ArticleNature protocols2015
Dissecting protein reaction dynamics in living cells by fluorescence recovery after photobleaching.
Article in Nature protocols, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 71 citations in OpenAlex.
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- ST3GAL1 and βII-spectrin pathways control CAR T cell migration to target tumors.Nature immunology · 2023Article
- The Utility of Fluorescence Recovery after Photobleaching (FRAP) to Study the Plasma Membrane.Membranes · 2023Review
- SPLIT-PIN software enabling confocal and super-resolution imaging with a virtually closed pinhole.Scientific reports · 2023Article
- Polarized branched Actin modulates cortical mechanics to produce unequal-size daughters during asymmetric division.Nature cell biology · 2023Article
- Targeting cell-matrix interface mechanobiology by integrating AFM with fluorescence microscopy.Progress in biophysics and molecular biology · 2022Review
- A phasor-based approach to improve optical sectioning in any confocal microscope with a tunable pinhole.Microscopy research and technique · 2022Article
- Diffusion and interaction dynamics of the cytosolic peroxisomal import receptor PEX5.Biophysical reports · 2022Article
- Multiphoton intravital microscopy of rodents.Nature reviews. Methods primers · 2022Article
- Actin stabilization in cell migration.Frontiers in cell and developmental biology · 2022Article
- Article
- Cellular Plasticity during Metastasis: New Insights Provided by Intravital Microscopy.Cold Spring Harbor perspectives in medicine · 2020Review
- The cortical actin network regulates avidity-dependent binding of hyaluronan by the lymphatic vessel endothelial receptor LYVE-1.The Journal of biological chemistry · 2020Article
- Quantitative Bio-Imaging Tools to Dissect the Interplay of Membrane and Cytoskeletal Actin Dynamics in Immune Cells.Frontiers in immunology · 2020Review
- Sterile activation of invariant natural killer T cells by ER-stressed antigen-presenting cells.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM-FRAP.Small (Weinheim an der Bergstrasse, Germany) · 2019Article
- Cytoskeletal Control of Antigen-Dependent T Cell Activation.Cell reports · 2019Article
- Statistical Analysis of Scanning Fluorescence Correlation Spectroscopy Data Differentiates Free from Hindered Diffusion.ACS nano · 2018Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins within most macromolecular complexes or organelles continuously turn over. This turnover results from association and dissociation reactions that are mediated by each of the protein's functional domains. Thus, studying organelle or macromolecular formation from the bottom up using theoretical and computational modeling approaches will necessitate the determination of all of these reaction rates in vivo. Yet current methods for examining protein dynamics either necessitate highly specialized equipment or limit themselves to basic measurements. In this protocol, we describe a broadly applicable method based on fluorescence recovery after photobleaching (FRAP) for determining how many reaction processes participate in the turnover of any given protein of interest, for characterizing their apparent association and dissociation rates, and for determining their relative importance in the turnover of the overall protein population. Experiments were performed in melanoma M2 cells expressing mutant forms of ezrin that provide a link between the plasma membrane and the cortical actin cytoskeleton. We also describe a general strategy for the identification of the protein domains that mediate each of the identified turnover processes. Our protocol uses widely available laser-scanning confocal microscopes, open-source software, graphing software and common molecular biology techniques. The entire FRAP experiment preparation, data acquisition and analysis require 3-4 d.
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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.