of muscle performance and metabolism (Berman and North, 2010), which has recently been linked to differential transcriptional regulation by calcineurin via calsarcin-2/myozenin-1/FATZ-1 at the α-actinin scaffold (Seto et al, 2013).…”

Section: Z-disk Cytoskeleton: Form Follows Function?mentioning

confidence: 99%

“…A scaffold of actin filaments, integrating α-actinin and titin, seems to be the core component for the subsequent integration of M-band modules, sarcomeric myosin and accessory proteins Sanger et al, 2010;Van der Ven et al, 1999;White et al, 2014). In vivo, primary sarcomere assembly occurs close to the cell membrane and seems to involve as yet poorly understood links to the membrane cytoskeletal system.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The sarcomeric cytoskeleton: from molecules to motion

Gautel

Djinović-Carugo

2016

Journal of Experimental Biology

190

177

View full text Add to dashboard Cite

Highly ordered organisation of striated muscle is the prerequisite for the fast and unidirectional development of force and motion during heart and skeletal muscle contraction. A group of proteins, summarised as the sarcomeric cytoskeleton, is essential for the ordered assembly of actin and myosin filaments into sarcomeres, by combining architectural, mechanical and signalling functions. This review discusses recent cell biological, biophysical and structural insight into the regulated assembly of sarcomeric cytoskeleton proteins and their roles in dissipating mechanical forces in order to maintain sarcomere integrity during passive extension and active contraction. α-Actinin crosslinks in the Z-disk show a pivot-and-rod structure that anchors both titin and actin filaments. In contrast, the myosin crosslinks formed by myomesin in the M-band are of a balland-spring type and may be crucial in providing stable yet elastic connections during active contractions, especially eccentric exercise.

show abstract

“…The general pattern of differentiation of cultured cardiac muscle cells has been reported elsewhere (DeHaan and Hirakow, 1972;Schultheiss et al, 1990;Ono, 2010;Sanger et al, 2010) and will not be reported here.…”

Section: Resultsmentioning

confidence: 90%

Morphological Modifications in Myofibrils by Suppressing Tropomyosin 4α in Chicken Cardiac Myocytes

Toyota

Fujitsuka

Ishibashi

et al. 2016

Cell Struct. Funct.

View full text Add to dashboard Cite

ABSTRACT. Tropomyosin (TPM) localizes along F-actin and, together with troponin T (TnT) and other components, controls calcium-sensitive muscle contraction. The role of the TPM isoform (TPM4α) that is expressed in embryonic and adult cardiac muscle cells in chicken is poorly understood. To analyze the function of TPM4α in myofibrils, the effects of TPM4α-suppression were examined in embryonic cardiomyocytes by small interference RNA transfection. Localization of myofibril proteins such as TPM, actin, TnT, α-actinin, myosin and connectin was examined by immunofluorescence microscopy on day 5 when almost complete TPM4α-suppression occurred in culture. A unique large structure was detected, consisting of an actin aggregate bulging from the actin bundle, and many curved filaments projecting from the aggregate. TPM, TnT and actin were detected on the large structure, but myosin, connectin, α-actinin and obvious myofibril striations were undetectable. It is possible that TPM4α-suppressed actin filaments are sorted and excluded at the place of the large structure. This suggests that TPM4α-suppression significantly affects actin filament, and that TPM4α plays an important role in constructing and maintaining sarcomeres and myofibrils in cardiac muscle.

show abstract

Assembly and Dynamics of Myofibrils

Cited by 139 publications

References 65 publications

Actin stress fibers – assembly, dynamics and biological roles

Actin stress fibers – assembly, dynamics and biological roles

The sarcomeric cytoskeleton: from molecules to motion

Morphological Modifications in Myofibrils by Suppressing Tropomyosin 4α in Chicken Cardiac Myocytes

Contact Info

Product

Resources

About