Distinct FAK-Src activation events promote α5β1 and α4β1 integrin-stimulated neuroblastoma cell motility
Signals from fibronectin-binding integrins promote neural crest cell motility during development in part through protein-tyrosine kinase (PTK) activation. Neuroblastoma (NB) is a neural crest malignancy with high metastatic potential. We find that α4 and α5 integrins are present in late-stage NB tum...
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| Veröffentlicht in: | Oncogene 2008-02, Vol.27 (10), p.1439-1448 |
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| creator | Wu, L Bernard-Trifilo, J A Lim, Y Lim, S-T Mitra, S K Uryu, S Chen, M Pallen, C J Cheung, N-Kv Mikolon, D Mielgo, A Stupack, D G Schlaepfer, D D |
| description | Signals from fibronectin-binding integrins promote neural crest cell motility during development in part through protein-tyrosine kinase (PTK) activation. Neuroblastoma (NB) is a neural crest malignancy with high metastatic potential. We find that α4 and α5 integrins are present in late-stage NB tumors and cell lines derived thereof. To determine the signaling connections promoting either α4β1- or α5β1-initiated NB cell motility, pharmacological, dominant negative and short-hairpin RNA (shRNA) inhibitory approaches were undertaken. shRNA knockdown revealed that α5β1-stimulated NB motility is dependent upon focal adhesion kinase (FAK) PTK, Src PTK and p130Cas adapter protein expression. Cell reconstitution showed that FAK catalytic activity is required for α5β1-stimulated Src activation in part through direct FAK phosphorylation of Src at Tyr-418. Alternatively, α4β1-stimulated NB cell motility is dependent upon Src and p130Cas but FAK is not essential. Catalytically inactive receptor protein-tyrosine phosphatase-α overexpression inhibited α4β1-stimulated NB motility and Src activation consistent with α4-regulated Src activity occurring through Src Tyr-529 dephosphorylation. In α4 shRNA-expressing NB cells, α4β1-stimulated Src activation and NB cell motility were rescued by wild type but not cytoplasmic domain-truncated α4 re-expression. These studies, supported by results using reconstituted fibroblasts, reveal that α4β1-mediated Src activation is mechanistically distinct from FAK-mediated Src activation during α5β1-mediated NB migration and support the evaluation of inhibitors to α4, Src and FAK in the control of NB tumor progression. |
| doi_str_mv | 10.1038/sj.onc.1210770 |
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Neuroblastoma (NB) is a neural crest malignancy with high metastatic potential. We find that α4 and α5 integrins are present in late-stage NB tumors and cell lines derived thereof. To determine the signaling connections promoting either α4β1- or α5β1-initiated NB cell motility, pharmacological, dominant negative and short-hairpin RNA (shRNA) inhibitory approaches were undertaken. shRNA knockdown revealed that α5β1-stimulated NB motility is dependent upon focal adhesion kinase (FAK) PTK, Src PTK and p130Cas adapter protein expression. Cell reconstitution showed that FAK catalytic activity is required for α5β1-stimulated Src activation in part through direct FAK phosphorylation of Src at Tyr-418. Alternatively, α4β1-stimulated NB cell motility is dependent upon Src and p130Cas but FAK is not essential. Catalytically inactive receptor protein-tyrosine phosphatase-α overexpression inhibited α4β1-stimulated NB motility and Src activation consistent with α4-regulated Src activity occurring through Src Tyr-529 dephosphorylation. In α4 shRNA-expressing NB cells, α4β1-stimulated Src activation and NB cell motility were rescued by wild type but not cytoplasmic domain-truncated α4 re-expression. These studies, supported by results using reconstituted fibroblasts, reveal that α4β1-mediated Src activation is mechanistically distinct from FAK-mediated Src activation during α5β1-mediated NB migration and support the evaluation of inhibitors to α4, Src and FAK in the control of NB tumor progression.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1210770</identifier><identifier>PMID: 17828307</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Adapter proteins ; Apoptosis ; Biological and medical sciences ; Cell activation ; Cell Biology ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cellular signal transduction ; Dephosphorylation ; Fibroblasts ; Fibronectin ; Focal adhesion kinase ; Fundamental and applied biological sciences. Psychology ; Genetic aspects ; Human Genetics ; Integrins ; Internal Medicine ; Malignancy ; Medical sciences ; Medicine ; Medicine & Public Health ; Metastases ; Molecular and cellular biology ; Motility ; Neural crest ; Neuroblastoma ; Neurology ; Oncology ; original-article ; Phosphorylation ; Physiological aspects ; Protein-tyrosine kinase ; Protein-tyrosine-phosphatase ; Risk factors ; Src protein ; Tumors ; Tumors of the nervous system. Phacomatoses</subject><ispartof>Oncogene, 2008-02, Vol.27 (10), p.1439-1448</ispartof><rights>Springer Nature Limited 2008</rights><rights>2008 INIST-CNRS</rights><rights>COPYRIGHT 2008 Nature Publishing Group</rights><rights>Nature Publishing Group 2008.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5020-bf7c0932c5456bd0cd9778be9b0f3f32b04771f631d2c1535b271adae9a243d73</citedby><cites>FETCH-LOGICAL-c5020-bf7c0932c5456bd0cd9778be9b0f3f32b04771f631d2c1535b271adae9a243d73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,2727,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20178584$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Wu, L</creatorcontrib><creatorcontrib>Bernard-Trifilo, J A</creatorcontrib><creatorcontrib>Lim, Y</creatorcontrib><creatorcontrib>Lim, S-T</creatorcontrib><creatorcontrib>Mitra, S K</creatorcontrib><creatorcontrib>Uryu, S</creatorcontrib><creatorcontrib>Chen, M</creatorcontrib><creatorcontrib>Pallen, C J</creatorcontrib><creatorcontrib>Cheung, N-Kv</creatorcontrib><creatorcontrib>Mikolon, D</creatorcontrib><creatorcontrib>Mielgo, A</creatorcontrib><creatorcontrib>Stupack, D G</creatorcontrib><creatorcontrib>Schlaepfer, D D</creatorcontrib><title>Distinct FAK-Src activation events promote α5β1 and α4β1 integrin-stimulated neuroblastoma cell motility</title><title>Oncogene</title><addtitle>Oncogene</addtitle><description>Signals from fibronectin-binding integrins promote neural crest cell motility during development in part through protein-tyrosine kinase (PTK) activation. Neuroblastoma (NB) is a neural crest malignancy with high metastatic potential. We find that α4 and α5 integrins are present in late-stage NB tumors and cell lines derived thereof. To determine the signaling connections promoting either α4β1- or α5β1-initiated NB cell motility, pharmacological, dominant negative and short-hairpin RNA (shRNA) inhibitory approaches were undertaken. shRNA knockdown revealed that α5β1-stimulated NB motility is dependent upon focal adhesion kinase (FAK) PTK, Src PTK and p130Cas adapter protein expression. Cell reconstitution showed that FAK catalytic activity is required for α5β1-stimulated Src activation in part through direct FAK phosphorylation of Src at Tyr-418. Alternatively, α4β1-stimulated NB cell motility is dependent upon Src and p130Cas but FAK is not essential. Catalytically inactive receptor protein-tyrosine phosphatase-α overexpression inhibited α4β1-stimulated NB motility and Src activation consistent with α4-regulated Src activity occurring through Src Tyr-529 dephosphorylation. In α4 shRNA-expressing NB cells, α4β1-stimulated Src activation and NB cell motility were rescued by wild type but not cytoplasmic domain-truncated α4 re-expression. These studies, supported by results using reconstituted fibroblasts, reveal that α4β1-mediated Src activation is mechanistically distinct from FAK-mediated Src activation during α5β1-mediated NB migration and support the evaluation of inhibitors to α4, Src and FAK in the control of NB tumor progression.</description><subject>Adapter proteins</subject><subject>Apoptosis</subject><subject>Biological and medical sciences</subject><subject>Cell activation</subject><subject>Cell Biology</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Cellular signal transduction</subject><subject>Dephosphorylation</subject><subject>Fibroblasts</subject><subject>Fibronectin</subject><subject>Focal adhesion kinase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genetic aspects</subject><subject>Human Genetics</subject><subject>Integrins</subject><subject>Internal Medicine</subject><subject>Malignancy</subject><subject>Medical sciences</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Metastases</subject><subject>Molecular and cellular biology</subject><subject>Motility</subject><subject>Neural crest</subject><subject>Neuroblastoma</subject><subject>Neurology</subject><subject>Oncology</subject><subject>original-article</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein-tyrosine kinase</subject><subject>Protein-tyrosine-phosphatase</subject><subject>Risk factors</subject><subject>Src protein</subject><subject>Tumors</subject><subject>Tumors of the nervous system. 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Action of oncogenes and antioncogenes</topic><topic>Cellular signal transduction</topic><topic>Dephosphorylation</topic><topic>Fibroblasts</topic><topic>Fibronectin</topic><topic>Focal adhesion kinase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Genetic aspects</topic><topic>Human Genetics</topic><topic>Integrins</topic><topic>Internal Medicine</topic><topic>Malignancy</topic><topic>Medical sciences</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Metastases</topic><topic>Molecular and cellular biology</topic><topic>Motility</topic><topic>Neural crest</topic><topic>Neuroblastoma</topic><topic>Neurology</topic><topic>Oncology</topic><topic>original-article</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Protein-tyrosine kinase</topic><topic>Protein-tyrosine-phosphatase</topic><topic>Risk factors</topic><topic>Src protein</topic><topic>Tumors</topic><topic>Tumors of the nervous system. Phacomatoses</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wu, L</creatorcontrib><creatorcontrib>Bernard-Trifilo, J A</creatorcontrib><creatorcontrib>Lim, Y</creatorcontrib><creatorcontrib>Lim, S-T</creatorcontrib><creatorcontrib>Mitra, S K</creatorcontrib><creatorcontrib>Uryu, S</creatorcontrib><creatorcontrib>Chen, M</creatorcontrib><creatorcontrib>Pallen, C J</creatorcontrib><creatorcontrib>Cheung, N-Kv</creatorcontrib><creatorcontrib>Mikolon, D</creatorcontrib><creatorcontrib>Mielgo, A</creatorcontrib><creatorcontrib>Stupack, D G</creatorcontrib><creatorcontrib>Schlaepfer, D D</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wu, L</au><au>Bernard-Trifilo, J A</au><au>Lim, Y</au><au>Lim, S-T</au><au>Mitra, S K</au><au>Uryu, S</au><au>Chen, M</au><au>Pallen, C J</au><au>Cheung, N-Kv</au><au>Mikolon, D</au><au>Mielgo, A</au><au>Stupack, D G</au><au>Schlaepfer, D D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct FAK-Src activation events promote α5β1 and α4β1 integrin-stimulated neuroblastoma cell motility</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><date>2008-02-28</date><risdate>2008</risdate><volume>27</volume><issue>10</issue><spage>1439</spage><epage>1448</epage><pages>1439-1448</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>Signals from fibronectin-binding integrins promote neural crest cell motility during development in part through protein-tyrosine kinase (PTK) activation. Neuroblastoma (NB) is a neural crest malignancy with high metastatic potential. We find that α4 and α5 integrins are present in late-stage NB tumors and cell lines derived thereof. To determine the signaling connections promoting either α4β1- or α5β1-initiated NB cell motility, pharmacological, dominant negative and short-hairpin RNA (shRNA) inhibitory approaches were undertaken. shRNA knockdown revealed that α5β1-stimulated NB motility is dependent upon focal adhesion kinase (FAK) PTK, Src PTK and p130Cas adapter protein expression. Cell reconstitution showed that FAK catalytic activity is required for α5β1-stimulated Src activation in part through direct FAK phosphorylation of Src at Tyr-418. Alternatively, α4β1-stimulated NB cell motility is dependent upon Src and p130Cas but FAK is not essential. Catalytically inactive receptor protein-tyrosine phosphatase-α overexpression inhibited α4β1-stimulated NB motility and Src activation consistent with α4-regulated Src activity occurring through Src Tyr-529 dephosphorylation. In α4 shRNA-expressing NB cells, α4β1-stimulated Src activation and NB cell motility were rescued by wild type but not cytoplasmic domain-truncated α4 re-expression. These studies, supported by results using reconstituted fibroblasts, reveal that α4β1-mediated Src activation is mechanistically distinct from FAK-mediated Src activation during α5β1-mediated NB migration and support the evaluation of inhibitors to α4, Src and FAK in the control of NB tumor progression.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>17828307</pmid><doi>10.1038/sj.onc.1210770</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adapter proteins Apoptosis Biological and medical sciences Cell activation Cell Biology Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cellular signal transduction Dephosphorylation Fibroblasts Fibronectin Focal adhesion kinase Fundamental and applied biological sciences. Psychology Genetic aspects Human Genetics Integrins Internal Medicine Malignancy Medical sciences Medicine Medicine & Public Health Metastases Molecular and cellular biology Motility Neural crest Neuroblastoma Neurology Oncology original-article Phosphorylation Physiological aspects Protein-tyrosine kinase Protein-tyrosine-phosphatase Risk factors Src protein Tumors Tumors of the nervous system. Phacomatoses |
| title | Distinct FAK-Src activation events promote α5β1 and α4β1 integrin-stimulated neuroblastoma cell motility |
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