Single-molecule Photobleaching Reveals Increased MET Receptor Dimerization Upon Ligand Binding in Intact Cells

Overview

Journal BMC Biophys

Specialty Biophysics

Date 2013 Jun 5

PMID 23731667

Citations 23

Authors

Marina S Dietz

Daniel Hasse

Davide M Ferraris

Antonia Gohler

Hartmut H Niemann

Mike Heilemann

Affiliations

Soon will be listed here.

Abstract

Background: The human receptor tyrosine kinase MET and its ligand hepatocyte growth factor/scatter factor are essential during embryonic development and play an important role during cancer metastasis and tissue regeneration. In addition, it was found that MET is also relevant for infectious diseases and is the target of different bacteria, amongst them Listeria monocytogenes that induces bacterial uptake through the surface protein internalin B. Binding of ligand to the MET receptor is proposed to lead to receptor dimerization. However, it is also discussed whether preformed MET dimers exist on the cell membrane.

Results: To address these issues we used single-molecule fluorescence microscopy techniques. Our photobleaching experiments show that MET exists in dimers on the membrane of cells in the absence of ligand and that the proportion of MET dimers increases significantly upon ligand binding.

Conclusions: Our results indicate that partially preformed MET dimers may play a role in ligand binding or MET signaling. The addition of the bacterial ligand internalin B leads to an increase of MET dimers which is in agreement with the model of ligand-induced dimerization of receptor tyrosine kinases.

Citing Articles

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