Document Detail


A two-segment model for thin filament architecture in skeletal muscle.
MedLine Citation:
PMID:  23299957     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Correct specification of myofilament length is essential for efficient skeletal muscle contraction. The length of thin actin filaments can be explained by a novel 'two-segment' model, wherein the thin filaments consist of two concatenated segments, which are of either constant or variable length. This is in contrast to the classic 'nebulin ruler' model, which postulates that thin filaments are uniform structures, the lengths of which are dictated by nebulin. The two-segment model implicates position-specific microregulation of actin dynamics as a general principle underlying actin filament length and stability.
Authors:
David S Gokhin; Velia M Fowler
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-01-09
Journal Detail:
Title:  Nature reviews. Molecular cell biology     Volume:  14     ISSN:  1471-0080     ISO Abbreviation:  Nat. Rev. Mol. Cell Biol.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-23     Completed Date:  2013-03-21     Revised Date:  2013-08-09    
Medline Journal Info:
Nlm Unique ID:  100962782     Medline TA:  Nat Rev Mol Cell Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  113-9     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
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MeSH Terms
Descriptor/Qualifier:
Actin Cytoskeleton / chemistry*,  physiology*
Animals
CapZ Actin Capping Protein / metabolism,  physiology
Humans
Models, Biological*
Muscle Contraction / physiology
Muscle Proteins / metabolism,  physiology
Muscle, Skeletal / metabolism,  physiology,  ultrastructure*
Myofibrils / chemistry,  metabolism,  physiology,  ultrastructure
Myopathies, Nemaline / genetics,  metabolism,  pathology,  physiopathology
Sarcomeres / metabolism,  physiology
Tropomyosin / metabolism,  physiology
Grant Support
ID/Acronym/Agency:
P30 AR061303/AR/NIAMS NIH HHS; P30‑AR061303/AR/NIAMS NIH HHS; R01 HL083464/HL/NHLBI NIH HHS; R01‑HL083464/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/CapZ Actin Capping Protein; 0/Muscle Proteins; 0/Tropomyosin; 0/nebulin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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