Novel Single Cell Fluorescence Approaches in the Investigation of Signaling at the Cellular Level

Nagy, Péter; Vereb, György; Post, Janine N.; Friedländer, Elza; Szölloősi, János

doi:10.1007/3-540-26511-2_2

Cited by 4 publications

(3 citation statements)

References 163 publications

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“…Several polypeptide growth factors which are overproduced in tumors can bind to these ErbB proteins, except for ErbB2, leading to induction of intracellular signaling via phosphorylation of cytoplasmic tyrosine residues. Surprisingly heteroassociation of ErbB3, which is kinase deficient, with ErbB2, which has no physiological ligands, has been found to constitute the most potent mitogenic pairing among all ErbB combinations [ 9 , 141 ]. Due to the high expression of these proteins, availability of many model cancer cell lines, and the great therapeutic importance of ErbB proteins, these proteins have been among the most widely studied RTKs.…”

Section: Applications Of Fret In Membrane Biologymentioning

confidence: 99%

“…In fact, these proteins present yet another convincing example to show that cellular fate is reflected by the distribution patterns of the molecular species in the membrane. Studies on ErbB proteins using various FRET approaches revealed that all ErbB kinases have formed homo- and hetero-assemblies in the plasma membrane [ 9 , 13 , 82 , 142 ]. We wanted to understand the degree of clustering of ErbB1 and ErbB2 receptors in cancer cell lines; therefore, we performed anisotropy-based homoFRET measurements in a flow cytometer.…”

Section: Applications Of Fret In Membrane Biologymentioning

confidence: 99%

“…FRET is a collision-free, but distance-dependent photophysical process where radiationless transfer of energy occurs from an excited donor (D) fluorophore to a suitable acceptor (A) protein or fluorophore via long-range dipole–dipole coupling mechanism. Donor absorbs energy at shorter wavelength whereas acceptor has energy absorption at longer wavelength [ 9 , 10 ]. FRET occurs over interatomic distances due to resonance-based interaction of chromophores without transmission of photons from donor to acceptor species.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Understanding FRET as a Research Tool for Cellular Studies

Shrestha

Jenei

Nagy

et al. 2015

IJMS

Self Cite

165

137

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Communication of molecular species through dynamic association and/or dissociation at various cellular sites governs biological functions. Understanding these physiological processes require delineation of molecular events occurring at the level of individual complexes in a living cell. Among the few non-invasive approaches with nanometer resolution are methods based on Förster Resonance Energy Transfer (FRET). FRET is effective at a distance of 1–10 nm which is equivalent to the size of macromolecules, thus providing an unprecedented level of detail on molecular interactions. The emergence of fluorescent proteins and SNAP- and CLIP- tag proteins provided FRET with the capability to monitor changes in a molecular complex in real-time making it possible to establish the functional significance of the studied molecules in a native environment. Now, FRET is widely used in biological sciences, including the field of proteomics, signal transduction, diagnostics and drug development to address questions almost unimaginable with biochemical methods and conventional microscopies. However, the underlying physics of FRET often scares biologists. Therefore, in this review, our goal is to introduce FRET to non-physicists in a lucid manner. We will also discuss our contributions to various FRET methodologies based on microscopy and flow cytometry, while describing its application for determining the molecular heterogeneity of the plasma membrane in various cell types.

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Section: Applications Of Fret In Membrane Biologymentioning

confidence: 99%

Section: Applications Of Fret In Membrane Biologymentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Understanding FRET as a Research Tool for Cellular Studies

Shrestha

Jenei

Nagy

et al. 2015

IJMS

Self Cite

165

137

View full text Add to dashboard Cite

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Using FRAP to Quantify Changes in Transcription Factor Dynamics After Cell Stimulation: Cell Culture, FRAP, Data Analysis, and Visualization

Govindaraj

Post

2020

Methods in Molecular Biology

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Imaging molecular interactions in living cells by FRET microscopy

Jares‐Erijman

Jovin

2006

Current Opinion in Chemical Biology

286

167

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Förster resonance energy transfer (FRET) is applied extensively in all fields of biological research and technology, generally as a 'nanoruler' with a dynamic range corresponding to the intramolecular and intermolecular distances characterizing the molecular structures that regulate cellular function. The complex underlying network of interactions reflects elementary reactions operating under strict spatio-temporal control: binding, conformational transition, covalent modification and transport. FRET imaging provides information about all these molecular processes with high specificity and sensitivity via probes expressed by or introduced from the external medium into the cell, tissue or organism. Current approaches and developments in the field are discussed with emphasis on formalism, probes and technical implementation.

show abstract

Novel Single Cell Fluorescence Approaches in the Investigation of Signaling at the Cellular Level

Cited by 4 publications

References 163 publications

Understanding FRET as a Research Tool for Cellular Studies

Understanding FRET as a Research Tool for Cellular Studies

Using FRAP to Quantify Changes in Transcription Factor Dynamics After Cell Stimulation: Cell Culture, FRAP, Data Analysis, and Visualization

Imaging molecular interactions in living cells by FRET microscopy

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