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Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells

Please always quote using this URN: urn:nbn:de:bvb:20-opus-121835
  • 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 isBackground: 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.show moreshow less

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Metadaten
Author: Mariana S. Dietz, Daniel Hasse, Davide M. Ferraris, Antonia Göhler, Hartmut H. Niemann, Mike Heilemann
URN:urn:nbn:de:bvb:20-opus-121835
Document Type:Journal article
Faculties:Fakultät für Biologie / Theodor-Boveri-Institut für Biowissenschaften
Language:English
Parent Title (English):BMC Biophysics
ISSN:2046-1682
Year of Completion:2013
Volume:6
Issue:6
Source:BMC Biophysics 2013, 6:6. doi:10.1186/2046-1682-6-6
DOI:https://doi.org/10.1186/2046-1682-6-6
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 571 Physiologie und verwandte Themen
Tag:EGF receptor; MET receptor; SEMA domain; Scatter factor; Signal transduction; dimerization; fluorescence; fluorescence correlation spectroscopy; hepatocyte-growth-factor; invasion protein-INLB; listeria-monocytogenes; living cells; rat hepatocytes; single-molecule photobleaching; structural insights; tyrosine kinase
Release Date:2016/02/22
Licence (German):License LogoCC BY: Creative-Commons-Lizenz: Namensnennung