Unknown

Dataset Information

0

?-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk.


ABSTRACT: 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 cross-linker ?-actinin. The calmodulin-like domain of ?-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 ?-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 ?-actinin/Z-repeat interactions cooperate to ensure long-term stable titin anchoring while allowing the individual components to exchange dynamically.

SUBMITTER: Grison M 

PROVIDER: S-EPMC5293040 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

α-Actinin/titin interaction: A dynamic and mechanically stable cluster of bonds in the muscle Z-disk.

Grison Marco M   Merkel Ulrich U   Kostan Julius J   Djinović-Carugo Kristina K   Rief Matthias M  

Proceedings of the National Academy of Sciences of the United States of America 20170117 5


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 cross-linker α-actinin. The calmodulin-like domain of α-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-molec  ...[more]

Similar Datasets

| S-EPMC2475687 | biostudies-literature
| S-EPMC2726412 | biostudies-literature
| S-EPMC305858 | biostudies-literature
| S-EPMC1170509 | biostudies-other
| S-EPMC3308006 | biostudies-literature
| S-EPMC3931057 | biostudies-literature
| S-EPMC6481931 | biostudies-literature
| S-EPMC3647160 | biostudies-literature
| S-EPMC3241960 | biostudies-literature
| S-EPMC6204599 | biostudies-literature