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Recombinant aequorin and green fluorescent protein as valuable tools in the study of cell signalling.

Authors :
Chiesa A
Rapizzi E
Tosello V
Pinton P
de Virgilio M
Fogarty KE
Rizzuto R
Source :
The Biochemical journal [Biochem J] 2001 Apr 01; Vol. 355 (Pt 1), pp. 1-12.
Publication Year :
2001

Abstract

Luminous proteins include primary light producers, such as aequorin, and secondary photoproteins that in some organisms red-shift light emission for better penetration in space. When expressed in heterologous systems, both types of proteins may act as versatile reporters capable of monitoring phenomena as diverse as calcium homoeostasis, protein sorting, gene expression, and so on. The Ca(2+)-sensitive photoprotein aequorin was targeted to defined intracellular locations (organelles, such as mitochondria, endoplasmic reticulum, sarcoplasmic reticulum, Golgi apparatus and nucleus, and cytoplasmic regions, such as the bulk cytosol and the subplasmalemmal rim), and was used to analyse Ca(2+) homoeostasis at the subcellular level. We will discuss this application, reviewing its advantages and disadvantages and the experimental procedure. The applications of green fluorescent protein (GFP) are even broader. Indeed, the ability to molecularly engineer and recombinantly express a strongly fluorescent probe has provided a powerful tool for investigating a wide variety of biological events in live cells (e.g. tracking of endogenous proteins, labelling of intracellular structures, analysing promoter activity etc.). More recently, the demonstration that, using appropriate mutants and/or fusion proteins, GFP fluorescence can become sensitive to physiological parameters or activities (ion concentration, protease activity, etc.) has further expanded its applications and made GFP the favourite probe of cell biologists. We will here present two applications in the field of cell signalling, i.e. the use of GFP chimaeras for studying the recruitment of protein kinase C isoforms and the activity of intracellular proteases.

Details

Language :
English
ISSN :
0264-6021
Volume :
355
Issue :
Pt 1
Database :
MEDLINE
Journal :
The Biochemical journal
Publication Type :
Academic Journal
Accession number :
11256942
Full Text :
https://doi.org/10.1042/0264-6021:3550001