PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells
Protein kinase C delta (PKCδ) is a serine (Ser)/threonine kinase, which regulates numerous cellular processes, including proliferation, differentiation, migration and apoptosis. In the current study, Chinese hamster ovary cells were transfected with either a constitutively activated PKCδ or a domina...
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| Veröffentlicht in: | Oncogene 2013-09, Vol.32 (38), p.4539-4548 |
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| creator | Li, N Du, Z-X Zong, Z-H Liu, B-Q Li, C Zhang, Q Wang, H-Q |
| description | Protein kinase C delta (PKCδ) is a serine (Ser)/threonine kinase, which regulates numerous cellular processes, including proliferation, differentiation, migration and apoptosis. In the current study, Chinese hamster ovary cells were transfected with either a constitutively activated PKCδ or a dominant negative PKCδ, phosphoprotein enrichment, two-dimensional difference gel electrophoresis and mass spectrometry was combined to globally identified candidates of PKCδ cascade. We found that Bcl-2 associated athanogene 3 (BAG3) was one of the targets of PKCδ cascade, and BAG3 interacted with PKCδ
in vivo
. In addition, we clarified that BAG3 was phosphorylate at Ser187 site in a PKCδ-dependent manner
in vivo
. BAG3 has been implicated in multiple cellular functions, including proliferation, differentiation, apoptosis, migration, invasion, macroautophagy and so on. We generated wild-type (WT)-, Ser187Ala (S187A)- or Ser187Asp (S187D)-BAG3 stably expressing FRO cells, and noticed that phosphorylation state of BAG3 influenced FRO morphology. Finally, for the first time, we showed that BAG3 was implicated in epithelial−mesenchymal transition (EMT) procedure, and phosphorylation state at Ser187 site had a critical role in EMT regulation by BAG3. Collectively, the current study indicates that BAG3 is a novel substrate of PKCδ, and PKCδ-mediated phosphorylation of BAG3 is implicated in EMT and invasiveness of thyroid cancer cells. |
| doi_str_mv | 10.1038/onc.2012.466 |
| format | Article |
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in vivo
. In addition, we clarified that BAG3 was phosphorylate at Ser187 site in a PKCδ-dependent manner
in vivo
. BAG3 has been implicated in multiple cellular functions, including proliferation, differentiation, apoptosis, migration, invasion, macroautophagy and so on. We generated wild-type (WT)-, Ser187Ala (S187A)- or Ser187Asp (S187D)-BAG3 stably expressing FRO cells, and noticed that phosphorylation state of BAG3 influenced FRO morphology. Finally, for the first time, we showed that BAG3 was implicated in epithelial−mesenchymal transition (EMT) procedure, and phosphorylation state at Ser187 site had a critical role in EMT regulation by BAG3. Collectively, the current study indicates that BAG3 is a novel substrate of PKCδ, and PKCδ-mediated phosphorylation of BAG3 is implicated in EMT and invasiveness of thyroid cancer cells.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2012.466</identifier><identifier>PMID: 23108398</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/67/1459/1843 ; 631/80/458/1733 ; 631/80/84/2176 ; 631/80/84/2336 ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; Apoptosis ; Apoptosis Regulatory Proteins ; Bcl-2 protein ; Cancer cells ; Cell Biology ; Cell Line, Tumor ; Cell Movement - genetics ; CHO Cells ; Cricetulus ; Cytology ; Development and progression ; Epithelial-Mesenchymal Transition - genetics ; Gel electrophoresis ; Human Genetics ; Humans ; Internal Medicine ; Invasiveness ; Kinases ; Mass spectroscopy ; Medicine ; Medicine & Public Health ; Mesenchyme ; Oncology ; original-article ; Phosphorylation ; Physiological aspects ; Protein Binding ; Protein kinase C ; Protein Kinase C-delta - genetics ; Protein Kinase C-delta - metabolism ; Protein kinases ; Protein-serine/threonine kinase ; Serine - metabolism ; Thyroid cancer ; Thyroid Neoplasms - genetics ; Thyroid Neoplasms - metabolism ; Thyroid Neoplasms - pathology</subject><ispartof>Oncogene, 2013-09, Vol.32 (38), p.4539-4548</ispartof><rights>Macmillan Publishers Limited 2013</rights><rights>COPYRIGHT 2013 Nature Publishing Group</rights><rights>Macmillan Publishers Limited 2013.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-fd632d6241cb74f08428b6d5f0ed67ae624a54e0f6924d75b983f275ec3171303</citedby><cites>FETCH-LOGICAL-c456t-fd632d6241cb74f08428b6d5f0ed67ae624a54e0f6924d75b983f275ec3171303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/onc.2012.466$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/onc.2012.466$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23108398$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, N</creatorcontrib><creatorcontrib>Du, Z-X</creatorcontrib><creatorcontrib>Zong, Z-H</creatorcontrib><creatorcontrib>Liu, B-Q</creatorcontrib><creatorcontrib>Li, C</creatorcontrib><creatorcontrib>Zhang, Q</creatorcontrib><creatorcontrib>Wang, H-Q</creatorcontrib><title>PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>Protein kinase C delta (PKCδ) is a serine (Ser)/threonine kinase, which regulates numerous cellular processes, including proliferation, differentiation, migration and apoptosis. In the current study, Chinese hamster ovary cells were transfected with either a constitutively activated PKCδ or a dominant negative PKCδ, phosphoprotein enrichment, two-dimensional difference gel electrophoresis and mass spectrometry was combined to globally identified candidates of PKCδ cascade. We found that Bcl-2 associated athanogene 3 (BAG3) was one of the targets of PKCδ cascade, and BAG3 interacted with PKCδ
in vivo
. In addition, we clarified that BAG3 was phosphorylate at Ser187 site in a PKCδ-dependent manner
in vivo
. BAG3 has been implicated in multiple cellular functions, including proliferation, differentiation, apoptosis, migration, invasion, macroautophagy and so on. We generated wild-type (WT)-, Ser187Ala (S187A)- or Ser187Asp (S187D)-BAG3 stably expressing FRO cells, and noticed that phosphorylation state of BAG3 influenced FRO morphology. Finally, for the first time, we showed that BAG3 was implicated in epithelial−mesenchymal transition (EMT) procedure, and phosphorylation state at Ser187 site had a critical role in EMT regulation by BAG3. Collectively, the current study indicates that BAG3 is a novel substrate of PKCδ, and PKCδ-mediated phosphorylation of BAG3 is implicated in EMT and invasiveness of thyroid cancer cells.</description><subject>631/67/1459/1843</subject><subject>631/80/458/1733</subject><subject>631/80/84/2176</subject><subject>631/80/84/2336</subject><subject>Adaptor Proteins, Signal Transducing - genetics</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis Regulatory Proteins</subject><subject>Bcl-2 protein</subject><subject>Cancer cells</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement - genetics</subject><subject>CHO Cells</subject><subject>Cricetulus</subject><subject>Cytology</subject><subject>Development and progression</subject><subject>Epithelial-Mesenchymal Transition - genetics</subject><subject>Gel electrophoresis</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Invasiveness</subject><subject>Kinases</subject><subject>Mass spectroscopy</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Mesenchyme</subject><subject>Oncology</subject><subject>original-article</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein Binding</subject><subject>Protein kinase C</subject><subject>Protein Kinase C-delta - genetics</subject><subject>Protein Kinase C-delta - metabolism</subject><subject>Protein kinases</subject><subject>Protein-serine/threonine kinase</subject><subject>Serine - metabolism</subject><subject>Thyroid cancer</subject><subject>Thyroid Neoplasms - genetics</subject><subject>Thyroid Neoplasms - metabolism</subject><subject>Thyroid Neoplasms - pathology</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNks2KFDEUhYMoTtu6cy0BNy6sNr-VyrJtnFEcGPFnHdLJrakM1ak2qRroN3DtxhfxOXwIn8QUPTogLlyEEM6Xc29yD0KPKVlRwpsXQ3QrRihbibq-gxZUqLqSUou7aEG0JJVmnJ2gBzlfEUKUJuw-OmGckobrZoG-vXu7-fG92oEPdgSP992Qy0qH3o5hiHho8cv1Gcd2xB8g0UbhHEbAIfrJQcawD2MHfbD9zy9fd5Ahuu6wsz0ek42FnC1s9BhiZ-N8IcRrm8M1RMjzAY_dIQ3BYzfLCZ--v8AO-j4_RPda22d4dLMv0afTVx83r6vzi7M3m_V55YSsx6r1NWe-ZoK6rRItaQRrtrWXLQFfKwtFsVIAaWvNhFdyqxveMiXBcaooJ3yJnh1992n4PEEezS7kuQMbYZiyoYJrRrWk9H9QoQTTQhX06V_o1TClWB5iWC2oZJILektd2h5MiO1Qfs3NpmZdrJjmM7hEz4-US0POCVqzT2Fn08FQYuYEmJIAMyfAlAQU_MlN6WlbpvoH_j3yAlRHIBcpXkK67e2fhr8Alri7kw</recordid><startdate>20130919</startdate><enddate>20130919</enddate><creator>Li, N</creator><creator>Du, Z-X</creator><creator>Zong, Z-H</creator><creator>Liu, B-Q</creator><creator>Li, C</creator><creator>Zhang, Q</creator><creator>Wang, H-Q</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20130919</creationdate><title>PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells</title><author>Li, N ; Du, Z-X ; Zong, Z-H ; Liu, B-Q ; Li, C ; Zhang, Q ; Wang, H-Q</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-fd632d6241cb74f08428b6d5f0ed67ae624a54e0f6924d75b983f275ec3171303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>631/67/1459/1843</topic><topic>631/80/458/1733</topic><topic>631/80/84/2176</topic><topic>631/80/84/2336</topic><topic>Adaptor Proteins, Signal Transducing - genetics</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis Regulatory Proteins</topic><topic>Bcl-2 protein</topic><topic>Cancer cells</topic><topic>Cell Biology</topic><topic>Cell Line, Tumor</topic><topic>Cell Movement - genetics</topic><topic>CHO Cells</topic><topic>Cricetulus</topic><topic>Cytology</topic><topic>Development and progression</topic><topic>Epithelial-Mesenchymal Transition - genetics</topic><topic>Gel electrophoresis</topic><topic>Human Genetics</topic><topic>Humans</topic><topic>Internal Medicine</topic><topic>Invasiveness</topic><topic>Kinases</topic><topic>Mass spectroscopy</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Mesenchyme</topic><topic>Oncology</topic><topic>original-article</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Protein Binding</topic><topic>Protein kinase C</topic><topic>Protein Kinase C-delta - genetics</topic><topic>Protein Kinase C-delta - metabolism</topic><topic>Protein kinases</topic><topic>Protein-serine/threonine kinase</topic><topic>Serine - metabolism</topic><topic>Thyroid cancer</topic><topic>Thyroid Neoplasms - genetics</topic><topic>Thyroid Neoplasms - metabolism</topic><topic>Thyroid Neoplasms - pathology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, N</creatorcontrib><creatorcontrib>Du, Z-X</creatorcontrib><creatorcontrib>Zong, Z-H</creatorcontrib><creatorcontrib>Liu, B-Q</creatorcontrib><creatorcontrib>Li, C</creatorcontrib><creatorcontrib>Zhang, Q</creatorcontrib><creatorcontrib>Wang, H-Q</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</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 Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</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>MEDLINE - Academic</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, N</au><au>Du, Z-X</au><au>Zong, Z-H</au><au>Liu, B-Q</au><au>Li, C</au><au>Zhang, Q</au><au>Wang, H-Q</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2013-09-19</date><risdate>2013</risdate><volume>32</volume><issue>38</issue><spage>4539</spage><epage>4548</epage><pages>4539-4548</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>Protein kinase C delta (PKCδ) is a serine (Ser)/threonine kinase, which regulates numerous cellular processes, including proliferation, differentiation, migration and apoptosis. In the current study, Chinese hamster ovary cells were transfected with either a constitutively activated PKCδ or a dominant negative PKCδ, phosphoprotein enrichment, two-dimensional difference gel electrophoresis and mass spectrometry was combined to globally identified candidates of PKCδ cascade. We found that Bcl-2 associated athanogene 3 (BAG3) was one of the targets of PKCδ cascade, and BAG3 interacted with PKCδ
in vivo
. In addition, we clarified that BAG3 was phosphorylate at Ser187 site in a PKCδ-dependent manner
in vivo
. BAG3 has been implicated in multiple cellular functions, including proliferation, differentiation, apoptosis, migration, invasion, macroautophagy and so on. We generated wild-type (WT)-, Ser187Ala (S187A)- or Ser187Asp (S187D)-BAG3 stably expressing FRO cells, and noticed that phosphorylation state of BAG3 influenced FRO morphology. Finally, for the first time, we showed that BAG3 was implicated in epithelial−mesenchymal transition (EMT) procedure, and phosphorylation state at Ser187 site had a critical role in EMT regulation by BAG3. Collectively, the current study indicates that BAG3 is a novel substrate of PKCδ, and PKCδ-mediated phosphorylation of BAG3 is implicated in EMT and invasiveness of thyroid cancer cells.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23108398</pmid><doi>10.1038/onc.2012.466</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Oncogene, 2013-09, Vol.32 (38), p.4539-4548 |
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| source | MEDLINE; SpringerLink Journals; Nature Journals Online; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | 631/67/1459/1843 631/80/458/1733 631/80/84/2176 631/80/84/2336 Adaptor Proteins, Signal Transducing - genetics Adaptor Proteins, Signal Transducing - metabolism Animals Apoptosis Apoptosis Regulatory Proteins Bcl-2 protein Cancer cells Cell Biology Cell Line, Tumor Cell Movement - genetics CHO Cells Cricetulus Cytology Development and progression Epithelial-Mesenchymal Transition - genetics Gel electrophoresis Human Genetics Humans Internal Medicine Invasiveness Kinases Mass spectroscopy Medicine Medicine & Public Health Mesenchyme Oncology original-article Phosphorylation Physiological aspects Protein Binding Protein kinase C Protein Kinase C-delta - genetics Protein Kinase C-delta - metabolism Protein kinases Protein-serine/threonine kinase Serine - metabolism Thyroid cancer Thyroid Neoplasms - genetics Thyroid Neoplasms - metabolism Thyroid Neoplasms - pathology |
| title | PKCδ-mediated phosphorylation of BAG3 at Ser187 site induces epithelial−mesenchymal transition and enhances invasiveness in thyroid cancer FRO cells |
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