α-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk
Author(s) -
Marco Grison,
U. Merkel,
Július Košťan,
Kristina DjinovićCarugo,
Matthias Rief
Publication year - 2017
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1612681114
Subject(s) - titin , biophysics , chemical physics , cluster (spacecraft) , molecule , mechanism (biology) , chemistry , materials science , nanotechnology , sarcomere , physics , myocyte , computer science , biology , microbiology and biotechnology , quantum mechanics , programming language , organic chemistry
Significance Muscle is the tissue in our body experiencing most extreme mechanical forces. The mechanism of active force generation has been investigated for more than 50 y and is fairly well understood. However, despite its physiological significance, it is still unknown what mechanical linkages hold together the muscle machinery under passive stretching forces. In this paper, we show with direct mechanical single-molecule measurements that an array of titin/α-actinin bonds composes a dynamic network that can provide stable anchoring, maintaining the integrity of the muscle Z-disk even under load. This dynamic network explains how components of the Z-disk are able to rapidly rearrange and, at the same time, form a long-term stable mechanical structure.
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