Intravesicular epidermal growth factor receptor subject to retrograde trafficking drives epidermal growth factor-dependent migration
The Epidermal Growth Factor Receptor (EGFR) is frequently mutated and overexpressed in metastatic cancer. Although EGFR is a transmembrane tyrosine kinase localized to the basolateral membrane in normal epithelium, it is frequently found intracellularly localized in transformed cells. We have previo...
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| Published in | Oncotarget Vol. 9; no. 5; pp. 6463 - 6477 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
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19.01.2018
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| ISSN | 1949-2553 1949-2553 |
| DOI | 10.18632/oncotarget.23766 |
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| Abstract | The Epidermal Growth Factor Receptor (EGFR) is frequently mutated and overexpressed in metastatic cancer. Although EGFR is a transmembrane tyrosine kinase localized to the basolateral membrane in normal epithelium, it is frequently found intracellularly localized in transformed cells. We have previously demonstrated the epithelial adaptor protein mucin 1 (MUC1) alters trafficking of EGFR, inhibiting its degradation and promoting its translocation to the nucleus, where it can directly modulate gene transcription. Here, we demonstrate that MUC1 promotes the retention of EGF-bound EGFR in Early Endosome Antigen1 (EEA1)-positive vesicles while preventing its trafficking to the lysosome. These events result in the accumulation of endosomal vesicles harboring active receptor throughout the cell and a reorganization of the actin cytoskeleton. EGF-dependent cell migration and filopodia formation is reliant upon this altered trafficking, and can be prevented by blocking retrograde trafficking. Together, these results indicate that intracellular EGFR may play an essential role in cancer metastasis and a potential mechanism for the failure of therapeutic antibodies in EGFR-driven metastatic breast cancer. |
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| AbstractList | The Epidermal Growth Factor Receptor (EGFR) is frequently mutated and overexpressed in metastatic cancer. Although EGFR is a transmembrane tyrosine kinase localized to the basolateral membrane in normal epithelium, it is frequently found intracellularly localized in transformed cells. We have previously demonstrated the epithelial adaptor protein mucin 1 (MUC1) alters trafficking of EGFR, inhibiting its degradation and promoting its translocation to the nucleus, where it can directly modulate gene transcription. Here, we demonstrate that MUC1 promotes the retention of EGF-bound EGFR in Early Endosome Antigen1 (EEA1)-positive vesicles while preventing its trafficking to the lysosome. These events result in the accumulation of endosomal vesicles harboring active receptor throughout the cell and a reorganization of the actin cytoskeleton. EGF-dependent cell migration and filopodia formation is reliant upon this altered trafficking, and can be prevented by blocking retrograde trafficking. Together, these results indicate that intracellular EGFR may play an essential role in cancer metastasis and a potential mechanism for the failure of therapeutic antibodies in EGFR-driven metastatic breast cancer. The Epidermal Growth Factor Receptor (EGFR) is frequently mutated and overexpressed in metastatic cancer. Although EGFR is a transmembrane tyrosine kinase localized to the basolateral membrane in normal epithelium, it is frequently found intracellularly localized in transformed cells. We have previously demonstrated the epithelial adaptor protein mucin 1 (MUC1) alters trafficking of EGFR, inhibiting its degradation and promoting its translocation to the nucleus, where it can directly modulate gene transcription. Here, we demonstrate that MUC1 promotes the retention of EGF-bound EGFR in Early Endosome Antigen1 (EEA1)-positive vesicles while preventing its trafficking to the lysosome. These events result in the accumulation of endosomal vesicles harboring active receptor throughout the cell and a reorganization of the actin cytoskeleton. EGF-dependent cell migration and filopodia formation is reliant upon this altered trafficking, and can be prevented by blocking retrograde trafficking. Together, these results indicate that intracellular EGFR may play an essential role in cancer metastasis and a potential mechanism for the failure of therapeutic antibodies in EGFR-driven metastatic breast cancer.The Epidermal Growth Factor Receptor (EGFR) is frequently mutated and overexpressed in metastatic cancer. Although EGFR is a transmembrane tyrosine kinase localized to the basolateral membrane in normal epithelium, it is frequently found intracellularly localized in transformed cells. We have previously demonstrated the epithelial adaptor protein mucin 1 (MUC1) alters trafficking of EGFR, inhibiting its degradation and promoting its translocation to the nucleus, where it can directly modulate gene transcription. Here, we demonstrate that MUC1 promotes the retention of EGF-bound EGFR in Early Endosome Antigen1 (EEA1)-positive vesicles while preventing its trafficking to the lysosome. These events result in the accumulation of endosomal vesicles harboring active receptor throughout the cell and a reorganization of the actin cytoskeleton. EGF-dependent cell migration and filopodia formation is reliant upon this altered trafficking, and can be prevented by blocking retrograde trafficking. Together, these results indicate that intracellular EGFR may play an essential role in cancer metastasis and a potential mechanism for the failure of therapeutic antibodies in EGFR-driven metastatic breast cancer. |
| Author | Maisel, Sabrina Schroeder, Joyce Broka, Derrick |
| Author_xml | – sequence: 1 givenname: Sabrina surname: Maisel fullname: Maisel, Sabrina organization: Cancer Biology Graduate Interdisciplinary Program, University of Arizona, Tucson, AZ, USA, Arizona Cancer Center, University of Arizona, Tucson, AZ, USA – sequence: 2 givenname: Derrick surname: Broka fullname: Broka, Derrick organization: Arizona Cancer Center, University of Arizona, Tucson, AZ, USA – sequence: 3 givenname: Joyce surname: Schroeder fullname: Schroeder, Joyce organization: Cancer Biology Graduate Interdisciplinary Program, University of Arizona, Tucson, AZ, USA, Arizona Cancer Center, University of Arizona, Tucson, AZ, USA, Department of Molecular and Cellular Biology, University of Arizona, Tucson, AZ, USA, BIO5 Institute, University of Arizona, Tucson, AZ, USA |
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| CitedBy_id | crossref_primary_10_1016_j_carres_2018_10_004 crossref_primary_10_3390_jnt2030011 crossref_primary_10_1016_j_phrs_2022_106606 crossref_primary_10_37349_etat_2023_00156 crossref_primary_10_1186_s12967_019_1939_7 crossref_primary_10_1111_tra_12931 crossref_primary_10_1038_s41467_025_57162_5 crossref_primary_10_1038_s41417_022_00541_7 |
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| Keywords | migration cetuximab MUC1 retrograde trafficking epidermal growth factor receptor |
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