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Nanosurgical Manipulation of Titin and Its M-Complex

  • Titin is a multifunctional filamentous protein anchored in the M-band, a hexagonally organized supramolecular lattice in the middle of the muscle sarcomere. Functionally, the M-band is a framework that cross-links myosin thick filaments, organizes associated proteins, and maintains sarcomeric symmetry via its structural and putative mechanical properties. Part of the M-band appears at the C-terminal end of isolated titin molecules in the form of a globular head, named here the “M-complex”, which also serves as the point of head-to-head attachment of titin. We used high-resolution atomic force microscopy and nanosurgical manipulation to investigate the topographical and internal structure and local mechanical properties of the M-complex and its associated titin molecules. We find that the M-complex is a stable structure that corresponds to the transverse unit of the M-band organized around the myosin thick filament. M-complexes may be interlinked into an M-complex array that reflects the local structural and mechanical status of the transversal M-band lattice. Local segments of titin and the M-complex could be nanosurgically manipulated to achieve extension and domain unfolding. Long threads could be pulled out of the M-complex, suggesting that it is a compact supramolecular reservoir of extensible filaments. Nanosurgery evoked an unexpected volume increment in the M-complex, which may be related to its function as a mechanical spacer. The M-complex thus displays both elastic and plastic properties which support the idea that the M-band may be involved in mechanical functions within the muscle sarcomere.

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Metadaten
Author: Dominik Sziklai, Judit Sallai, Zsombor Papp, Dalma Kellermayer, Zsolt Mártonfalvi, Ricardo H. Pires, Miklós S. Z. Kellermayer
URN:urn:nbn:de:gbv:9-opus-59375
DOI:https://doi.org/10.3390/nano12020178
ISSN:2079-4991
Parent Title (English):Nanomaterials
Publisher:MDPI
Place of publication:Basel
Editor: Gabriel Žoldák
Document Type:Article
Language:English
Date of first Publication:2022/01/06
Release Date:2022/07/05
Tag:atomic force microscopy; domain unfolding; mechanical stability; molecular mechanics; nanomanipulation; polymer extension; titin
GND Keyword:-
Volume:12
Article Number:178
Page Number:17
Faculties:Universitätsmedizin
Licence (German):License LogoCreative Commons - Namensnennung