Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 5, Pages 1015-1020Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1612681114
Keywords
alpha-actinin; titin Z-repeats; Z-disk mechanics; optical tweezers
Categories
Funding
- Marie Curie Initial Training Network MUZIC Grant [238423]
- Austrian Science Fund [I525, I1593, P22276, P19060]
- Federal Ministry of Economy, Family and Youth through the initiative, Laura Bassi Centres of Expertise
- Center of Optimized Structural Studies Grant [253275]
- University of Vienna
- Deutsche Forschungsgemeinschaft [FOR 1352 P8]
- Austrian Science Fund (FWF) [I1593, P19060, I525] Funding Source: Austrian Science Fund (FWF)
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Stable anchoring of titin within the muscle Z-disk is essential for preserving muscle integrity during passive stretching. One of the main candidates for anchoring titin in the Z-disk is the actin crosslinker a-actinin. The calmodulin-like domain of alpha-actinin binds to the Z-repeats of titin. However, the mechanical and kinetic properties of this important interaction are still unknown. Here, we use a dual-beam optical tweezers assay to study the mechanics of this interaction at the single-molecule level. A single interaction of alpha-actinin and titin turns out to be surprisingly weak if force is applied. Depending on the direction of force application, the unbinding forces can more than triple. Our results suggest a model where multiple alpha-actinin/Z-repeat interactions cooperate to ensure long-term stable titin anchoring while allowing the individual components to exchange dynamically.
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