ArticleBiophysical journal2009
Determination of dissociation constants in living zebrafish embryos with single wavelength fluorescence cross-correlation spectroscopy.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 92 citations in OpenAlex.
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- Cytoplasmic fluidization contributes to breaking spore dormancy in fission yeast.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Computational Approaches to Predict Protein-Protein Interactions in Crowded Cellular Environments.Chemical reviews · 2024Review
- Current capabilities and future perspectives of FCS: super-resolution microscopy, machine learning, and in vivo applications.Communications biology · 2023Review
- Multicolor fluorescence fluctuation spectroscopy in living cells via spectral detection.eLife · 2021Article
- Integrin intra-heterodimer affinity inversely correlates with integrin activatability.Cell reports · 2021Article
- Wnt3 Is Lipidated at Conserved Cysteine and Serine Residues in Zebrafish Neural Tissue.Frontiers in cell and developmental biology · 2021Article
- Article
- Influence of FRET and fluorescent protein maturation on the quantification of binding affinity with dual-channel fluorescence cross-correlation spectroscopy.Biomedical optics express · 2020Article
- Studying molecular interactions in the intact organism: fluorescence correlation spectroscopy in the living zebrafish embryo.Histochemistry and cell biology · 2020Review
- Splitting the Difference: Sorting Photons to Improve Quantitative Measurements in Correlation Spectroscopy.Biophysical journal · 2020Article
- Adult and Developing Zebrafish as Suitable Models for Cardiac Electrophysiology and Pathology in Research and Industry.Frontiers in physiology · 2020Review
- Single-cell quantification of the concentrations and dissociation constants of endogenous proteins.The Journal of biological chemistry · 2019Article
- Fluorescence techniques in developmental biology.Journal of biosciences · 2018Review
- Quantifying membrane protein oligomerization with fluorescence cross-correlation spectroscopy.Methods (San Diego, Calif.) · 2018Article
- Toward an understanding of biochemical equilibria within living cells.Biophysical reviews · 2018Review
- Dynamic changes in Sox2 spatio-temporal expression promote the second cell fate decision throughThe Biochemical journal · 2018Article
- Article
- Quantifying transcription factor-DNA binding in single cells in vivo with photoactivatable fluorescence correlation spectroscopy.Nature protocols · 2017Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The quantification of biological interactions is very important in life sciences. Here we report for the first time, to our knowledge, the determination of a biomolecular dissociation constant (K(D)) in living zebrafish embryos at physiological protein expression levels. For that purpose, we extend the application of single wavelength fluorescence cross-correlation spectroscopy into small organisms and measure the interaction of Cdc42, a small Rho-GTPase, and IQGAP1, an actin-binding scaffolding protein. Cdc42 and IQGAP1 were labeled with monomeric red fluorescent protein and enhanced green fluorescent protein, respectively. Both fluorophores were excited at a single wavelength of 514 nm, simplifying the fluorescence spectroscopy measurements and allowing quantification. For the determination of the interaction, we used two Cdc42 mutants, the constitutively active Cdc42(G12V) which is in a predominantly GTP-bound form and the dominant-negative GDP-bound Cdc42(T17N). While Cdc42(G12V) binds to IQGAP1 with an apparent K(D) of approximately 100 nM, Cdc42(T17N) has at least a one-order-of-magnitude lower affinity for the same protein. As a comparison, we measure the same protein-protein interactions in Chinese hamster ovary cell cultures but observe significant differences in protein mobility and K(D) from the zebrafish measurements, supporting the notion that bimolecular interactions depend on the biological system under investigation and are best performed under physiologically relevant conditions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.