The giant muscle protein titin is an adjustable molecular spring

Hendrikus "Henk" Granzier, Siegfried Labeit

Research output: Contribution to journalArticle

47 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)50-53
Number of pages4
JournalExercise and Sport Sciences Reviews
Volume34
Issue number2
DOIs
StatePublished - Apr 2006
Externally publishedYes

Fingerprint

Connectin
Muscle Proteins
Muscles
Sarcomeres
Alternative Splicing
Post Translational Protein Processing
Signal Transduction
Proteins

Keywords

  • Differential splicing
  • Mechanosensing
  • Muscle mechanics
  • Passive force
  • Posttranslational modification
  • Titin

ASJC Scopus subject areas

  • Public Health, Environmental and Occupational Health
  • Endocrinology
  • Orthopedics and Sports Medicine
  • Physical Therapy, Sports Therapy and Rehabilitation

Cite this

The giant muscle protein titin is an adjustable molecular spring. / Granzier, Hendrikus "Henk"; Labeit, Siegfried.

In: Exercise and Sport Sciences Reviews, Vol. 34, No. 2, 04.2006, p. 50-53.

Research output: Contribution to journalArticle

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