A Titan but not Necessarily a Ruler: Assessing the Role of Titin During Thick Filament Patterning and Assembly

ABSTRACT The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these semicrystalline filament networks are initially patterned and assembled remain contentious. In addition to the acto‐myosin filaments that provi...

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Published inAnatomical record (Hoboken, N.J. : 2007) Vol. 297; no. 9; pp. 1604 - 1614
Main Authors Myhre, J. Layne, Pilgrim, David
Format Journal Article
LanguageEnglish
Published United States Wiley Subscription Services, Inc 01.09.2014
Subjects
Animals
Connectin - metabolism
Humans
muscle
Muscle Development
Muscle, Striated - growth & development
Muscle, Striated - metabolism
Muscle, Striated - physiology
sarcomere
Sarcomeres - metabolism
Sarcomeres - physiology
Signal Transduction
titin
titin
sarcomere
muscle
Online AccessGet full text

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Abstract ABSTRACT The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these semicrystalline filament networks are initially patterned and assembled remain contentious. In addition to the acto‐myosin filaments that provide motor function, the sarcomere contains titin filaments, comprised of individual molecules of the giant Ig‐ and fibronectin domain‐rich protein titin. Titin is the largest known protein, containing many structurally distinct domains with a variety of proposed functions, including sarcomere stabilization, the prevention of over‐stretching, and returning to resting length after contraction. One molecule of titin, which binds to both the Z‐disk and the M‐line, spans a half‐sarcomere, and is proposed to serve as a “molecular ruler” that dictates the spacing of sarcomeres. The semirigid rod‐like A‐band region of titin has also been proposed to act as a scaffold for thick filament formation during muscle development, but despite decades of research, this hypothesis has not been rigorously tested. Recent studies in zebrafish have brought into question the necessity for the A‐band region of titin during the early stages of sarcomere patterning. In this review, we give an overview of the many different roles of titin in the development and function of striated muscle, and address the validity of the “molecular ruler” model of myofibrillogenesis in light of the current literature. Anat Rec, 297:1604–1614, 2014. © 2014 Wiley Periodicals, Inc.
AbstractList The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these semicrystalline filament networks are initially patterned and assembled remain contentious. In addition to the acto-myosin filaments that provide motor function, the sarcomere contains titin filaments, comprised of individual molecules of the giant Ig- and fibronectin domain-rich protein titin. Titin is the largest known protein, containing many structurally distinct domains with a variety of proposed functions, including sarcomere stabilization, the prevention of over-stretching, and returning to resting length after contraction. One molecule of titin, which binds to both the Z-disk and the M-line, spans a half-sarcomere, and is proposed to serve as a "molecular ruler" that dictates the spacing of sarcomeres. The semirigid rod-like A-band region of titin has also been proposed to act as a scaffold for thick filament formation during muscle development, but despite decades of research, this hypothesis has not been rigorously tested. Recent studies in zebrafish have brought into question the necessity for the A-band region of titin during the early stages of sarcomere patterning. In this review, we give an overview of the many different roles of titin in the development and function of striated muscle, and address the validity of the "molecular ruler" model of myofibrillogenesis in light of the current literature. Anat Rec, 297:1604-1614, 2014. © 2014 Wiley Periodicals, Inc. [PUBLICATION ABSTRACT]
The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these semicrystalline filament networks are initially patterned and assembled remain contentious. In addition to the acto-myosin filaments that provide motor function, the sarcomere contains titin filaments, comprised of individual molecules of the giant Ig- and fibronectin domain-rich protein titin. Titin is the largest known protein, containing many structurally distinct domains with a variety of proposed functions, including sarcomere stabilization, the prevention of over-stretching, and returning to resting length after contraction. One molecule of titin, which binds to both the Z-disk and the M-line, spans a half-sarcomere, and is proposed to serve as a "molecular ruler" that dictates the spacing of sarcomeres. The semirigid rod-like A-band region of titin has also been proposed to act as a scaffold for thick filament formation during muscle development, but despite decades of research, this hypothesis has not been rigorously tested. Recent studies in zebrafish have brought into question the necessity for the A-band region of titin during the early stages of sarcomere patterning. In this review, we give an overview of the many different roles of titin in the development and function of striated muscle, and address the validity of the "molecular ruler" model of myofibrillogenesis in light of the current literature.
ABSTRACT The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these semicrystalline filament networks are initially patterned and assembled remain contentious. In addition to the acto‐myosin filaments that provide motor function, the sarcomere contains titin filaments, comprised of individual molecules of the giant Ig‐ and fibronectin domain‐rich protein titin. Titin is the largest known protein, containing many structurally distinct domains with a variety of proposed functions, including sarcomere stabilization, the prevention of over‐stretching, and returning to resting length after contraction. One molecule of titin, which binds to both the Z‐disk and the M‐line, spans a half‐sarcomere, and is proposed to serve as a “molecular ruler” that dictates the spacing of sarcomeres. The semirigid rod‐like A‐band region of titin has also been proposed to act as a scaffold for thick filament formation during muscle development, but despite decades of research, this hypothesis has not been rigorously tested. Recent studies in zebrafish have brought into question the necessity for the A‐band region of titin during the early stages of sarcomere patterning. In this review, we give an overview of the many different roles of titin in the development and function of striated muscle, and address the validity of the “molecular ruler” model of myofibrillogenesis in light of the current literature. Anat Rec, 297:1604–1614, 2014. © 2014 Wiley Periodicals, Inc.
Author Myhre, J. Layne
Pilgrim, David
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  fullname: Pilgrim, David
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Snippet ABSTRACT The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these...
The sarcomeres of striated muscle are among the most elaborate and dynamic eukaryotic cellular protein machinery, and the mechanisms by which these...
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SubjectTerms Animals
Connectin - metabolism
Humans
muscle
Muscle Development
Muscle, Striated - growth & development
Muscle, Striated - metabolism
Muscle, Striated - physiology
sarcomere
Sarcomeres - metabolism
Sarcomeres - physiology
Signal Transduction
titin
Title A Titan but not Necessarily a Ruler: Assessing the Role of Titin During Thick Filament Patterning and Assembly
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https://www.ncbi.nlm.nih.gov/pubmed/25125174
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