Applications of fluorescence resonance energy transfer for mapping biological membranes

J. Szöllősi, Péter Nagy, Zsolt Sebestyén, S. Damjanovich, John W. Park, L. Mátyus

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The interaction of the cell surface proteins plays a key role in the process of transmembrane signaling. Receptor clustering and changes in their conformation are often essential factors in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool for determining distance relationships and supramolecular organization of cell surface molecules. This paper reviews the theoretical background of fluorescence resonance energy transfer, its flow cytometric and microscopic applications (including the intensity based and photobleaching versions), and provides a critical evaluation of the methods as well. In order to illustrate the applicability of the method, we summarize a few biological results: clustering of lectin receptors, cell surface distribution of hematopoietic cluster of differentiation (CD) molecules, and that of the receptor tyrosine kinases, conformational changes of Major Histocompatibility Complex (MHC) I molecules upon membrane potential change and ligand binding.

Original languageEnglish
Pages (from-to)251-266
Number of pages16
JournalReviews in Molecular Biotechnology
Volume82
Issue number3
DOIs
Publication statusPublished - 2002

Fingerprint

Fluorescence Resonance Energy Transfer
Cluster Analysis
Mitogen Receptors
Ligands
Photobleaching
Membranes
Receptor Protein-Tyrosine Kinases
Major Histocompatibility Complex
Membrane Potentials
Membrane Proteins

Keywords

  • Antigen presentation
  • Cell surface receptor conformation
  • Flow cytometry
  • Fluorescence microscopy
  • Fluorescence resonance energy transfer
  • Membrane potential

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Biotechnology

Cite this

Applications of fluorescence resonance energy transfer for mapping biological membranes. / Szöllősi, J.; Nagy, Péter; Sebestyén, Zsolt; Damjanovich, S.; Park, John W.; Mátyus, L.

In: Reviews in Molecular Biotechnology, Vol. 82, No. 3, 2002, p. 251-266.

Research output: Contribution to journalArticle

@article{1506bb1dbbf14041adcb8ffb6d60005d,
title = "Applications of fluorescence resonance energy transfer for mapping biological membranes",
abstract = "The interaction of the cell surface proteins plays a key role in the process of transmembrane signaling. Receptor clustering and changes in their conformation are often essential factors in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool for determining distance relationships and supramolecular organization of cell surface molecules. This paper reviews the theoretical background of fluorescence resonance energy transfer, its flow cytometric and microscopic applications (including the intensity based and photobleaching versions), and provides a critical evaluation of the methods as well. In order to illustrate the applicability of the method, we summarize a few biological results: clustering of lectin receptors, cell surface distribution of hematopoietic cluster of differentiation (CD) molecules, and that of the receptor tyrosine kinases, conformational changes of Major Histocompatibility Complex (MHC) I molecules upon membrane potential change and ligand binding.",
keywords = "Antigen presentation, Cell surface receptor conformation, Flow cytometry, Fluorescence microscopy, Fluorescence resonance energy transfer, Membrane potential",
author = "J. Sz{\"o}llősi and P{\'e}ter Nagy and Zsolt Sebesty{\'e}n and S. Damjanovich and Park, {John W.} and L. M{\'a}tyus",
year = "2002",
doi = "10.1016/S1389-0352(01)00041-1",
language = "English",
volume = "82",
pages = "251--266",
journal = "Reviews in Molecular Biotechnology",
issn = "1389-0352",
publisher = "Elsevier BV",
number = "3",

}

TY - JOUR

T1 - Applications of fluorescence resonance energy transfer for mapping biological membranes

AU - Szöllősi, J.

AU - Nagy, Péter

AU - Sebestyén, Zsolt

AU - Damjanovich, S.

AU - Park, John W.

AU - Mátyus, L.

PY - 2002

Y1 - 2002

N2 - The interaction of the cell surface proteins plays a key role in the process of transmembrane signaling. Receptor clustering and changes in their conformation are often essential factors in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool for determining distance relationships and supramolecular organization of cell surface molecules. This paper reviews the theoretical background of fluorescence resonance energy transfer, its flow cytometric and microscopic applications (including the intensity based and photobleaching versions), and provides a critical evaluation of the methods as well. In order to illustrate the applicability of the method, we summarize a few biological results: clustering of lectin receptors, cell surface distribution of hematopoietic cluster of differentiation (CD) molecules, and that of the receptor tyrosine kinases, conformational changes of Major Histocompatibility Complex (MHC) I molecules upon membrane potential change and ligand binding.

AB - The interaction of the cell surface proteins plays a key role in the process of transmembrane signaling. Receptor clustering and changes in their conformation are often essential factors in the final outcome of ligand receptor interactions. Fluorescence resonance energy transfer (FRET) is an excellent tool for determining distance relationships and supramolecular organization of cell surface molecules. This paper reviews the theoretical background of fluorescence resonance energy transfer, its flow cytometric and microscopic applications (including the intensity based and photobleaching versions), and provides a critical evaluation of the methods as well. In order to illustrate the applicability of the method, we summarize a few biological results: clustering of lectin receptors, cell surface distribution of hematopoietic cluster of differentiation (CD) molecules, and that of the receptor tyrosine kinases, conformational changes of Major Histocompatibility Complex (MHC) I molecules upon membrane potential change and ligand binding.

KW - Antigen presentation

KW - Cell surface receptor conformation

KW - Flow cytometry

KW - Fluorescence microscopy

KW - Fluorescence resonance energy transfer

KW - Membrane potential

UR - http://www.scopus.com/inward/record.url?scp=0036176443&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036176443&partnerID=8YFLogxK

U2 - 10.1016/S1389-0352(01)00041-1

DO - 10.1016/S1389-0352(01)00041-1

M3 - Article

VL - 82

SP - 251

EP - 266

JO - Reviews in Molecular Biotechnology

JF - Reviews in Molecular Biotechnology

SN - 1389-0352

IS - 3

ER -