The giant muscle protein titin is an adjustable molecular spring

Exerc Sport Sci Rev. 2006 Apr;34(2):50-3. doi: 10.1249/00003677-200604000-00002.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium / pharmacology
  • Connectin
  • Elasticity
  • Humans
  • Muscle Proteins / drug effects
  • Muscle Proteins / genetics
  • Muscle Proteins / physiology*
  • Muscles / cytology
  • Muscles / physiology*
  • Protein Isoforms / agonists
  • Protein Kinases / drug effects
  • Protein Kinases / genetics
  • Protein Kinases / physiology*
  • Protein Processing, Post-Translational / physiology
  • Sarcomeres / genetics
  • Sarcomeres / physiology
  • Tensile Strength / physiology

Substances

  • Connectin
  • Muscle Proteins
  • Protein Isoforms
  • TTN protein, human
  • Protein Kinases
  • Calcium