Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer
Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and e...
Ausführliche Beschreibung
Autor*in: |
Sherly I. Celada [verfasserIn] Guoliang Li [verfasserIn] Lindsay J. Celada [verfasserIn] Wenfu Lu [verfasserIn] Thanigaivelan Kanagasabai [verfasserIn] Weiran Feng [verfasserIn] Zhen Cao [verfasserIn] Nazifa Salsabeel [verfasserIn] Ninghui Mao [verfasserIn] LaKendria K. Brown [verfasserIn] Zaniya A. Mark [verfasserIn] Michael G. Izban [verfasserIn] Billy R. Ballard [verfasserIn] Xinchun Zhou [verfasserIn] Samuel E. Adunyah [verfasserIn] Robert J. Matusik [verfasserIn] Xiaofei Wang [verfasserIn] Zhenbang Chen [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2023 |
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Übergeordnetes Werk: |
In: Molecular Oncology - Wiley, 2017, 17(2023), 10, Seite 2126-2146 |
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Übergeordnetes Werk: |
volume:17 ; year:2023 ; number:10 ; pages:2126-2146 |
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Link aufrufen |
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DOI / URN: |
10.1002/1878-0261.13497 |
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Katalog-ID: |
DOAJ09673177X |
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245 | 1 | 0 | |a Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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520 | |a Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. | ||
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653 | 0 | |a Neoplasms. Tumors. Oncology. Including cancer and carcinogens | |
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700 | 0 | |a Lindsay J. Celada |e verfasserin |4 aut | |
700 | 0 | |a Wenfu Lu |e verfasserin |4 aut | |
700 | 0 | |a Thanigaivelan Kanagasabai |e verfasserin |4 aut | |
700 | 0 | |a Weiran Feng |e verfasserin |4 aut | |
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700 | 0 | |a Nazifa Salsabeel |e verfasserin |4 aut | |
700 | 0 | |a Ninghui Mao |e verfasserin |4 aut | |
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700 | 0 | |a Zaniya A. Mark |e verfasserin |4 aut | |
700 | 0 | |a Michael G. Izban |e verfasserin |4 aut | |
700 | 0 | |a Billy R. Ballard |e verfasserin |4 aut | |
700 | 0 | |a Xinchun Zhou |e verfasserin |4 aut | |
700 | 0 | |a Samuel E. Adunyah |e verfasserin |4 aut | |
700 | 0 | |a Robert J. Matusik |e verfasserin |4 aut | |
700 | 0 | |a Xiaofei Wang |e verfasserin |4 aut | |
700 | 0 | |a Zhenbang Chen |e verfasserin |4 aut | |
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10.1002/1878-0261.13497 doi (DE-627)DOAJ09673177X (DE-599)DOAJ0cac8103e1024d5d960e34525c1fc17d DE-627 ger DE-627 rakwb eng RC254-282 Sherly I. Celada verfasserin aut Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. FOXA1 luminal lineage prostate cancer SKP2 ubiquitination Neoplasms. Tumors. Oncology. Including cancer and carcinogens Guoliang Li verfasserin aut Lindsay J. Celada verfasserin aut Wenfu Lu verfasserin aut Thanigaivelan Kanagasabai verfasserin aut Weiran Feng verfasserin aut Zhen Cao verfasserin aut Nazifa Salsabeel verfasserin aut Ninghui Mao verfasserin aut LaKendria K. Brown verfasserin aut Zaniya A. Mark verfasserin aut Michael G. Izban verfasserin aut Billy R. Ballard verfasserin aut Xinchun Zhou verfasserin aut Samuel E. Adunyah verfasserin aut Robert J. Matusik verfasserin aut Xiaofei Wang verfasserin aut Zhenbang Chen verfasserin aut In Molecular Oncology Wiley, 2017 17(2023), 10, Seite 2126-2146 (DE-627)531199800 (DE-600)2322586-5 18780261 nnns volume:17 year:2023 number:10 pages:2126-2146 https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d kostenfrei https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/toc/1574-7891 Journal toc kostenfrei https://doaj.org/toc/1878-0261 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2023 10 2126-2146 |
spelling |
10.1002/1878-0261.13497 doi (DE-627)DOAJ09673177X (DE-599)DOAJ0cac8103e1024d5d960e34525c1fc17d DE-627 ger DE-627 rakwb eng RC254-282 Sherly I. Celada verfasserin aut Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. FOXA1 luminal lineage prostate cancer SKP2 ubiquitination Neoplasms. Tumors. Oncology. Including cancer and carcinogens Guoliang Li verfasserin aut Lindsay J. Celada verfasserin aut Wenfu Lu verfasserin aut Thanigaivelan Kanagasabai verfasserin aut Weiran Feng verfasserin aut Zhen Cao verfasserin aut Nazifa Salsabeel verfasserin aut Ninghui Mao verfasserin aut LaKendria K. Brown verfasserin aut Zaniya A. Mark verfasserin aut Michael G. Izban verfasserin aut Billy R. Ballard verfasserin aut Xinchun Zhou verfasserin aut Samuel E. Adunyah verfasserin aut Robert J. Matusik verfasserin aut Xiaofei Wang verfasserin aut Zhenbang Chen verfasserin aut In Molecular Oncology Wiley, 2017 17(2023), 10, Seite 2126-2146 (DE-627)531199800 (DE-600)2322586-5 18780261 nnns volume:17 year:2023 number:10 pages:2126-2146 https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d kostenfrei https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/toc/1574-7891 Journal toc kostenfrei https://doaj.org/toc/1878-0261 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2023 10 2126-2146 |
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10.1002/1878-0261.13497 doi (DE-627)DOAJ09673177X (DE-599)DOAJ0cac8103e1024d5d960e34525c1fc17d DE-627 ger DE-627 rakwb eng RC254-282 Sherly I. Celada verfasserin aut Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. FOXA1 luminal lineage prostate cancer SKP2 ubiquitination Neoplasms. Tumors. Oncology. Including cancer and carcinogens Guoliang Li verfasserin aut Lindsay J. Celada verfasserin aut Wenfu Lu verfasserin aut Thanigaivelan Kanagasabai verfasserin aut Weiran Feng verfasserin aut Zhen Cao verfasserin aut Nazifa Salsabeel verfasserin aut Ninghui Mao verfasserin aut LaKendria K. Brown verfasserin aut Zaniya A. Mark verfasserin aut Michael G. Izban verfasserin aut Billy R. Ballard verfasserin aut Xinchun Zhou verfasserin aut Samuel E. Adunyah verfasserin aut Robert J. Matusik verfasserin aut Xiaofei Wang verfasserin aut Zhenbang Chen verfasserin aut In Molecular Oncology Wiley, 2017 17(2023), 10, Seite 2126-2146 (DE-627)531199800 (DE-600)2322586-5 18780261 nnns volume:17 year:2023 number:10 pages:2126-2146 https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d kostenfrei https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/toc/1574-7891 Journal toc kostenfrei https://doaj.org/toc/1878-0261 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2023 10 2126-2146 |
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10.1002/1878-0261.13497 doi (DE-627)DOAJ09673177X (DE-599)DOAJ0cac8103e1024d5d960e34525c1fc17d DE-627 ger DE-627 rakwb eng RC254-282 Sherly I. Celada verfasserin aut Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. FOXA1 luminal lineage prostate cancer SKP2 ubiquitination Neoplasms. Tumors. Oncology. Including cancer and carcinogens Guoliang Li verfasserin aut Lindsay J. Celada verfasserin aut Wenfu Lu verfasserin aut Thanigaivelan Kanagasabai verfasserin aut Weiran Feng verfasserin aut Zhen Cao verfasserin aut Nazifa Salsabeel verfasserin aut Ninghui Mao verfasserin aut LaKendria K. Brown verfasserin aut Zaniya A. Mark verfasserin aut Michael G. Izban verfasserin aut Billy R. Ballard verfasserin aut Xinchun Zhou verfasserin aut Samuel E. Adunyah verfasserin aut Robert J. Matusik verfasserin aut Xiaofei Wang verfasserin aut Zhenbang Chen verfasserin aut In Molecular Oncology Wiley, 2017 17(2023), 10, Seite 2126-2146 (DE-627)531199800 (DE-600)2322586-5 18780261 nnns volume:17 year:2023 number:10 pages:2126-2146 https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d kostenfrei https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/toc/1574-7891 Journal toc kostenfrei https://doaj.org/toc/1878-0261 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2023 10 2126-2146 |
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10.1002/1878-0261.13497 doi (DE-627)DOAJ09673177X (DE-599)DOAJ0cac8103e1024d5d960e34525c1fc17d DE-627 ger DE-627 rakwb eng RC254-282 Sherly I. Celada verfasserin aut Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. FOXA1 luminal lineage prostate cancer SKP2 ubiquitination Neoplasms. Tumors. Oncology. Including cancer and carcinogens Guoliang Li verfasserin aut Lindsay J. Celada verfasserin aut Wenfu Lu verfasserin aut Thanigaivelan Kanagasabai verfasserin aut Weiran Feng verfasserin aut Zhen Cao verfasserin aut Nazifa Salsabeel verfasserin aut Ninghui Mao verfasserin aut LaKendria K. Brown verfasserin aut Zaniya A. Mark verfasserin aut Michael G. Izban verfasserin aut Billy R. Ballard verfasserin aut Xinchun Zhou verfasserin aut Samuel E. Adunyah verfasserin aut Robert J. Matusik verfasserin aut Xiaofei Wang verfasserin aut Zhenbang Chen verfasserin aut In Molecular Oncology Wiley, 2017 17(2023), 10, Seite 2126-2146 (DE-627)531199800 (DE-600)2322586-5 18780261 nnns volume:17 year:2023 number:10 pages:2126-2146 https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d kostenfrei https://doi.org/10.1002/1878-0261.13497 kostenfrei https://doaj.org/toc/1574-7891 Journal toc kostenfrei https://doaj.org/toc/1878-0261 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_647 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2118 GBV_ILN_2122 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2232 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 17 2023 10 2126-2146 |
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Sherly I. Celada @@aut@@ Guoliang Li @@aut@@ Lindsay J. Celada @@aut@@ Wenfu Lu @@aut@@ Thanigaivelan Kanagasabai @@aut@@ Weiran Feng @@aut@@ Zhen Cao @@aut@@ Nazifa Salsabeel @@aut@@ Ninghui Mao @@aut@@ LaKendria K. Brown @@aut@@ Zaniya A. Mark @@aut@@ Michael G. Izban @@aut@@ Billy R. Ballard @@aut@@ Xinchun Zhou @@aut@@ Samuel E. Adunyah @@aut@@ Robert J. Matusik @@aut@@ Xiaofei Wang @@aut@@ Zhenbang Chen @@aut@@ |
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R - Medicine |
author |
Sherly I. Celada |
spellingShingle |
Sherly I. Celada misc RC254-282 misc FOXA1 misc luminal lineage misc prostate cancer misc SKP2 misc ubiquitination misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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RC254-282 Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer FOXA1 luminal lineage prostate cancer SKP2 ubiquitination |
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misc RC254-282 misc FOXA1 misc luminal lineage misc prostate cancer misc SKP2 misc ubiquitination misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens |
topic_unstemmed |
misc RC254-282 misc FOXA1 misc luminal lineage misc prostate cancer misc SKP2 misc ubiquitination misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens |
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misc RC254-282 misc FOXA1 misc luminal lineage misc prostate cancer misc SKP2 misc ubiquitination misc Neoplasms. Tumors. Oncology. Including cancer and carcinogens |
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Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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Sherly I. Celada |
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Sherly I. Celada Guoliang Li Lindsay J. Celada Wenfu Lu Thanigaivelan Kanagasabai Weiran Feng Zhen Cao Nazifa Salsabeel Ninghui Mao LaKendria K. Brown Zaniya A. Mark Michael G. Izban Billy R. Ballard Xinchun Zhou Samuel E. Adunyah Robert J. Matusik Xiaofei Wang Zhenbang Chen |
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Sherly I. Celada |
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10.1002/1878-0261.13497 |
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verfasserin |
title_sort |
lysosome‐dependent foxa1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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RC254-282 |
title_auth |
Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
abstract |
Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. |
abstractGer |
Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. |
abstract_unstemmed |
Changes in FOXA1 (forkhead box protein A1) protein levels are well associated with prostate cancer (PCa) progression. Unfortunately, direct targeting of FOXA1 in progressive PCa remains challenging due to variations in FOXA1 protein levels, increased FOXA1 mutations at different stages of PCa, and elusive post‐translational FOXA1 regulating mechanisms. Here, we show that SKP2 (S‐phase kinase‐associated protein 2) catalyzes K6‐ and K29‐linked polyubiquitination of FOXA1 for lysosomal‐dependent degradation. Our data indicate increased SKP2:FOXA1 protein ratios in stage IV human PCa compared to stages I–III, together with a strong inverse correlation (r = −0.9659) between SKP2 and FOXA1 levels, suggesting that SKP2–FOXA1 protein interactions play a significant role in PCa progression. Prostate tumors of Pten/Trp53 mice displayed increased Skp2–Foxa1–Pcna signaling and colocalization, whereas disruption of the Skp2–Foxa1 interplay in Pten/Trp53/Skp2 triple‐null mice demonstrated decreased Pcna levels and increased expression of Foxa1 and luminal positive cells. Treatment of xenograft mice with the SKP2 inhibitor SZL P1‐41 decreased tumor proliferation, SKP2:FOXA1 ratios, and colocalization. Thus, our results highlight the significance of the SKP2–FOXA1 interplay on the luminal lineage in PCa and the potential of therapeutically targeting FOXA1 through SKP2 to improve PCa control. |
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Lysosome‐dependent FOXA1 ubiquitination contributes to luminal lineage of advanced prostate cancer |
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https://doi.org/10.1002/1878-0261.13497 https://doaj.org/article/0cac8103e1024d5d960e34525c1fc17d https://doaj.org/toc/1574-7891 https://doaj.org/toc/1878-0261 |
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Guoliang Li Lindsay J. Celada Wenfu Lu Thanigaivelan Kanagasabai Weiran Feng Zhen Cao Nazifa Salsabeel Ninghui Mao LaKendria K. Brown Zaniya A. Mark Michael G. Izban Billy R. Ballard Xinchun Zhou Samuel E. Adunyah Robert J. Matusik Xiaofei Wang Zhenbang Chen |
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Guoliang Li Lindsay J. Celada Wenfu Lu Thanigaivelan Kanagasabai Weiran Feng Zhen Cao Nazifa Salsabeel Ninghui Mao LaKendria K. Brown Zaniya A. Mark Michael G. Izban Billy R. Ballard Xinchun Zhou Samuel E. Adunyah Robert J. Matusik Xiaofei Wang Zhenbang Chen |
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2024-07-03T21:48:24.409Z |
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