PTPD1 Supports Receptor Stability and Mitogenic Signaling in Bladder Cancer Cells
PTPD1, a cytosolic non-receptor protein-tyrosine phosphatase, stimulates the Src-EGF transduction pathway. Localization of PTPD1 at actin cytoskeleton and adhesion sites is required for cell scattering and migration. Here, we show that during EGF stimulation, PTPD1 is rapidly recruited to endocytic...
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| Veröffentlicht in: | The Journal of biological chemistry 2010-12, Vol.285 (50), p.39260-39270 |
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| container_title | The Journal of biological chemistry |
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| creator | Carlucci, Annalisa Porpora, Monia Garbi, Corrado Galgani, Mario Santoriello, Margherita Mascolo, Massimo di Lorenzo, Domenico Altieri, Vincenzo Quarto, Maria Terracciano, Luigi Gottesman, Max E. Insabato, Luigi Feliciello, Antonio |
| description | PTPD1, a cytosolic non-receptor protein-tyrosine phosphatase, stimulates the Src-EGF transduction pathway. Localization of PTPD1 at actin cytoskeleton and adhesion sites is required for cell scattering and migration. Here, we show that during EGF stimulation, PTPD1 is rapidly recruited to endocytic vesicles containing the EGF receptor. Endosomal localization of PTPD1 is mediated by interaction with KIF16B, an endosomal kinesin that modulates receptor recycling at the plasma membrane. Silencing of PTPD1 promotes degradation of EGF receptor and inhibits downstream ERK signaling. We also found that PTPD1 is markedly increased in bladder cancer tissue samples. PTPD1 levels positively correlated with the grading and invasiveness potential of these tumors. Transgenic expression of an inactive PTPD1 mutant or genetic knockdown of the endogenous PTPD1 severely inhibited both growth and motility of human bladder cancer cells. These findings identify PTPD1 as a novel component of the endocytic machinery that impacts on EGF receptor stability and on growth and motility of bladder cancer cells. |
| doi_str_mv | 10.1074/jbc.M110.174706 |
| format | Article |
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Localization of PTPD1 at actin cytoskeleton and adhesion sites is required for cell scattering and migration. Here, we show that during EGF stimulation, PTPD1 is rapidly recruited to endocytic vesicles containing the EGF receptor. Endosomal localization of PTPD1 is mediated by interaction with KIF16B, an endosomal kinesin that modulates receptor recycling at the plasma membrane. Silencing of PTPD1 promotes degradation of EGF receptor and inhibits downstream ERK signaling. We also found that PTPD1 is markedly increased in bladder cancer tissue samples. PTPD1 levels positively correlated with the grading and invasiveness potential of these tumors. Transgenic expression of an inactive PTPD1 mutant or genetic knockdown of the endogenous PTPD1 severely inhibited both growth and motility of human bladder cancer cells. These findings identify PTPD1 as a novel component of the endocytic machinery that impacts on EGF receptor stability and on growth and motility of bladder cancer cells.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M110.174706</identifier><identifier>PMID: 20923765</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Actins - chemistry ; Biomarkers, Tumor ; Cell Biology ; Cell Line, Tumor ; Cell Movement ; Cytoskeleton - metabolism ; ErbB Receptors - metabolism ; Gene Expression Regulation, Neoplastic ; Gene Silencing ; HEK293 Cells ; Humans ; Kinesin - chemistry ; Neoplasm Invasiveness ; Phosphatase ; Protein Tyrosine Phosphatases, Non-Receptor - metabolism ; Receptor-tyrosine Kinase ; Signal Transduction ; Tumor ; Tumor Marker ; Urinary Bladder Neoplasms - metabolism</subject><ispartof>The Journal of biological chemistry, 2010-12, Vol.285 (50), p.39260-39270</ispartof><rights>2010 © 2010 ASBMB. 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These findings identify PTPD1 as a novel component of the endocytic machinery that impacts on EGF receptor stability and on growth and motility of bladder cancer cells.</description><subject>Actins - chemistry</subject><subject>Biomarkers, Tumor</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement</subject><subject>Cytoskeleton - metabolism</subject><subject>ErbB Receptors - metabolism</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Gene Silencing</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Kinesin - chemistry</subject><subject>Neoplasm Invasiveness</subject><subject>Phosphatase</subject><subject>Protein Tyrosine Phosphatases, Non-Receptor - metabolism</subject><subject>Receptor-tyrosine Kinase</subject><subject>Signal Transduction</subject><subject>Tumor</subject><subject>Tumor Marker</subject><subject>Urinary Bladder Neoplasms - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kdFv1SAUxolxcXdXn33TvvnUjVNaCi8m7urUZIvTuyW-EQqnlaW3VOhdsv9-NJ2LexghORB-fAe-j5C3QI-B1uXJTWOOL2De1WVN-QuyAipYzir4_ZKsKC0gl0UlDslRjDc0jVLCK3JYUFmwmlcr8vPy6vIzZNv9OPowxewXGhwnH7LtpBvXu-ku04PNLtzkOxycybauG3Tvhi5zQ3baa2sxZBs9mLlg38fX5KDVfcQ3D3VNrs--XG2-5ec_vn7ffDrPTcn5lDdQt23DG0AqjAVkjOpC1LRBMGklBSsRtAQrao5gDS8rpltZCdsUkjWSrcnHRXfcNzu0Bocp6F6Nwe10uFNeO_X0ZHB_VOdvVSGlgJIngQ8PAsH_3WOc1M5Fk76gB_T7qARwJsp5rsnJQprgYwzYPnYBquYcVMpBzTmoJYd0493_j3vk_xmfgPcL0GqvdBdcVNfbggKjIIELThMhFwKTibcOg4rGYfLZuoBmUta7Z9vfAwOdoOg</recordid><startdate>20101210</startdate><enddate>20101210</enddate><creator>Carlucci, Annalisa</creator><creator>Porpora, Monia</creator><creator>Garbi, Corrado</creator><creator>Galgani, Mario</creator><creator>Santoriello, Margherita</creator><creator>Mascolo, Massimo</creator><creator>di Lorenzo, Domenico</creator><creator>Altieri, Vincenzo</creator><creator>Quarto, Maria</creator><creator>Terracciano, Luigi</creator><creator>Gottesman, Max E.</creator><creator>Insabato, Luigi</creator><creator>Feliciello, Antonio</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><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>7X8</scope><scope>5PM</scope></search><sort><creationdate>20101210</creationdate><title>PTPD1 Supports Receptor Stability and Mitogenic Signaling in Bladder Cancer Cells</title><author>Carlucci, Annalisa ; 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Localization of PTPD1 at actin cytoskeleton and adhesion sites is required for cell scattering and migration. Here, we show that during EGF stimulation, PTPD1 is rapidly recruited to endocytic vesicles containing the EGF receptor. Endosomal localization of PTPD1 is mediated by interaction with KIF16B, an endosomal kinesin that modulates receptor recycling at the plasma membrane. Silencing of PTPD1 promotes degradation of EGF receptor and inhibits downstream ERK signaling. We also found that PTPD1 is markedly increased in bladder cancer tissue samples. PTPD1 levels positively correlated with the grading and invasiveness potential of these tumors. Transgenic expression of an inactive PTPD1 mutant or genetic knockdown of the endogenous PTPD1 severely inhibited both growth and motility of human bladder cancer cells. 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| ispartof | The Journal of biological chemistry, 2010-12, Vol.285 (50), p.39260-39270 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Actins - chemistry Biomarkers, Tumor Cell Biology Cell Line, Tumor Cell Movement Cytoskeleton - metabolism ErbB Receptors - metabolism Gene Expression Regulation, Neoplastic Gene Silencing HEK293 Cells Humans Kinesin - chemistry Neoplasm Invasiveness Phosphatase Protein Tyrosine Phosphatases, Non-Receptor - metabolism Receptor-tyrosine Kinase Signal Transduction Tumor Tumor Marker Urinary Bladder Neoplasms - metabolism |
| title | PTPD1 Supports Receptor Stability and Mitogenic Signaling in Bladder Cancer Cells |
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