Neratinib induces ErbB2 ubiquitylation and endocytic degradation via HSP90 dissociation in breast cancer cells
Paper Highlights • Tyrosine kinase inhibitors lapatinib and neratinib show opposite effects on ErbB2 levels • Both lapatinib and neratinib treatment elevates ErbB2 mRNA • Neratinib induces more potent endocytic degradation via endolysosome system than lapatinib • Neratinib triggers ErbB2 ubiquitylat...
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| Veröffentlicht in: | Cancer letters 2016-11, Vol.382 (2), p.176-185 |
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| container_end_page | 185 |
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| container_issue | 2 |
| container_start_page | 176 |
| container_title | Cancer letters |
| container_volume | 382 |
| creator | Zhang, Yingqiu Zhang, Jinrui Liu, Congcong Du, Sha Feng, Lu Luan, Xuelin Zhang, Yayun Shi, Yulin Wang, Taishu Wu, Yue Cheng, Wei Meng, Songshu Li, Man Liu, Han |
| description | Paper Highlights • Tyrosine kinase inhibitors lapatinib and neratinib show opposite effects on ErbB2 levels • Both lapatinib and neratinib treatment elevates ErbB2 mRNA • Neratinib induces more potent endocytic degradation via endolysosome system than lapatinib • Neratinib triggers ErbB2 ubiquitylation through HSP90 dissociation |
| doi_str_mv | 10.1016/j.canlet.2016.08.026 |
| format | Article |
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All rights reserved.</rights><rights>Copyright Elsevier Limited Nov 28, 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-d7b7878db620a16cd239f954169289841ac35f0419e5dda8574e4c8de8ca81a83</citedby><cites>FETCH-LOGICAL-c478t-d7b7878db620a16cd239f954169289841ac35f0419e5dda8574e4c8de8ca81a83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.canlet.2016.08.026$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27597738$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Yingqiu</creatorcontrib><creatorcontrib>Zhang, Jinrui</creatorcontrib><creatorcontrib>Liu, Congcong</creatorcontrib><creatorcontrib>Du, Sha</creatorcontrib><creatorcontrib>Feng, Lu</creatorcontrib><creatorcontrib>Luan, Xuelin</creatorcontrib><creatorcontrib>Zhang, Yayun</creatorcontrib><creatorcontrib>Shi, Yulin</creatorcontrib><creatorcontrib>Wang, Taishu</creatorcontrib><creatorcontrib>Wu, Yue</creatorcontrib><creatorcontrib>Cheng, Wei</creatorcontrib><creatorcontrib>Meng, Songshu</creatorcontrib><creatorcontrib>Li, Man</creatorcontrib><creatorcontrib>Liu, Han</creatorcontrib><title>Neratinib induces ErbB2 ubiquitylation and endocytic degradation via HSP90 dissociation in breast cancer cells</title><title>Cancer letters</title><addtitle>Cancer Lett</addtitle><description>Paper Highlights • Tyrosine kinase inhibitors lapatinib and neratinib show opposite effects on ErbB2 levels • Both lapatinib and neratinib treatment elevates ErbB2 mRNA • Neratinib induces more potent endocytic degradation via endolysosome system than lapatinib • Neratinib triggers ErbB2 ubiquitylation through HSP90 dissociation</description><subject>Antineoplastic Agents - pharmacology</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - drug therapy</subject><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - metabolism</subject><subject>Breast Neoplasms - pathology</subject><subject>Cell cycle</subject><subject>Cell Line, Tumor</subject><subject>Conflicts of interest</subject><subject>Endocytosis</subject><subject>Endocytosis - drug effects</subject><subject>ErbB2</subject><subject>Experiments</subject><subject>Female</subject><subject>Hematology, Oncology and Palliative Medicine</subject><subject>HER2</subject><subject>HSP90 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunoglobulins</subject><subject>Kinases</subject><subject>Lysosomes - drug effects</subject><subject>Lysosomes - metabolism</subject><subject>Microscopy</subject><subject>Mutation</subject><subject>Neratinib</subject><subject>Phosphatase</subject><subject>Protein Binding</subject><subject>Protein Kinase Inhibitors - pharmacology</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Quinolines - pharmacology</subject><subject>Receptor, ErbB-2 - antagonists & inhibitors</subject><subject>Receptor, ErbB-2 - genetics</subject><subject>Receptor, ErbB-2 - metabolism</subject><subject>Signal transduction</subject><subject>Time Factors</subject><subject>Transfection</subject><subject>Ubiquitination - drug effects</subject><subject>Ubiquitylation</subject><issn>0304-3835</issn><issn>1872-7980</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkl1rFTEQhoMo9lj9ByIBb7zZYz43szeCLdUKRYXqdcgmcyTHPdk22S2cf2-WrQq90auQzDNvZuYdQl5ytuWMt2_3W-_SgNNW1NuWwZaJ9hHZcDCiMR2wx2TDJFONBKlPyLNS9owxrYx-Sk6E0Z0xEjYkfcbspphiT2MKs8dCL3J_Jujcx9s5TsehRsdEXQoUUxj9cYqeBvyRXVgjd9HRy-uvHaMhljL6uD7HRPuMrky0lukxU4_DUJ6TJzs3FHxxf56S7x8uvp1fNldfPn46f3_VeGVgaoLpDRgIfSuY460PQna7TivedgI6UNx5qXdM8Q51CA60Uag8BATvgDuQp-TNqnuTx9sZy2QPsSwVuITjXCwHaaRg0On_QbXUoERX0dcP0P0451QbWSguOQDjlVIr5fNYSsadvcnx4PLRcmYX6-zertbZxTrLwFbratqre_G5P2D4k_Tbqwq8WwGsg7uLmG3xEetsQ8zoJxvG-K8fHgr4oTrv3fATj1j-9mKLsMxeL-uzbA9vJdOcM_kLRCy_6A</recordid><startdate>20161128</startdate><enddate>20161128</enddate><creator>Zhang, Yingqiu</creator><creator>Zhang, Jinrui</creator><creator>Liu, Congcong</creator><creator>Du, Sha</creator><creator>Feng, Lu</creator><creator>Luan, Xuelin</creator><creator>Zhang, Yayun</creator><creator>Shi, Yulin</creator><creator>Wang, Taishu</creator><creator>Wu, Yue</creator><creator>Cheng, Wei</creator><creator>Meng, Songshu</creator><creator>Li, Man</creator><creator>Liu, Han</creator><general>Elsevier Ireland Ltd</general><general>Elsevier Limited</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TO</scope><scope>7U9</scope><scope>H94</scope><scope>K9.</scope><scope>NAPCQ</scope><scope>7X8</scope></search><sort><creationdate>20161128</creationdate><title>Neratinib induces ErbB2 ubiquitylation and endocytic degradation via HSP90 dissociation in breast cancer cells</title><author>Zhang, Yingqiu ; Zhang, Jinrui ; Liu, Congcong ; Du, Sha ; Feng, Lu ; Luan, Xuelin ; Zhang, Yayun ; Shi, Yulin ; Wang, Taishu ; Wu, Yue ; Cheng, Wei ; Meng, Songshu ; Li, Man ; Liu, Han</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-d7b7878db620a16cd239f954169289841ac35f0419e5dda8574e4c8de8ca81a83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Antineoplastic Agents - pharmacology</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - drug therapy</topic><topic>Breast Neoplasms - genetics</topic><topic>Breast Neoplasms - metabolism</topic><topic>Breast Neoplasms - pathology</topic><topic>Cell cycle</topic><topic>Cell Line, Tumor</topic><topic>Conflicts of interest</topic><topic>Endocytosis</topic><topic>Endocytosis - drug effects</topic><topic>ErbB2</topic><topic>Experiments</topic><topic>Female</topic><topic>Hematology, Oncology and Palliative Medicine</topic><topic>HER2</topic><topic>HSP90 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Immunoglobulins</topic><topic>Kinases</topic><topic>Lysosomes - drug effects</topic><topic>Lysosomes - metabolism</topic><topic>Microscopy</topic><topic>Mutation</topic><topic>Neratinib</topic><topic>Phosphatase</topic><topic>Protein Binding</topic><topic>Protein Kinase Inhibitors - pharmacology</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Quinolines - pharmacology</topic><topic>Receptor, ErbB-2 - 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| fulltext | fulltext |
| identifier | ISSN: 0304-3835 |
| ispartof | Cancer letters, 2016-11, Vol.382 (2), p.176-185 |
| issn | 0304-3835 1872-7980 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Antineoplastic Agents - pharmacology Breast cancer Breast Neoplasms - drug therapy Breast Neoplasms - genetics Breast Neoplasms - metabolism Breast Neoplasms - pathology Cell cycle Cell Line, Tumor Conflicts of interest Endocytosis Endocytosis - drug effects ErbB2 Experiments Female Hematology, Oncology and Palliative Medicine HER2 HSP90 Heat-Shock Proteins - metabolism Humans Immunoglobulins Kinases Lysosomes - drug effects Lysosomes - metabolism Microscopy Mutation Neratinib Phosphatase Protein Binding Protein Kinase Inhibitors - pharmacology Proteins Proteolysis Quinolines - pharmacology Receptor, ErbB-2 - antagonists & inhibitors Receptor, ErbB-2 - genetics Receptor, ErbB-2 - metabolism Signal transduction Time Factors Transfection Ubiquitination - drug effects Ubiquitylation |
| title | Neratinib induces ErbB2 ubiquitylation and endocytic degradation via HSP90 dissociation in breast cancer cells |
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