Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction
The erbB/HER family of transmembrane receptor tyrosine kinases (RTKs) mediate cellular responses to epidermal growth factor (EGF) and related ligands. We have imaged the early stages of RTK-dependent signaling in living cells using: (i) stable expression of erbB1/2/3 fused with visible fluorescent p...
Guardado en:
| Publicado: |
2004
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10870156_v22_n2_p198_Lidke http://hdl.handle.net/20.500.12110/paper_10870156_v22_n2_p198_Lidke |
| Aporte de: |
| id |
paper:paper_10870156_v22_n2_p198_Lidke |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_10870156_v22_n2_p198_Lidke2023-06-08T16:06:10Z Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction Cells Enzymes Semiconductor quantum dots Epidermal growth factors (EGF) Biotechnology citrine epidermal growth factor epidermal growth factor receptor epidermal growth factor receptor 2 epidermal growth factor receptor 3 fluorescent dye hybrid protein ligand monomer oligomer protein tyrosine kinase unclassified drug yellow fluorescent protein animal cell article biotechnology cell line cell strain A431 CHO cell confocal laser microscopy controlled study dimerization endocytosis endosome filopodium flow cytometry fluorescence human human cell internalization ligand binding nonhuman priority journal quantitative analysis quantum mechanics signal transduction Animals Cell Membrane Cricetinae Endosomes Epidermal Growth Factor Humans Motion Oncogene Proteins v-erbB Protein Binding Protein Interaction Mapping Protein Transport Quantum Dots Receptors, Cell Surface Signal Transduction Spectrometry, Fluorescence Animalia The erbB/HER family of transmembrane receptor tyrosine kinases (RTKs) mediate cellular responses to epidermal growth factor (EGF) and related ligands. We have imaged the early stages of RTK-dependent signaling in living cells using: (i) stable expression of erbB1/2/3 fused with visible fluorescent proteins (VFPs), (ii) fluorescent quantum dots (QDs) bearing epidermal growth factor (EGF-QD) and (iii) continuous confocal laser scanning microscopy and flow cytometry. Here we demonstrate that EGF-QDs are highly specific and potent in the binding and activation of the EGF receptor (erbB1), being rapidly internalized into endosomes that exhibit active trafficking and extensive fusion. EGF-QDs bound to erbB1 expressed on filopodia revealed a previously unreported mechanism of retrograde transport to the cell body. When erbB2-monomeric yellow fluorescent protein (mYFP) or erbB3-monomeric Citrine (mCitrine) were coexpressed with erbB1, the rates and extent of endocytosis of EGF-QD and the RTK-VFP demonstrated that erbB2 but not erbB3 heterodimerizes with erbB1 after EGF stimulation, thereby modulating EGF-induced signaling. QD-ligands will find widespread use in basic research and biotechnological developments. 2004 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10870156_v22_n2_p198_Lidke http://hdl.handle.net/20.500.12110/paper_10870156_v22_n2_p198_Lidke |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Cells Enzymes Semiconductor quantum dots Epidermal growth factors (EGF) Biotechnology citrine epidermal growth factor epidermal growth factor receptor epidermal growth factor receptor 2 epidermal growth factor receptor 3 fluorescent dye hybrid protein ligand monomer oligomer protein tyrosine kinase unclassified drug yellow fluorescent protein animal cell article biotechnology cell line cell strain A431 CHO cell confocal laser microscopy controlled study dimerization endocytosis endosome filopodium flow cytometry fluorescence human human cell internalization ligand binding nonhuman priority journal quantitative analysis quantum mechanics signal transduction Animals Cell Membrane Cricetinae Endosomes Epidermal Growth Factor Humans Motion Oncogene Proteins v-erbB Protein Binding Protein Interaction Mapping Protein Transport Quantum Dots Receptors, Cell Surface Signal Transduction Spectrometry, Fluorescence Animalia |
| spellingShingle |
Cells Enzymes Semiconductor quantum dots Epidermal growth factors (EGF) Biotechnology citrine epidermal growth factor epidermal growth factor receptor epidermal growth factor receptor 2 epidermal growth factor receptor 3 fluorescent dye hybrid protein ligand monomer oligomer protein tyrosine kinase unclassified drug yellow fluorescent protein animal cell article biotechnology cell line cell strain A431 CHO cell confocal laser microscopy controlled study dimerization endocytosis endosome filopodium flow cytometry fluorescence human human cell internalization ligand binding nonhuman priority journal quantitative analysis quantum mechanics signal transduction Animals Cell Membrane Cricetinae Endosomes Epidermal Growth Factor Humans Motion Oncogene Proteins v-erbB Protein Binding Protein Interaction Mapping Protein Transport Quantum Dots Receptors, Cell Surface Signal Transduction Spectrometry, Fluorescence Animalia Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| topic_facet |
Cells Enzymes Semiconductor quantum dots Epidermal growth factors (EGF) Biotechnology citrine epidermal growth factor epidermal growth factor receptor epidermal growth factor receptor 2 epidermal growth factor receptor 3 fluorescent dye hybrid protein ligand monomer oligomer protein tyrosine kinase unclassified drug yellow fluorescent protein animal cell article biotechnology cell line cell strain A431 CHO cell confocal laser microscopy controlled study dimerization endocytosis endosome filopodium flow cytometry fluorescence human human cell internalization ligand binding nonhuman priority journal quantitative analysis quantum mechanics signal transduction Animals Cell Membrane Cricetinae Endosomes Epidermal Growth Factor Humans Motion Oncogene Proteins v-erbB Protein Binding Protein Interaction Mapping Protein Transport Quantum Dots Receptors, Cell Surface Signal Transduction Spectrometry, Fluorescence Animalia |
| description |
The erbB/HER family of transmembrane receptor tyrosine kinases (RTKs) mediate cellular responses to epidermal growth factor (EGF) and related ligands. We have imaged the early stages of RTK-dependent signaling in living cells using: (i) stable expression of erbB1/2/3 fused with visible fluorescent proteins (VFPs), (ii) fluorescent quantum dots (QDs) bearing epidermal growth factor (EGF-QD) and (iii) continuous confocal laser scanning microscopy and flow cytometry. Here we demonstrate that EGF-QDs are highly specific and potent in the binding and activation of the EGF receptor (erbB1), being rapidly internalized into endosomes that exhibit active trafficking and extensive fusion. EGF-QDs bound to erbB1 expressed on filopodia revealed a previously unreported mechanism of retrograde transport to the cell body. When erbB2-monomeric yellow fluorescent protein (mYFP) or erbB3-monomeric Citrine (mCitrine) were coexpressed with erbB1, the rates and extent of endocytosis of EGF-QD and the RTK-VFP demonstrated that erbB2 but not erbB3 heterodimerizes with erbB1 after EGF stimulation, thereby modulating EGF-induced signaling. QD-ligands will find widespread use in basic research and biotechnological developments. |
| title |
Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| title_short |
Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| title_full |
Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| title_fullStr |
Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| title_full_unstemmed |
Quantum dot ligands provide new insights into erbB/HER receptor-mediated signal transduction |
| title_sort |
quantum dot ligands provide new insights into erbb/her receptor-mediated signal transduction |
| publishDate |
2004 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_10870156_v22_n2_p198_Lidke http://hdl.handle.net/20.500.12110/paper_10870156_v22_n2_p198_Lidke |
| _version_ |
1768544924874047488 |