Identification of nucleolin as new ErbB receptors- interacting protein
The ErbB receptor tyrosine kinases are major contributors to malignant transformation. These receptors are frequently overexpressed in a variety of human carcinomas. The role of the ErbB receptors and their ligands in carcinomas and the mechanism by which their overexpression leads to cancer develop...
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| Veröffentlicht in: | PloS one 2008-06, Vol.3 (6), p.e2310-e2310 |
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| creator | Di Segni, Ayelet Farin, Keren Pinkas-Kramarski, Ronit |
| description | The ErbB receptor tyrosine kinases are major contributors to malignant transformation. These receptors are frequently overexpressed in a variety of human carcinomas. The role of the ErbB receptors and their ligands in carcinomas and the mechanism by which their overexpression leads to cancer development is still unclear. Ligand binding to specific ErbB receptor is followed by receptor dimerization, phosphorylation and recruitment of SH2 containing cytoplasmic proteins, which initiate the cascade of signaling events. Nevertheless, increasing data suggest that there are non-phosphorylated receptor-substrate interactions that may affect ErbB-mediated responses.
In the present study, using GST-ErbB4 fusion protein pull down assay and mass spectroscopic analysis, we have found the ErbB receptors interact with nucleolin via their cytoplasmic tail. Nucleolin is a ubiquitous, nonhistone, nucleolar, multifunctional phosphoprotein that is also overexpressed in cancer cells. Our results demonstrate that overexpression of ErbB1 and nucleolin may lead to receptor dimerization, phosphorylation and to anchorage independent growth.
The oncogenic potential of ErbB depends on receptor levels and activation. Our results suggest that nucleolin may affect ErbB dimerization and activation leading to enhanced cell growth. |
| doi_str_mv | 10.1371/journal.pone.0002310 |
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In the present study, using GST-ErbB4 fusion protein pull down assay and mass spectroscopic analysis, we have found the ErbB receptors interact with nucleolin via their cytoplasmic tail. Nucleolin is a ubiquitous, nonhistone, nucleolar, multifunctional phosphoprotein that is also overexpressed in cancer cells. Our results demonstrate that overexpression of ErbB1 and nucleolin may lead to receptor dimerization, phosphorylation and to anchorage independent growth.
The oncogenic potential of ErbB depends on receptor levels and activation. Our results suggest that nucleolin may affect ErbB dimerization and activation leading to enhanced cell growth.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0002310</identifier><identifier>PMID: 18523588</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Activation ; Analysis ; Animals ; Base Sequence ; Cancer ; Carcinoma ; Cell activation ; Cell Biology/Cell Signaling ; Cell Division ; Cell Line ; Dimerization ; DNA Primers ; Epidermal growth factor ; ErbB protein ; ErbB-1 protein ; ErbB-2 protein ; Fusion protein ; Gene expression ; Humans ; Kinases ; Ligands ; Neurobiology ; Neurosciences ; Nucleoli ; Nucleolin ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphotransferases ; Prostate cancer ; Protein Binding ; Proteins ; Rats ; Receptor Protein-Tyrosine Kinases - chemistry ; Receptor Protein-Tyrosine Kinases - metabolism ; Receptors ; Recruitment ; RNA polymerase ; RNA-Binding Proteins - metabolism ; Rodents ; Signal Transduction ; Spectroscopic analysis ; Transcription factors ; Transformation ; Tyrosine</subject><ispartof>PloS one, 2008-06, Vol.3 (6), p.e2310-e2310</ispartof><rights>COPYRIGHT 2008 Public Library of Science</rights><rights>2008 Di Segni et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Di Segni et al. 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c759t-6cd319e058e6b879b439d0927c7a115a264778c787fbd3703256850530d44b763</citedby><cites>FETCH-LOGICAL-c759t-6cd319e058e6b879b439d0927c7a115a264778c787fbd3703256850530d44b763</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2390759/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2390759/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793,79600,79601</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18523588$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Koch, Karl-Wilhelm</contributor><creatorcontrib>Di Segni, Ayelet</creatorcontrib><creatorcontrib>Farin, Keren</creatorcontrib><creatorcontrib>Pinkas-Kramarski, Ronit</creatorcontrib><title>Identification of nucleolin as new ErbB receptors- interacting protein</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The ErbB receptor tyrosine kinases are major contributors to malignant transformation. These receptors are frequently overexpressed in a variety of human carcinomas. The role of the ErbB receptors and their ligands in carcinomas and the mechanism by which their overexpression leads to cancer development is still unclear. Ligand binding to specific ErbB receptor is followed by receptor dimerization, phosphorylation and recruitment of SH2 containing cytoplasmic proteins, which initiate the cascade of signaling events. Nevertheless, increasing data suggest that there are non-phosphorylated receptor-substrate interactions that may affect ErbB-mediated responses.
In the present study, using GST-ErbB4 fusion protein pull down assay and mass spectroscopic analysis, we have found the ErbB receptors interact with nucleolin via their cytoplasmic tail. Nucleolin is a ubiquitous, nonhistone, nucleolar, multifunctional phosphoprotein that is also overexpressed in cancer cells. Our results demonstrate that overexpression of ErbB1 and nucleolin may lead to receptor dimerization, phosphorylation and to anchorage independent growth.
The oncogenic potential of ErbB depends on receptor levels and activation. Our results suggest that nucleolin may affect ErbB dimerization and activation leading to enhanced cell growth.</description><subject>Activation</subject><subject>Analysis</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cancer</subject><subject>Carcinoma</subject><subject>Cell activation</subject><subject>Cell Biology/Cell Signaling</subject><subject>Cell Division</subject><subject>Cell Line</subject><subject>Dimerization</subject><subject>DNA Primers</subject><subject>Epidermal growth factor</subject><subject>ErbB protein</subject><subject>ErbB-1 protein</subject><subject>ErbB-2 protein</subject><subject>Fusion protein</subject><subject>Gene expression</subject><subject>Humans</subject><subject>Kinases</subject><subject>Ligands</subject><subject>Neurobiology</subject><subject>Neurosciences</subject><subject>Nucleoli</subject><subject>Nucleolin</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphotransferases</subject><subject>Prostate cancer</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Rats</subject><subject>Receptor Protein-Tyrosine Kinases - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Di Segni, Ayelet</au><au>Farin, Keren</au><au>Pinkas-Kramarski, Ronit</au><au>Koch, Karl-Wilhelm</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of nucleolin as new ErbB receptors- interacting protein</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2008-06-04</date><risdate>2008</risdate><volume>3</volume><issue>6</issue><spage>e2310</spage><epage>e2310</epage><pages>e2310-e2310</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The ErbB receptor tyrosine kinases are major contributors to malignant transformation. These receptors are frequently overexpressed in a variety of human carcinomas. The role of the ErbB receptors and their ligands in carcinomas and the mechanism by which their overexpression leads to cancer development is still unclear. Ligand binding to specific ErbB receptor is followed by receptor dimerization, phosphorylation and recruitment of SH2 containing cytoplasmic proteins, which initiate the cascade of signaling events. Nevertheless, increasing data suggest that there are non-phosphorylated receptor-substrate interactions that may affect ErbB-mediated responses.
In the present study, using GST-ErbB4 fusion protein pull down assay and mass spectroscopic analysis, we have found the ErbB receptors interact with nucleolin via their cytoplasmic tail. Nucleolin is a ubiquitous, nonhistone, nucleolar, multifunctional phosphoprotein that is also overexpressed in cancer cells. Our results demonstrate that overexpression of ErbB1 and nucleolin may lead to receptor dimerization, phosphorylation and to anchorage independent growth.
The oncogenic potential of ErbB depends on receptor levels and activation. Our results suggest that nucleolin may affect ErbB dimerization and activation leading to enhanced cell growth.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>18523588</pmid><doi>10.1371/journal.pone.0002310</doi><tpages>e2310</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Activation Analysis Animals Base Sequence Cancer Carcinoma Cell activation Cell Biology/Cell Signaling Cell Division Cell Line Dimerization DNA Primers Epidermal growth factor ErbB protein ErbB-1 protein ErbB-2 protein Fusion protein Gene expression Humans Kinases Ligands Neurobiology Neurosciences Nucleoli Nucleolin Phosphoproteins - metabolism Phosphorylation Phosphotransferases Prostate cancer Protein Binding Proteins Rats Receptor Protein-Tyrosine Kinases - chemistry Receptor Protein-Tyrosine Kinases - metabolism Receptors Recruitment RNA polymerase RNA-Binding Proteins - metabolism Rodents Signal Transduction Spectroscopic analysis Transcription factors Transformation Tyrosine |
| title | Identification of nucleolin as new ErbB receptors- interacting protein |
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