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

Dietz MS, Haße D, Ferraris DM, Göhler A, Niemann H, Heilemann M (2013)
BMC biophysics 6(1): 6.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
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.
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BMC biophysics
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Dietz MS, Haße D, Ferraris DM, Göhler A, Niemann H, Heilemann M. Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells. BMC biophysics. 2013;6(1):6.
Dietz, M. S., Haße, D., Ferraris, D. M., Göhler, A., Niemann, H., & Heilemann, M. (2013). Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells. BMC biophysics, 6(1), 6. doi:10.1186/2046-1682-6-6
Dietz, M. S., Haße, D., Ferraris, D. M., Göhler, A., Niemann, H., and Heilemann, M. (2013). Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells. BMC biophysics 6, 6.
Dietz, M.S., et al., 2013. Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells. BMC biophysics, 6(1), p 6.
M.S. Dietz, et al., “Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells”, BMC biophysics, vol. 6, 2013, pp. 6.
Dietz, M.S., Haße, D., Ferraris, D.M., Göhler, A., Niemann, H., Heilemann, M.: Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells. BMC biophysics. 6, 6 (2013).
Dietz, Marina S., Haße, Daniel, Ferraris, Davide M., Göhler, Antonia, Niemann, Hartmut, and Heilemann, Mike. “Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells”. BMC biophysics 6.1 (2013): 6.

15 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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PMID: 25521567
Direct binding of hepatocyte growth factor and vascular endothelial growth factor to CD44v6.
Volz Y, Koschut D, Matzke-Ogi A, Dietz MS, Karathanasis C, Richert L, Wagner MG, Mély Y, Heilemann M, Niemann HH, Orian-Rousseau V., Biosci Rep 35(4), 2015
PMID: 26181364
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PMID: 24519400
Receptor-ligand interactions: binding affinities studied by single-molecule and super-resolution microscopy on intact cells.
Dietz MS, Fricke F, Krüger CL, Niemann HH, Heilemann M., Chemphyschem 15(4), 2014
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50 References

Daten bereitgestellt von Europe PubMed Central.

Met, metastasis, motility and more.
Birchmeier C, Birchmeier W, Gherardi E, Vande Woude GF., Nat. Rev. Mol. Cell Biol. 4(12), 2003
PMID: 14685170
Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family.
Dramsi S, Biswas I, Maguin E, Braun L, Mastroeni P, Cossart P., Mol. Microbiol. 16(2), 1995
PMID: 7565087
InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase.
Shen Y, Naujokas M, Park M, Ireton K., Cell 103(3), 2000
PMID: 11081636
InlB: an invasion protein of Listeria monocytogenes with a novel type of surface association.
Braun L, Dramsi S, Dehoux P, Bierne H, Lindahl G, Cossart P., Mol. Microbiol. 25(2), 1997
PMID: 9282740
Structure of the human receptor tyrosine kinase met in complex with the Listeria invasion protein InlB.
Niemann HH, Jager V, Butler PJ, van den Heuvel J, Schmidt S, Ferraris D, Gherardi E, Heinz DW., Cell 130(2), 2007
PMID: 17662939
Cell signaling by receptor tyrosine kinases.
Schlessinger J., Cell 103(2), 2000
PMID: 11057895
Structural insights into Met receptor activation.
Niemann HH., Eur. J. Cell Biol. 90(11), 2011
PMID: 21242015
Crystal structure of the HGF beta-chain in complex with the Sema domain of the Met receptor.
Stamos J, Lazarus RA, Yao X, Kirchhofer D, Wiesmann C., EMBO J. 23(12), 2004
PMID: 15167892
Structural basis of hepatocyte growth factor/scatter factor and MET signalling.
Gherardi E, Sandin S, Petoukhov MV, Finch J, Youles ME, Ofverstedt LG, Miguel RN, Blundell TL, Vande Woude GF, Skoglund U, Svergun DI., Proc. Natl. Acad. Sci. U.S.A. 103(11), 2006
PMID: 16537482
The Sema domain of Met is necessary for receptor dimerization and activation.
Kong-Beltran M, Stamos J, Wickramasinghe D., Cancer Cell 6(1), 2004
PMID: 15261143
Evidence for non-covalent clusters of the c-met proto-oncogene product.
Faletto DL, Tsarfaty I, Kmiecik TE, Gonzatti M, Suzuki T, Vande Woude GF., Oncogene 7(6), 1992
PMID: 1317541
GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation.
Banerjee M, Copp J, Vuga D, Marino M, Chapman T, van der Geer P, Ghosh P., Mol. Microbiol. 52(1), 2004
PMID: 15049825
Ligand-mediated dimerization of the Met receptor tyrosine kinase by the bacterial invasion protein InlB.
Ferraris DM, Gherardi E, Di Y, Heinz DW, Niemann HH., J. Mol. Biol. 395(3), 2009
PMID: 19900460
X-ray and neutron small-angle scattering analysis of the complex formed by the Met receptor and the Listeria monocytogenes invasion protein InlB.
Niemann HH, Petoukhov MV, Hartlein M, Moulin M, Gherardi E, Timmins P, Heinz DW, Svergun DI., J. Mol. Biol. 377(2), 2008
PMID: 18262542
Surfing on a new wave of single-molecule fluorescence methods.
Hohlbein J, Gryte K, Heilemann M, Kapanidis AN., Phys Biol 7(3), 2010
PMID: 20686191
Subunit counting in membrane-bound proteins.
Ulbrich MH, Isacoff EY., Nat. Methods 4(4), 2007
PMID: 17369835
Functional stoichiometry of the unitary calcium-release-activated calcium channel.
Ji W, Xu P, Li Z, Lu J, Liu L, Zhan Y, Chen Y, Hille B, Xu T, Chen L., Proc. Natl. Acad. Sci. U.S.A. 105(36), 2008
PMID: 18757751
Single-molecule imaging reveals transforming growth factor-beta-induced type II receptor dimerization.
Zhang W, Jiang Y, Wang Q, Ma X, Xiao Z, Zuo W, Fang X, Chen YG., Proc. Natl. Acad. Sci. U.S.A. 106(37), 2009
PMID: 19720988
Single-molecule analysis of epidermal growth factor binding on the surface of living cells.
Teramura Y, Ichinose J, Takagi H, Nishida K, Yanagida T, Sako Y., EMBO J. 25(18), 2006
PMID: 16946702
In vivo direct molecular imaging of early tumorigenesis and malignant progression induced by transgenic expression of GFP-Met.
Moshitch-Moshkovitz S, Tsarfaty G, Kaufman DW, Stein GY, Shichrur K, Solomon E, Sigler RH, Resau JH, Vande Woude GF, Tsarfaty I., Neoplasia 8(5), 2006
PMID: 16790084
Met, the hepatocyte growth factor receptor, localizes to the nucleus in cells at low density.
Pozner-Moulis S, Pappas DJ, Rimm DL., Cancer Res. 66(16), 2006
PMID: 16912172
Targeting the tumor and its microenvironment by a dual-function decoy Met receptor.
Michieli P, Mazzone M, Basilico C, Cavassa S, Sottile A, Naldini L, Comoglio PM., Cancer Cell 6(1), 2004
PMID: 15261142
Met activation and receptor dimerization in cancer: a role for the Sema domain.
Wickramasinghe D, Kong-Beltran M., Cell Cycle 4(5), 2005
PMID: 15846105
Identification and partial characterization of receptor binding sites for HGF on rat hepatocytes.
Zarnegar R, DeFrances MC, Oliver L, Michalopoulos G., Biochem. Biophys. Res. Commun. 173(3), 1990
PMID: 2148475
Cell density-dependent regulation of hepatocyte growth factor receptor on adult rat hepatocytes in primary culture.
Mizuno K, Higuchi O, Tajima H, Yonemasu T, Nakamura T., J. Biochem. 114(1), 1993
PMID: 8407884
Characterization of hepatocyte-growth-factor receptors on Meth A cells.
Komada M, Miyazawa K, Ishii T, Kitamura N., Eur. J. Biochem. 204(2), 1992
PMID: 1311683
Subdiffraction-resolution fluorescence imaging with conventional fluorescent probes.
Heilemann M, van de Linde S, Schuttpelz M, Kasper R, Seefeldt B, Mukherjee A, Tinnefeld P, Sauer M., Angew. Chem. Int. Ed. Engl. 47(33), 2008
PMID: 18646237
Analysis of homodimeric avian and human galectins by two methods based on fluorescence spectroscopy: Different structural alterations upon oxidation and ligand binding
AUTHOR UNKNOWN, 2012
Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes.
Machner MP, Frese S, Schubert WD, Orian-Rousseau V, Gherardi E, Wehland J, Niemann HH, Heinz DW., Mol. Microbiol. 48(6), 2003
PMID: 12791136
Fold and function of the InlB B-repeat.
Ebbes M, Bleymuller WM, Cernescu M, Nolker R, Brutschy B, Niemann HH., J. Biol. Chem. 286(17), 2011
PMID: 21345802
Reduction of Dimensionality in Biological Diffusion Processes
AUTHOR UNKNOWN, 1968
Structural basis of MET receptor dimerization by the bacterial invasion protein InlB and the HGF/SF splice variant NK1
AUTHOR UNKNOWN, 2012
A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist.
Tolbert WD, Daugherty J, Gao C, Xie Q, Miranti C, Gherardi E, Vande Woude G, Xu HE., Proc. Natl. Acad. Sci. U.S.A. 104(37), 2007
PMID: 17804794
Structural insights into semaphorins and their receptors.
Siebold C, Jones EY., Semin. Cell Dev. Biol. 24(3), 2012
PMID: 23253452
Deletion of the ectodomain unleashes the transforming, invasive, and tumorigenic potential of the MET oncogene.
Merlin S, Pietronave S, Locarno D, Valente G, Follenzi A, Prat M., Cancer Sci. 100(4), 2009
PMID: 19175607
Regulation of the catalytic activity of the EGF receptor.
Endres NF, Engel K, Das R, Kovacs E, Kuriyan J., Curr. Opin. Struct. Biol. 21(6), 2011
PMID: 21868214
Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation.
Livnah O, Stura EA, Middleton SA, Johnson DL, Jolliffe LK, Wilson IA., Science 283(5404), 1999
PMID: 9974392
Model for growth hormone receptor activation based on subunit rotation within a receptor dimer.
Brown RJ, Adams JJ, Pelekanos RA, Wan Y, McKinstry WJ, Palethorpe K, Seeber RM, Monks TA, Eidne KA, Parker MW, Waters MJ., Nat. Struct. Mol. Biol. 12(9), 2005
PMID: 16116438
Single-molecule imaging of EGFR signalling on the surface of living cells.
Sako Y, Minoghchi S, Yanagida T., Nat. Cell Biol. 2(3), 2000
PMID: 10707088
Spatial control of EGF receptor activation by reversible dimerization on living cells.
Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I., Nature 464(7289), 2010
PMID: 20208517
Functional map and domain structure of MET, the product of the c-met protooncogene and receptor for hepatocyte growth factor/scatter factor.
Gherardi E, Youles ME, Miguel RN, Blundell TL, Iamele L, Gough J, Bandyopadhyay A, Hartmann G, Butler PJ., Proc. Natl. Acad. Sci. U.S.A. 100(21), 2003
PMID: 14528000
Hydrodynamic properties of human adhesion/growth-regulatory galectins studied by fluorescence correlation spectroscopy.
Gohler A, Andre S, Kaltner H, Sauer M, Gabius HJ, Doose S., Biophys. J. 98(12), 2010
PMID: 20550917
Icy: an open bioimage informatics platform for extended reproducible research.
de Chaumont F, Dallongeville S, Chenouard N, Herve N, Pop S, Provoost T, Meas-Yedid V, Pankajakshan P, Lecomte T, Le Montagner Y, Lagache T, Dufour A, Olivo-Marin JC., Nat. Methods 9(7), 2012
PMID: 22743774

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