Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)
Sirtuins are mammalian homologs of yeast silent information regulator two (SIRT) and are a highly conserved family of proteins, which act as nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. The seven sirtuins (SIRT 1-7) share a conserved catalytic core domain; however, they h...
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| Veröffentlicht in: | Oncology letters 2020-10, Vol.20 (4), p.1-11 |
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| creator | Wang, Changming Liu, Yan Zhu, Yuyan Kong, Chutze |
| description | Sirtuins are mammalian homologs of yeast silent information regulator two (SIRT) and are a highly conserved family of proteins, which act as nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. The seven sirtuins (SIRT 1-7) share a conserved catalytic core domain; however, they have different enzyme activities, biological functions, and subcellular localizations. Among them, mitochondrial SIRT4 possesses ADP-ribosyltransferase, NAD+-dependent deacetylase, lipoamidase, and long-chain deacylase activities and can modulate the function of substrate proteins via ADP-ribosylation, delipoylation, deacetylation and long-chain deacylation. SIRT4 has been shown to play a crucial role in insulin secretion, fatty acid oxidation, amino acid metabolism, ATP homeostasis, apoptosis, neurodegeneration, and cardiovascular diseases. In addition, recent studies have demonstrated that SIRT4 acts as a tumor suppressor. Here, the present review summarizes the enzymatic activities and biological functions of SIRT4, as well as its roles in cellular metabolism and human cancer, which are described in the current literature. |
| doi_str_mv | 10.3892/ol.2020.11872 |
| format | Article |
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The seven sirtuins (SIRT 1-7) share a conserved catalytic core domain; however, they have different enzyme activities, biological functions, and subcellular localizations. Among them, mitochondrial SIRT4 possesses ADP-ribosyltransferase, NAD+-dependent deacetylase, lipoamidase, and long-chain deacylase activities and can modulate the function of substrate proteins via ADP-ribosylation, delipoylation, deacetylation and long-chain deacylation. SIRT4 has been shown to play a crucial role in insulin secretion, fatty acid oxidation, amino acid metabolism, ATP homeostasis, apoptosis, neurodegeneration, and cardiovascular diseases. In addition, recent studies have demonstrated that SIRT4 acts as a tumor suppressor. Here, the present review summarizes the enzymatic activities and biological functions of SIRT4, as well as its roles in cellular metabolism and human cancer, which are described in the current literature.</description><identifier>ISSN: 1792-1074</identifier><identifier>EISSN: 1792-1082</identifier><identifier>DOI: 10.3892/ol.2020.11872</identifier><identifier>PMID: 32774484</identifier><language>eng</language><publisher>Athens: Spandidos Publications</publisher><subject>Amino acids ; Binding sites ; Cancer ; Cancer research ; Cell cycle ; Enzymes ; Fatty acids ; Homeostasis ; Insulin ; Kinases ; Mammals ; Metabolism ; Metabolites ; Mitochondria ; Niacinamide ; Oncology ; Physiological aspects ; Physiology ; Proteins ; Review ; Tumorigenesis</subject><ispartof>Oncology letters, 2020-10, Vol.20 (4), p.1-11</ispartof><rights>COPYRIGHT 2020 Spandidos Publications</rights><rights>Copyright Spandidos Publications UK Ltd. 2020</rights><rights>Copyright: © Wang et al. 2020</rights><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-79d67ff2ef682c806301c2987b664c16ed1449127b5be1d8d603384e1045ebe53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7405384/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7405384/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids></links><search><creatorcontrib>Wang, Changming</creatorcontrib><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Zhu, Yuyan</creatorcontrib><creatorcontrib>Kong, Chutze</creatorcontrib><title>Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)</title><title>Oncology letters</title><description>Sirtuins are mammalian homologs of yeast silent information regulator two (SIRT) and are a highly conserved family of proteins, which act as nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. The seven sirtuins (SIRT 1-7) share a conserved catalytic core domain; however, they have different enzyme activities, biological functions, and subcellular localizations. Among them, mitochondrial SIRT4 possesses ADP-ribosyltransferase, NAD+-dependent deacetylase, lipoamidase, and long-chain deacylase activities and can modulate the function of substrate proteins via ADP-ribosylation, delipoylation, deacetylation and long-chain deacylation. SIRT4 has been shown to play a crucial role in insulin secretion, fatty acid oxidation, amino acid metabolism, ATP homeostasis, apoptosis, neurodegeneration, and cardiovascular diseases. In addition, recent studies have demonstrated that SIRT4 acts as a tumor suppressor. Here, the present review summarizes the enzymatic activities and biological functions of SIRT4, as well as its roles in cellular metabolism and human cancer, which are described in the current literature.</description><subject>Amino acids</subject><subject>Binding sites</subject><subject>Cancer</subject><subject>Cancer research</subject><subject>Cell cycle</subject><subject>Enzymes</subject><subject>Fatty acids</subject><subject>Homeostasis</subject><subject>Insulin</subject><subject>Kinases</subject><subject>Mammals</subject><subject>Metabolism</subject><subject>Metabolites</subject><subject>Mitochondria</subject><subject>Niacinamide</subject><subject>Oncology</subject><subject>Physiological aspects</subject><subject>Physiology</subject><subject>Proteins</subject><subject>Review</subject><subject>Tumorigenesis</subject><issn>1792-1074</issn><issn>1792-1082</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNptkstr3DAQh01paUKaY--GQkkP3uplSb4UQmgeECik6VnI8nitoMdWshP631dOQtotlQ4aSd_8NDOaqnqP0YbKjnyObkMQQRuMpSCvqkMsOtJgJMnrF1uwg-o45ztURsuxlPxtdUCJEIxJdlj150sws40h13GsvfZeO6tD_f3q5pbVNtQGnFucTrWHWffR2exrHYY6QQadzFTvUtyWTV7hafHF1-hgINUnN3Bv4eHTu-rNqF2G4-f1qPpx_vX27LK5_nZxdXZ63Zi25XMjuoGLcSQwckmMRJwibEgnRc85M5jDgBnrMBF92wMe5MARpZIBRqyFHlp6VH150t0tvYfBQJiTdmqXrNfpl4raqv2bYCe1jfdKMNQWpSJw8iyQ4s8F8qy8zWv-OkBcsiKMEsl5iaGgH_5B7-KSQklvpQTlpfjiD7XVDpQNYyzvmlVUnXLaMlTk1rg3_6HKHMBbEwOMtpzvOXz8y2EC7eYpR7c8fuM-2DyBJsWcE4wvxcBIrQ2kolNrA6nHBqK_AW-Qs-8</recordid><startdate>20201001</startdate><enddate>20201001</enddate><creator>Wang, Changming</creator><creator>Liu, Yan</creator><creator>Zhu, Yuyan</creator><creator>Kong, Chutze</creator><general>Spandidos Publications</general><general>Spandidos Publications UK Ltd</general><general>D.A. Spandidos</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AN0</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>M0S</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20201001</creationdate><title>Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)</title><author>Wang, Changming ; Liu, Yan ; Zhu, Yuyan ; Kong, Chutze</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-79d67ff2ef682c806301c2987b664c16ed1449127b5be1d8d603384e1045ebe53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Amino acids</topic><topic>Binding sites</topic><topic>Cancer</topic><topic>Cancer research</topic><topic>Cell cycle</topic><topic>Enzymes</topic><topic>Fatty acids</topic><topic>Homeostasis</topic><topic>Insulin</topic><topic>Kinases</topic><topic>Mammals</topic><topic>Metabolism</topic><topic>Metabolites</topic><topic>Mitochondria</topic><topic>Niacinamide</topic><topic>Oncology</topic><topic>Physiological aspects</topic><topic>Physiology</topic><topic>Proteins</topic><topic>Review</topic><topic>Tumorigenesis</topic><toplevel>online_resources</toplevel><creatorcontrib>Wang, Changming</creatorcontrib><creatorcontrib>Liu, Yan</creatorcontrib><creatorcontrib>Zhu, Yuyan</creatorcontrib><creatorcontrib>Kong, Chutze</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>British Nursing Database</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Oncology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Changming</au><au>Liu, Yan</au><au>Zhu, Yuyan</au><au>Kong, Chutze</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review)</atitle><jtitle>Oncology letters</jtitle><date>2020-10-01</date><risdate>2020</risdate><volume>20</volume><issue>4</issue><spage>1</spage><epage>11</epage><pages>1-11</pages><issn>1792-1074</issn><eissn>1792-1082</eissn><abstract>Sirtuins are mammalian homologs of yeast silent information regulator two (SIRT) and are a highly conserved family of proteins, which act as nicotinamide adenine dinucleotide (NAD+)-dependent histone deacetylases. The seven sirtuins (SIRT 1-7) share a conserved catalytic core domain; however, they have different enzyme activities, biological functions, and subcellular localizations. Among them, mitochondrial SIRT4 possesses ADP-ribosyltransferase, NAD+-dependent deacetylase, lipoamidase, and long-chain deacylase activities and can modulate the function of substrate proteins via ADP-ribosylation, delipoylation, deacetylation and long-chain deacylation. SIRT4 has been shown to play a crucial role in insulin secretion, fatty acid oxidation, amino acid metabolism, ATP homeostasis, apoptosis, neurodegeneration, and cardiovascular diseases. In addition, recent studies have demonstrated that SIRT4 acts as a tumor suppressor. 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| source | Spandidos Publications Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino acids Binding sites Cancer Cancer research Cell cycle Enzymes Fatty acids Homeostasis Insulin Kinases Mammals Metabolism Metabolites Mitochondria Niacinamide Oncology Physiological aspects Physiology Proteins Review Tumorigenesis |
| title | Functions of mammalian SIRT4 in cellular metabolism and research progress in human cancer (Review) |
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