Live cell imaging shows hepatocyte growth factor-induced Met dimerization

Koschut D, Richert L, Pace G, Niemann H, Mely Y, Orian-Rousseau V (2016)
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 1863(7): 1552-1558.

Download
No fulltext has been uploaded. References only!
Journal Article | Original Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Abstract
The canonical model of receptor tyrosine kinase (RTK) activation assumes that ligand-induced dimerization of inactive receptor monomers is a prerequisite for autophosphorylation. For several RTK families, recent results of fluorescence microscopy provided evidence for preformed receptor dimers that may or may not require ligand binding for kinase activity. Here we report, for the first time, the application of advanced quantitative fluorescence microscopy techniques to study changes in the oligomerization state of the RTK Met in response to stimulation by its endogenous ligand hepatocyte growth factor (HGF). We used inducible C-terminal fusions be, tween Met and enhanced green fluorescent protein (EGFP) or red fluorescent protein (RFP) in combination with fluorescence resonance energy transfer (FRET)-based fluorescence-lifetime imaging microscopy (FLIM) and fluorescence correlation spectroscopy (FCS). A small fraction of HGF-independent Met dimers appeared to be present in cells even at low receptor density. At high receptor density, both the fraction of Met dimers and the level of Met autophosphorylation increased in the absence of HGF. Stimulation with HGF at low receptor density significantly increased the fraction of Met dimers on live cells. We found no indications of Met oligomers larger than dimers. Our findings thus confirm a model of Met activation through HGF-induced dimerization and at the same time they support previous reports of Met dimers in unstimulated cells. The tools established in this work will be useful to further characterize the mechanism of Met activation and to define the contribution of co-receptors. (C) 2016 Elsevier B.V. All rights reserved.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Koschut D, Richert L, Pace G, Niemann H, Mely Y, Orian-Rousseau V. Live cell imaging shows hepatocyte growth factor-induced Met dimerization. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH. 2016;1863(7):1552-1558.
Koschut, D., Richert, L., Pace, G., Niemann, H., Mely, Y., & Orian-Rousseau, V. (2016). Live cell imaging shows hepatocyte growth factor-induced Met dimerization. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1863(7), 1552-1558. doi:10.1016/j.bbamcr.2016.04.015
Koschut, D., Richert, L., Pace, G., Niemann, H., Mely, Y., and Orian-Rousseau, V. (2016). Live cell imaging shows hepatocyte growth factor-induced Met dimerization. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 1863, 1552-1558.
Koschut, D., et al., 2016. Live cell imaging shows hepatocyte growth factor-induced Met dimerization. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1863(7), p 1552-1558.
D. Koschut, et al., “Live cell imaging shows hepatocyte growth factor-induced Met dimerization”, BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, vol. 1863, 2016, pp. 1552-1558.
Koschut, D., Richert, L., Pace, G., Niemann, H., Mely, Y., Orian-Rousseau, V.: Live cell imaging shows hepatocyte growth factor-induced Met dimerization. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH. 1863, 1552-1558 (2016).
Koschut, David, Richert, Ludovic, Pace, Giuseppina, Niemann, Hartmut, Mely, Yves, and Orian-Rousseau, Veronique. “Live cell imaging shows hepatocyte growth factor-induced Met dimerization”. BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH 1863.7 (2016): 1552-1558.
This data publication is cited in the following publications:
This publication cites the following data publications:

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 27094128
PubMed | Europe PMC

Search this title in

Google Scholar