ArticleProceedings of the National Academy of Sciences of the United States of America2009
Single-molecule force spectroscopy distinguishes target binding modes of calmodulin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 53 citations in OpenAlex.
- Force-Induced Ankle Opening Reveals Mechanical Stabilization of the Ankle of Human β-Cardiac Myosin.ACS nano · 2026Article
- Further Evidence of the Melatonin Calmodulin Interaction: Effect on CaMKII Activity.International journal of molecular sciences · 2022Article
- Model systems for optical trapping: the physical basis and biological applications.Biophysical reviews · 2021Review
- Depicting Conformational Ensembles of α-Synuclein by Single Molecule Force Spectroscopy and Native Mass Spectroscopy.International journal of molecular sciences · 2019Article
- Unraveling the Mechanical Unfolding Pathways of a Multidomain Protein: Phosphoglycerate Kinase.Biophysical journal · 2018Article
- Synthetic oligorotaxanes exert high forces when folding under mechanical load.Nature nanotechnology · 2018Article
- Improving single molecule force spectroscopy through automated real-time data collection and quantification of experimental conditions.Ultramicroscopy · 2014Article
- Protein folding and unfolding under force.Biopolymers · 2013Article
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Mechanical anisotropy of ankyrin repeats.Biophysical journal · 2012Article
- Article
- Single-molecule force spectroscopy reveals the individual mechanical unfolding pathways of a surface layer protein.The Journal of biological chemistry · 2011Article
- Protein folding at single-molecule resolution.Biochimica et biophysica acta · 2011Review
- The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.PLoS computational biology · 2011Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The eukaryotic signaling protein calmodulin (CaM) can bind to more than 300 known target proteins to regulate numerous functions in our body in a calcium-dependent manner. How CaM distinguishes between these various targets is still largely unknown. Here, we investigate fluctuations of the complex formation of CaM and its target peptide sequences using single-molecule force spectroscopy by AFM. By applying mechanical force, we can steer a single CaM molecule through its folding energy landscape from the fully unfolded state to the native target-bound state revealing equilibrium fluctuations between numerous intermediate states. We find that the prototypical CaM target sequence skMLCK, a fragment from skeletal muscle myosin light chain kinase, binds to CaM in a highly cooperative way, while only a lower degree of interdomain binding cooperativity emerges for CaMKK, a target peptide from CaM-dependent kinase kinase. We identify minimal binding motifs for both of these peptides, confirming that affinities of target peptides are not exclusively determined by their pattern of hydrophobic anchor residues. Our results reveal an association mode for CaMKK in which the peptide binds strongly to only partially Ca(2+)-saturated CaM. This binding mode might allow for a fine-tuning of the intracellular response to changes in Ca(2+) concentration.
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