SIRT3 regulates cancer cell proliferation through deacetylation of PYCR1 in proline metabolism
SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to pro...
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| Published in | Neoplasia (New York, N.Y.) Vol. 21; no. 7; pp. 665 - 675 |
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| Main Authors | , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
01.07.2019
Elsevier |
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| Abstract | SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to proline with concomitant generation of NAD+ and NADP+. PYCR1 is highly expressed in various cancers, and it can promote the growth of tumor cells. Here, through immunoprecipitation and mass spectrometry, we found that PYCR1 is in SIRT3’s interacting network. PYCR1 directly binds to SIRT3 both in vivo and in vitro. CBP is the acetyltransferase for PYCR1, whereas SIRT3 deacetylates PYCR1. We further identified that K228 is the major acetylation site for PYCR1. Acetylation of PYCR1 at K228 reduced its enzymatic activity by impairing the formation of the decamer of PYCR1. As a result, acetylation of PYCR1 at K228 inhibits cell proliferation, while deacetylation of PYCR1 mediated by SIRT3 increases PYCR1’s activity. Our findings on the regulation of PYCR1 linked proline metabolism with SIRT3, CBP and cell growth, thus providing a potential approach for cancer therapy. |
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| AbstractList | SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to proline with concomitant generation of NAD+ and NADP+. PYCR1 is highly expressed in various cancers, and it can promote the growth of tumor cells. Here, through immunoprecipitation and mass spectrometry, we found that PYCR1 is in SIRT3’s interacting network. PYCR1 directly binds to SIRT3 both in vivo and in vitro. CBP is the acetyltransferase for PYCR1, whereas SIRT3 deacetylates PYCR1. We further identified that K228 is the major acetylation site for PYCR1. Acetylation of PYCR1 at K228 reduced its enzymatic activity by impairing the formation of the decamer of PYCR1. As a result, acetylation of PYCR1 at K228 inhibits cell proliferation, while deacetylation of PYCR1 mediated by SIRT3 increases PYCR1’s activity. Our findings on the regulation of PYCR1 linked proline metabolism with SIRT3, CBP and cell growth, thus providing a potential approach for cancer therapy. SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to proline with concomitant generation of NAD+ and NADP+. PYCR1 is highly expressed in various cancers, and it can promote the growth of tumor cells. Here, through immunoprecipitation and mass spectrometry, we found that PYCR1 is in SIRT3's interacting network. PYCR1 directly binds to SIRT3 both in vivo and in vitro. CBP is the acetyltransferase for PYCR1, whereas SIRT3 deacetylates PYCR1. We further identified that K228 is the major acetylation site for PYCR1. Acetylation of PYCR1 at K228 reduced its enzymatic activity by impairing the formation of the decamer of PYCR1. As a result, acetylation of PYCR1 at K228 inhibits cell proliferation, while deacetylation of PYCR1 mediated by SIRT3 increases PYCR1's activity. Our findings on the regulation of PYCR1 linked proline metabolism with SIRT3, CBP and cell growth, thus providing a potential approach for cancer therapy.SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to proline with concomitant generation of NAD+ and NADP+. PYCR1 is highly expressed in various cancers, and it can promote the growth of tumor cells. Here, through immunoprecipitation and mass spectrometry, we found that PYCR1 is in SIRT3's interacting network. PYCR1 directly binds to SIRT3 both in vivo and in vitro. CBP is the acetyltransferase for PYCR1, whereas SIRT3 deacetylates PYCR1. We further identified that K228 is the major acetylation site for PYCR1. Acetylation of PYCR1 at K228 reduced its enzymatic activity by impairing the formation of the decamer of PYCR1. As a result, acetylation of PYCR1 at K228 inhibits cell proliferation, while deacetylation of PYCR1 mediated by SIRT3 increases PYCR1's activity. Our findings on the regulation of PYCR1 linked proline metabolism with SIRT3, CBP and cell growth, thus providing a potential approach for cancer therapy. SIRT3 is a major mitochondrial deacetylase, which regulates various metabolic pathways by deacetylation; however, the effect of SIRT3 on proline metabolism is not reported. Pyrroline-5-carboxylate reductase 1 (PYCR1) participates in proline synthesis process by catalyzing the reduction of P5C to proline with concomitant generation of NAD and NADP . PYCR1 is highly expressed in various cancers, and it can promote the growth of tumor cells. Here, through immunoprecipitation and mass spectrometry, we found that PYCR1 is in SIRT3's interacting network. PYCR1 directly binds to SIRT3 both in vivo and in vitro. CBP is the acetyltransferase for PYCR1, whereas SIRT3 deacetylates PYCR1. We further identified that K228 is the major acetylation site for PYCR1. Acetylation of PYCR1 at K228 reduced its enzymatic activity by impairing the formation of the decamer of PYCR1. As a result, acetylation of PYCR1 at K228 inhibits cell proliferation, while deacetylation of PYCR1 mediated by SIRT3 increases PYCR1's activity. Our findings on the regulation of PYCR1 linked proline metabolism with SIRT3, CBP and cell growth, thus providing a potential approach for cancer therapy. |
| Author | Wang, Zhe Yang, Xin Yu, Miao Qi, Hao Zou, Junhua Luo, Jianyuan Ren, Mengmeng Chen, Shuaiyi Liu, Minghui Liu, Boya Vucenik, Ivana Liu, Lu Zhu, Wei-Guo |
| Author_xml | – sequence: 1 givenname: Shuaiyi surname: Chen fullname: Chen, Shuaiyi organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 2 givenname: Xin surname: Yang fullname: Yang, Xin organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 3 givenname: Miao surname: Yu fullname: Yu, Miao organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 4 givenname: Zhe surname: Wang fullname: Wang, Zhe organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 5 givenname: Boya surname: Liu fullname: Liu, Boya organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 6 givenname: Minghui surname: Liu fullname: Liu, Minghui organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 7 givenname: Lu surname: Liu fullname: Liu, Lu organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 8 givenname: Mengmeng surname: Ren fullname: Ren, Mengmeng organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 9 givenname: Hao surname: Qi fullname: Qi, Hao organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 10 givenname: Junhua surname: Zou fullname: Zou, Junhua organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China – sequence: 11 givenname: Ivana surname: Vucenik fullname: Vucenik, Ivana organization: Department of Medical and Research Technology, University of Maryland, Baltimore, MD 21201, USA – sequence: 12 givenname: Wei-Guo surname: Zhu fullname: Zhu, Wei-Guo organization: Department of Biochemistry and Molecular Biology, Shenzhen University School of Medicine, Shenzhen, 518060, China – sequence: 13 givenname: Jianyuan surname: Luo fullname: Luo, Jianyuan email: luojianyuan@bjmu.edu.cn organization: Department of Medical Genetics, Peking University Health Science Center, Beijing, 100191, China |
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