General Information:
Id: | 6,387 (click here to show other Interactions for entry) |
Diseases: |
Metabolic
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Mammalia | |
review | |
Reference: | Cetrullo S et al.(2015) mTOR, AMPK, and Sirt1: Key Players in Metabolic Stress Management Crit. Rev. Eukaryot. Gene Expr. 25: 59-75 [PMID: 25955819] |
Interaction Information:
Comment | Sir2 hast seven orthologs (Sirt1-Sirt7) in mammals that are ubiquitously expressed in tissues and have different subcellular localizations and activities. While Sirt1, Sirt6, and Sirt7 lie mainly in the nucleus, Sirt3, Sirt4, and Sirt5 are mitochondrial protein and Sirt2 is found to act in the cytoplasm. |
Formal Description Interaction-ID: 61567 |
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Comment | The NAD+ biosynthetic rate is crucial in Sirt1 regulation. Only in the presence of the cosubstrate NAD+ does the reaction lead to removal of actyl groups from an acetylated substrate, releasing nicotinamide, 2'-O-acetyl-ADP-ribose and the deacetylated target (e.g. histonic lysines). |
Formal Description Interaction-ID: 61617 |
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Comment | Two studies have reported an interaction between Sirt1 and CLOCK-BMAL1, joint master regulators of the circadian clock, which implies that Sirt1 is the molcular link among several cellular processes, playing a regulatory role in the circadian clock, aging, cellular metabolism, and stress response. These different processes are characterized by changes in NAD+ levels and in turn influence Sirt1 activity in a fine and detailed circuit. |
Formal Description Interaction-ID: 61621 |
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Comment | It has been shown that NAD+ increases in mammals during exercise, fasting, and caloric restriction, and the same conditions are associated with intensive Sirt1 activity. |
Formal Description Interaction-ID: 61624 |
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Comment | It has been shown that NAD+ increases in mammals during exercise, fasting, and caloric restriction, and the same conditions are associated with intensive Sirt1 activity. |
Formal Description Interaction-ID: 61625 |
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Comment | It has been shown that NAD+ increases in mammals during exercise, fasting, and caloric restriction, and the same conditions are associated with intensive Sirt1 activity. |
Formal Description Interaction-ID: 61626 |
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Comment | Two studies have reported an interaction between Sirt1 and CLOCK-BMAL1, joint master regulators of the circadian clock, which implies that Sirt1 is the molecular link among several cellular processes, playing a regulatory role in the circadian clock, aging, cellular metabolism, and stress response. These different processes are characterized by changes in NAD+ levels and in turn influence Sirt1 activity in a fine and detailed circuit. |
Formal Description Interaction-ID: 61630 |
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Comment | Several signals converge on Sirt1 to stimulate its protein deacetylase activity, which uses NAD+ as a cosubstrate and releases acetyl-ADP-ribose and nicotinamide (NAM). |
Formal Description Interaction-ID: 61631 |
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Comment | Several signals converge on Sirt1 to stimulate its protein deacetylase activity, which uses NAD+ as a cosubstrate and releases acetyl-ADP-ribose and nicotinamide (NAM). |
Formal Description Interaction-ID: 61632 |
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Drugbank entries | Show/Hide entries for |
Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61635 |
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Drugbank entries | Show/Hide entries for TP53 |
Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61641 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61642 |
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Drugbank entries | Show/Hide entries for HIF1A |
Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61643 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61644 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61645 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61646 |
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Drugbank entries | Show/Hide entries for NR1H4 |
Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61647 |
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Drugbank entries | Show/Hide entries for NFKB1 |
Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61648 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61649 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61650 |
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Comment | Substrates / targets of Sirt1 are p53, PGC-1alpha, HIF1a and HIF2a, LXR (liver X receptor), SREB-Ps, FXR (farnesoid X receptor), NF-kappaB, PER2 (period circadian protein homolog 2), CRTC2 (CREB-regulated transcription coactivator 2), E2F1, and KU70. |
Formal Description Interaction-ID: 61651 |
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Comment | Resveratrol cannot stimulate Sirt1 activity without a functional AMPK. It is proposed that Sirt1 is a downstream AMPK effector. |
Formal Description Interaction-ID: 61652 |
drug/chemical compound increases_activity of gene/protein |
Drugbank entries | Show/Hide entries for Resveratrol |
Comment | Hydroxytyrosol, a molecule mainly derived from olives, increases Sirt1 expression. |
Formal Description Interaction-ID: 61653 |
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Comment | Sirt1 interacts with and deacetylates FoxO transcription factors. |
Formal Description Interaction-ID: 61654 |
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Comment | Sirt1 interacts with and deacetylates FoxO transcription factors. |
Formal Description Interaction-ID: 61655 |
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Comment | Sirt1 may be involved in autophagy by deacetylating Atg5, Atg7, and Atg8. |
Formal Description Interaction-ID: 61656 |
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Comment | Sirt1 may be involved in autophagy by deacetylating Atg5, Atg7, and Atg8. |
Formal Description Interaction-ID: 61657 |
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Comment | Sirt1 may be involved in autophagy by deacetylating Atg5, Atg7, and Atg8. |
Formal Description Interaction-ID: 61658 |
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Comment | It has been demonstrated that AMPK does not directly phosphorylate SIRT1, but the effect of this kinase on lipid oxidation is to modify the NAD+/NADH ratio, thus modulating SIRT1 deacetylase activity. Some evidence indicates that the expression of Nampt (Nicotinamide phosphoribosyl-transferase), which is involved in the synthesis of NAD+ by the NAD+ salvage pathway, is induced by AMPK. |
Formal Description Interaction-ID: 61674 |
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Comment | LKB1, upstream of AMPK activation, is target of Sirt1, which may regulate its acetylation status, intracellular localization, and activity. |
Formal Description Interaction-ID: 61676 |
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Comment | SIRT1 overexpression in neurons is associated with a reduction in mTOR protein levels and activity, thus providing a new SIRT1 negative modulation of mTOR signaling. |
Formal Description Interaction-ID: 61677 |
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Drugbank entries | Show/Hide entries for MTOR |
Comment | SIRT1 overexpression in neurons is associated with a reduction in mTOR protein levels and activity, thus providing a new SIRT1 negative modulation of mTOR signaling. |
Formal Description Interaction-ID: 61679 |
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Drugbank entries | Show/Hide entries for MTOR |
Comment | SIRT1 overexpression in neurons is associated with a reduction in mTOR protein levels and activity, thus providing a new SIRT1 negative modulation of mTOR signaling. |
Formal Description Interaction-ID: 61680 |
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