Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae
Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Singh, Vikash [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014transfer abstract |
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| Schlagwörter: |
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| Umfang: |
9 |
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| Übergeordnetes Werk: |
Enthalten in: Mexican student-teachers’ “English” language praxicum: Decolonizing attempts - López-Gopar, Mario E. ELSEVIER, 2022, EJP, New York, NY [u.a.] |
|---|---|
| Übergeordnetes Werk: |
volume:736 ; year:2014 ; day:5 ; month:08 ; pages:77-85 ; extent:9 |
| Links: |
|---|
| DOI / URN: |
10.1016/j.ejphar.2014.04.032 |
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ELV023058838 |
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| 245 | 1 | 0 | |a Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae |
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| 520 | |a Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. | ||
| 520 | |a Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. | ||
| 650 | 7 | |a Hog1 phosphorylation |2 Elsevier | |
| 650 | 7 | |a KP1019 |2 Elsevier | |
| 650 | 7 | |a Anti-cancer drug |2 Elsevier | |
| 650 | 7 | |a GPD1 up-regulation |2 Elsevier | |
| 650 | 7 | |a Mitogen-activated protein kinases |2 Elsevier | |
| 650 | 7 | |a Protein ubiquitination |2 Elsevier | |
| 700 | 1 | |a Azad, Gajendra Kumar |4 oth | |
| 700 | 1 | |a Reddy M., Amarendar |4 oth | |
| 700 | 1 | |a Baranwal, Shivani |4 oth | |
| 700 | 1 | |a Tomar, Raghuvir S. |4 oth | |
| 773 | 0 | 8 | |i Enthalten in |n Elsevier |a López-Gopar, Mario E. ELSEVIER |t Mexican student-teachers’ “English” language praxicum: Decolonizing attempts |d 2022 |d EJP |g New York, NY [u.a.] |w (DE-627)ELV008405875 |
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10.1016/j.ejphar.2014.04.032 doi GBVA2014020000026.pica (DE-627)ELV023058838 (ELSEVIER)S0014-2999(14)00328-8 DE-627 ger DE-627 rakwb eng 610 610 DE-600 370 VZ 5,3 ssgn Singh, Vikash verfasserin aut Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae 2014transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Hog1 phosphorylation Elsevier KP1019 Elsevier Anti-cancer drug Elsevier GPD1 up-regulation Elsevier Mitogen-activated protein kinases Elsevier Protein ubiquitination Elsevier Azad, Gajendra Kumar oth Reddy M., Amarendar oth Baranwal, Shivani oth Tomar, Raghuvir S. oth Enthalten in Elsevier López-Gopar, Mario E. ELSEVIER Mexican student-teachers’ “English” language praxicum: Decolonizing attempts 2022 EJP New York, NY [u.a.] (DE-627)ELV008405875 volume:736 year:2014 day:5 month:08 pages:77-85 extent:9 https://doi.org/10.1016/j.ejphar.2014.04.032 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U AR 736 2014 5 0805 77-85 9 045F 610 |
| spelling |
10.1016/j.ejphar.2014.04.032 doi GBVA2014020000026.pica (DE-627)ELV023058838 (ELSEVIER)S0014-2999(14)00328-8 DE-627 ger DE-627 rakwb eng 610 610 DE-600 370 VZ 5,3 ssgn Singh, Vikash verfasserin aut Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae 2014transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Hog1 phosphorylation Elsevier KP1019 Elsevier Anti-cancer drug Elsevier GPD1 up-regulation Elsevier Mitogen-activated protein kinases Elsevier Protein ubiquitination Elsevier Azad, Gajendra Kumar oth Reddy M., Amarendar oth Baranwal, Shivani oth Tomar, Raghuvir S. oth Enthalten in Elsevier López-Gopar, Mario E. ELSEVIER Mexican student-teachers’ “English” language praxicum: Decolonizing attempts 2022 EJP New York, NY [u.a.] (DE-627)ELV008405875 volume:736 year:2014 day:5 month:08 pages:77-85 extent:9 https://doi.org/10.1016/j.ejphar.2014.04.032 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U AR 736 2014 5 0805 77-85 9 045F 610 |
| allfields_unstemmed |
10.1016/j.ejphar.2014.04.032 doi GBVA2014020000026.pica (DE-627)ELV023058838 (ELSEVIER)S0014-2999(14)00328-8 DE-627 ger DE-627 rakwb eng 610 610 DE-600 370 VZ 5,3 ssgn Singh, Vikash verfasserin aut Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae 2014transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Hog1 phosphorylation Elsevier KP1019 Elsevier Anti-cancer drug Elsevier GPD1 up-regulation Elsevier Mitogen-activated protein kinases Elsevier Protein ubiquitination Elsevier Azad, Gajendra Kumar oth Reddy M., Amarendar oth Baranwal, Shivani oth Tomar, Raghuvir S. oth Enthalten in Elsevier López-Gopar, Mario E. ELSEVIER Mexican student-teachers’ “English” language praxicum: Decolonizing attempts 2022 EJP New York, NY [u.a.] (DE-627)ELV008405875 volume:736 year:2014 day:5 month:08 pages:77-85 extent:9 https://doi.org/10.1016/j.ejphar.2014.04.032 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U AR 736 2014 5 0805 77-85 9 045F 610 |
| allfieldsGer |
10.1016/j.ejphar.2014.04.032 doi GBVA2014020000026.pica (DE-627)ELV023058838 (ELSEVIER)S0014-2999(14)00328-8 DE-627 ger DE-627 rakwb eng 610 610 DE-600 370 VZ 5,3 ssgn Singh, Vikash verfasserin aut Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae 2014transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Hog1 phosphorylation Elsevier KP1019 Elsevier Anti-cancer drug Elsevier GPD1 up-regulation Elsevier Mitogen-activated protein kinases Elsevier Protein ubiquitination Elsevier Azad, Gajendra Kumar oth Reddy M., Amarendar oth Baranwal, Shivani oth Tomar, Raghuvir S. oth Enthalten in Elsevier López-Gopar, Mario E. ELSEVIER Mexican student-teachers’ “English” language praxicum: Decolonizing attempts 2022 EJP New York, NY [u.a.] (DE-627)ELV008405875 volume:736 year:2014 day:5 month:08 pages:77-85 extent:9 https://doi.org/10.1016/j.ejphar.2014.04.032 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U AR 736 2014 5 0805 77-85 9 045F 610 |
| allfieldsSound |
10.1016/j.ejphar.2014.04.032 doi GBVA2014020000026.pica (DE-627)ELV023058838 (ELSEVIER)S0014-2999(14)00328-8 DE-627 ger DE-627 rakwb eng 610 610 DE-600 370 VZ 5,3 ssgn Singh, Vikash verfasserin aut Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae 2014transfer abstract 9 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. Hog1 phosphorylation Elsevier KP1019 Elsevier Anti-cancer drug Elsevier GPD1 up-regulation Elsevier Mitogen-activated protein kinases Elsevier Protein ubiquitination Elsevier Azad, Gajendra Kumar oth Reddy M., Amarendar oth Baranwal, Shivani oth Tomar, Raghuvir S. oth Enthalten in Elsevier López-Gopar, Mario E. ELSEVIER Mexican student-teachers’ “English” language praxicum: Decolonizing attempts 2022 EJP New York, NY [u.a.] (DE-627)ELV008405875 volume:736 year:2014 day:5 month:08 pages:77-85 extent:9 https://doi.org/10.1016/j.ejphar.2014.04.032 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U AR 736 2014 5 0805 77-85 9 045F 610 |
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Anti-cancer drug KP1019 induces Hog1 phosphorylation and protein ubiquitylation in Saccharomyces cerevisiae |
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Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. |
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Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. |
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Ruthenium-based anti-cancer drugs have attracted increasing interest in the last 20 years. KP1019 is one of the ruthenium-containing compounds that has demonstrated anti-tumor activity against various cancers, and has been tested in several clinical trials. Despite its success, the mode of action of KP1019 is not well described. In the present study, we have used budding yeast Saccharomyces cerevisiae to elucidate the action of KP1019. We have found that KP1019 causes dose-dependent cell arrest in the S-phase of cell cycle. Furthermore, we have demonstrated for the first time that the yeast mitogen-activated protein (MAP) kinase Hog1 is essential for the cells in response to KP1019. Hog1 is rapidly phosphorylated upon treatment with KP1019, and the deletion of the HOG1 gene potentiates the growth inhibition effect of KP1019. Moreover, we also observed the up-regulation of glycerol-3-phosphate dehydrogenase 1 (GPD1) mRNA in response to KP1019 treatment, a factor that is essential for the hyperosmotic stress response. Our results also reveal that membrane-bound sensor proteins of high osmolarity glycerol (HOG) pathway are crucial for Hog1 phosphorylation in response to KP1019-induced stress. Furthermore, KP1019 has also been found to increase the accumulation of ubiquitinated proteins and deletion of several members of ubiquitination pathways conferred sensitivity for KP1019. The findings presented here strongly suggest the ability of KP1019 to activate Hog1 MAP kinase and induce protein ubiquitination, which may underlie the therapeutic potential of this compound. In summary, we have disclosed a novel mechanism of KP1019 activity. |
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