Related Experiment Video
Updated: Nov 25, 2025
08:28
Measurement of Force-Sensitive Protein Dynamics in Living Cells Using a Combination of Fluorescent Techniques
Published on: November 2, 2018
8.5K
Metavinculin modulates force transduction in cell adhesion sites.
Verena Kanoldt1,2, Carleen Kluger2, Christiane Barz2
1Department of Quantitative Cell Biology, Institute of Molecular Cell Biology, University of Münster, 48149, Münster, Germany.
Nature Communications
|December 18, 2020
Summary
Metavinculin, a heart muscle protein, bears higher forces but is less engaged than vinculin, altering cell adhesion force. However, its absence did not impact cardiac hypertrophy in mice, suggesting a subtle role in heart function.
Area of Science:
- Cellular mechanics
- Molecular biology
- Cardiovascular research
Background:
- Vinculin regulates cellular force transduction.
- Metavinculin, a vinculin splice-isoform in muscle cells, is linked to cardiomyopathies.
- The precise function of metavinculin in heart muscle disorders remains unclear.
Purpose of the Study:
- To investigate the molecular mechanics of metavinculin using piconewton-sensitive tension sensors.
- To determine the in vivo consequences of metavinculin loss using knockout mice.
- To clarify metavinculin's role in cardiac function and heart muscle disorders.
Main Methods:
- Utilized piconewton-sensitive tension sensors to measure metavinculin mechanics in cells.
- Generated and analyzed metavinculin knockout mice.
- Studied tissue response in a cardiac hypertrophy model.
Main Results:
- Metavinculin bears higher molecular forces but is engaged less frequently than vinculin.
- Altered force propagation in cell adhesions was observed due to metavinculin expression.
- Metavinculin knockout mice showed no significant difference in tissue response during cardiac hypertrophy.
Conclusions:
- Metavinculin modulates the transduction of cell adhesion forces.
- The role of metavinculin in heart muscle function and cardiomyopathies is more subtle than previously assumed.
- Further research is needed to fully elucidate metavinculin's contribution to cardiac health and disease.
Related Concept Videos
01:26Tension Response at Adherens Junctions
3.2K
The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin...
3.2K
01:13Cell-matrix's Response to Mechanical Forces
3.2K
In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue.
Anchoring junctions mechanically attach a cell to the...
Anchoring junctions mechanically attach a cell to the...
3.2K
01:17Intracellular Signaling Affects Focal Adhesions
3.2K
Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Some...
3.2K
01:18Role of Myosin in Cell Migration
2.8K
Myosins are multimeric motor proteins involved in various cellular processes such as migration, adhesion, and proliferation. Myosin II is the most common type in animal cells, which binds and cross-links actin filaments.
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
Myosin II is a hexamer comprising two heavy chains with globular heads and coiled-coil tails, two regulatory light chains, and two essential light chains. The ATPase sites on the myosin heads hydrolyze ATP, and the released phosphate generates the force for contraction....
2.8K
01:39Mechanism of Filopodia Formation
2.8K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.8K
01:32Pinching-off of Coated Vesicles
3.7K
Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
3.7K