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Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin.

The sarcomeric Z-disk, the anchoring plane of thin (actin) filaments, links titin (also called connectin) and actin filaments from opposing sarcomere halves in a lattice connected by alpha-actinin. We demonstrate by protein interaction analysis that two types of titin interactions are involved in the assembly of alpha-actinin into the Z-disk. Titin interacts via a single binding site with the two central spectrin-like repeats of the outermost pair of alpha-actinin molecules. In the central Z-disk, titin can interact with multiple alpha-actinin molecules via their C-terminal domains. These interactions allow the assembly of a ternary complex of titin, actin and alpha-actinin in vitro, and are expected to constrain the path of titin in the Z-disk. In thick skeletal muscle Z-disks, titin filaments cross over the Z-disk centre by approximately 30 nm, suggesting that their alpha-actinin-binding sites overlap in an antiparallel fashion. The combination of our biochemical and ultrastructural data now allows a molecular model of the sarcomeric Z-disk, where overlapping titin filaments and their interactions with the alpha-actinin rod and C-terminal domain can account for the essential ultrastructural features.

Pubmed ID: 9501083


  • Young P
  • Ferguson C
  • BaƱuelos S
  • Gautel M


The EMBO journal

Publication Data

March 16, 1998

Associated Grants


Mesh Terms

  • Actin Cytoskeleton
  • Actinin
  • Actins
  • Amino Acid Sequence
  • Animals
  • Chickens
  • Connectin
  • Humans
  • Ligands
  • Molecular Sequence Data
  • Muscle Proteins
  • Muscle, Skeletal
  • Protein Kinases
  • Rabbits
  • Sarcomeres
  • Spectrin