Dynamic Strength of Titin's Z-Disk End

Author:

Kollár Veronika1,Szatmári Dávid1,Grama László1,Kellermayer Miklós S. Z.2

Affiliation:

1. Department of Biophysics, Faculty of Medicine, University of Pécs, Szigeti ut 12., Pécs 7624, Hungary

2. Department of Biophysics and Radiation Biology, Faculty of Medicine, Semmelweis University, Tűzoltó u. 37-47., Budapest 1094, Hungary

Abstract

Titin is a giant filamentous protein traversing the half sarcomere of striated muscle with putative functions as diverse as providing structural template, generating elastic response, and sensing and relaying mechanical information. The Z-disk region of titin, which corresponds to the N-terminal end of the molecule, has been thought to be a hot spot for mechanosensing while also serving as anchorage for its sarcomeric attachment. Understanding the mechanics of titin's Z-disk region, particularly under the effect of binding proteins, is of great interest. Here we briefly review recent findings on the structure, molecular associations, and mechanics of titin's Z-disk region. In addition, we report experimental results on the dynamic strength of titin's Z1Z2 domains measured by nanomechanical manipulation of the chemical dimer of a recombinant protein fragment.

Funder

Hungarian Science Foundation

Publisher

Hindawi Limited

Subject

Health, Toxicology and Mutagenesis,Genetics,Molecular Biology,Molecular Medicine,General Medicine,Biotechnology

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