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spelling paper:paper_19326203_v12_n3_p_Toscani2023-06-08T16:30:39Z Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models Simian, Marina beta1 integrin epidermal growth factor receptor 2 CD18 antigen epidermal growth factor receptor 2 ERBB2 protein, human Article breast cancer cell line cell adhesion cell compartmentalization cell membrane confocal microscopy enzyme localization extracellular matrix HeLa cell line human human cell immunofluorescence MCF-7 cell line molecular imaging protein analysis protein expression protein function protein interaction protein localization protein structure sequence analysis SKBR3 cell line T47D cell line Western blotting breast tumor metabolism pathology tumor cell line Breast Neoplasms CD18 Antigens Cell Line, Tumor Humans Receptor, ErbB-2 ERBB2 is a member of the ERBB family of tyrosine kinase receptors that plays a major role in breast cancer progression. Located at the plasma membrane, ERBB2 forms large clusters in spite of the presence of growth factors. Beta1 integrin, membrane receptor of extracellular matrix proteins, regulates adhesion, migration and invasiveness of breast cancer cells. Physical interaction between beta1 integrin and ERBB2 has been suggested although published data are contradictory. The aim of the present work was to study the interaction between ERBB2 and beta1 integrin in different scenarios of expression and activation. We determined that beta1 integrin and ERBB2 colocalization is dependent on the expression level of both receptors exclusively in adherent cells. In suspension cells, lack of focal adhesions leave integrins free to diffuse on the plasma membrane and interact with ERBB2 even at low expression levels of both receptors. In adherent cells, high expression of beta1 integrin leaves unbound receptors outside focal complexes that diffuse within the plasma membrane and interact with ERBB2 membrane domains. Superresolution imaging showed the existence of two distinct populations of ERBB2: a major population located in large clusters and a minor population outside these structures. Upon ERBB2 overexpression, receptors outside large clusters can freely diffuse at the membrane and interact with integrins. These results reveal how expression levels of beta1 integrin and ERBB2 determine their frequency of colocalization and show that extracellular matrix proteins shape membrane clusters distribution, regulating ERBB2 and beta1 integrin activity in breast cancer cells. © 2017 Toscani et al.This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Fil:Simian, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v12_n3_p_Toscani http://hdl.handle.net/20.500.12110/paper_19326203_v12_n3_p_Toscani
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic beta1 integrin
epidermal growth factor receptor 2
CD18 antigen
epidermal growth factor receptor 2
ERBB2 protein, human
Article
breast cancer cell line
cell adhesion
cell compartmentalization
cell membrane
confocal microscopy
enzyme localization
extracellular matrix
HeLa cell line
human
human cell
immunofluorescence
MCF-7 cell line
molecular imaging
protein analysis
protein expression
protein function
protein interaction
protein localization
protein structure
sequence analysis
SKBR3 cell line
T47D cell line
Western blotting
breast tumor
metabolism
pathology
tumor cell line
Breast Neoplasms
CD18 Antigens
Cell Line, Tumor
Humans
Receptor, ErbB-2
spellingShingle beta1 integrin
epidermal growth factor receptor 2
CD18 antigen
epidermal growth factor receptor 2
ERBB2 protein, human
Article
breast cancer cell line
cell adhesion
cell compartmentalization
cell membrane
confocal microscopy
enzyme localization
extracellular matrix
HeLa cell line
human
human cell
immunofluorescence
MCF-7 cell line
molecular imaging
protein analysis
protein expression
protein function
protein interaction
protein localization
protein structure
sequence analysis
SKBR3 cell line
T47D cell line
Western blotting
breast tumor
metabolism
pathology
tumor cell line
Breast Neoplasms
CD18 Antigens
Cell Line, Tumor
Humans
Receptor, ErbB-2
Simian, Marina
Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
topic_facet beta1 integrin
epidermal growth factor receptor 2
CD18 antigen
epidermal growth factor receptor 2
ERBB2 protein, human
Article
breast cancer cell line
cell adhesion
cell compartmentalization
cell membrane
confocal microscopy
enzyme localization
extracellular matrix
HeLa cell line
human
human cell
immunofluorescence
MCF-7 cell line
molecular imaging
protein analysis
protein expression
protein function
protein interaction
protein localization
protein structure
sequence analysis
SKBR3 cell line
T47D cell line
Western blotting
breast tumor
metabolism
pathology
tumor cell line
Breast Neoplasms
CD18 Antigens
Cell Line, Tumor
Humans
Receptor, ErbB-2
description ERBB2 is a member of the ERBB family of tyrosine kinase receptors that plays a major role in breast cancer progression. Located at the plasma membrane, ERBB2 forms large clusters in spite of the presence of growth factors. Beta1 integrin, membrane receptor of extracellular matrix proteins, regulates adhesion, migration and invasiveness of breast cancer cells. Physical interaction between beta1 integrin and ERBB2 has been suggested although published data are contradictory. The aim of the present work was to study the interaction between ERBB2 and beta1 integrin in different scenarios of expression and activation. We determined that beta1 integrin and ERBB2 colocalization is dependent on the expression level of both receptors exclusively in adherent cells. In suspension cells, lack of focal adhesions leave integrins free to diffuse on the plasma membrane and interact with ERBB2 even at low expression levels of both receptors. In adherent cells, high expression of beta1 integrin leaves unbound receptors outside focal complexes that diffuse within the plasma membrane and interact with ERBB2 membrane domains. Superresolution imaging showed the existence of two distinct populations of ERBB2: a major population located in large clusters and a minor population outside these structures. Upon ERBB2 overexpression, receptors outside large clusters can freely diffuse at the membrane and interact with integrins. These results reveal how expression levels of beta1 integrin and ERBB2 determine their frequency of colocalization and show that extracellular matrix proteins shape membrane clusters distribution, regulating ERBB2 and beta1 integrin activity in breast cancer cells. © 2017 Toscani et al.This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
author Simian, Marina
author_facet Simian, Marina
author_sort Simian, Marina
title Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
title_short Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
title_full Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
title_fullStr Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
title_full_unstemmed Distinct ErbB2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
title_sort distinct erbb2 receptor populations differentially interact with beta1 integrin in breast cancer cell models
publishDate 2017
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_19326203_v12_n3_p_Toscani
http://hdl.handle.net/20.500.12110/paper_19326203_v12_n3_p_Toscani
work_keys_str_mv AT simianmarina distincterbb2receptorpopulationsdifferentiallyinteractwithbeta1integrininbreastcancercellmodels
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