The giant muscle protein titin is an adjustable molecular spring

Henk L. Granzier; Siegfried Labeit

doi:10.1249/00003677-200604000-00002

The giant muscle protein titin is an adjustable molecular spring

Henk L. Granzier, Siegfried Labeit

Research output: Contribution to journal › Review article › peer-review

58 Scopus citations

Abstract

When muscles are stretched, the giant protein titin develops passive force. Titin's force performs important functions that include maintaining the structural integrity of the sarcomere, and triggering signal transduction pathways. We propose that the mechanical properties of titin can be tuned according to the mechanical demands places on muscle, using mechanisms that include alternative splicing and posttranslational modifications.

Original language	English (US)
Pages (from-to)	50-53
Number of pages	4
Journal	Exercise and Sport Sciences Reviews
Volume	34
Issue number	2
DOIs	https://doi.org/10.1249/00003677-200604000-00002
State	Published - Apr 2006
Externally published	Yes

Keywords

Differential splicing
Mechanosensing
Muscle mechanics
Passive force
Posttranslational modification
Titin

ASJC Scopus subject areas

Orthopedics and Sports Medicine
Physical Therapy, Sports Therapy and Rehabilitation

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10.1249/00003677-200604000-00002

Cite this

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AU - Labeit, Siegfried

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AB - When muscles are stretched, the giant protein titin develops passive force. Titin's force performs important functions that include maintaining the structural integrity of the sarcomere, and triggering signal transduction pathways. We propose that the mechanical properties of titin can be tuned according to the mechanical demands places on muscle, using mechanisms that include alternative splicing and posttranslational modifications.

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KW - Muscle mechanics

KW - Passive force

KW - Posttranslational modification

KW - Titin

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The giant muscle protein titin is an adjustable molecular spring

Abstract

Keywords

ASJC Scopus subject areas

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