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Appears in Networks 3

In-Edges 11

a(CHEBI:"AICA ribonucleotide") increases act(p(FPLX:AMPK)) View Subject | View Object

The aminoimidazole derivative 5-aminoimidazole- 4-carboxamide ribonucleotide (AICAR) undergoes intra- cellular transformation to an AMP analogue that triggers AMPK-mediated autophagy 21,108 . PubMed:30116051

a(CHEBI:"alpha,alpha-trehalose") increases act(p(FPLX:AMPK)) View Subject | View Object

The di-glucose derivative trehalose inhibits the sol- ute carrier 2A (SLC2A) family of glucose transporters to promote AMPK-induced autophagy and reduce neurotoxic protein load, although it also exerts other actions downstream in the ALN 4,120 . PubMed:30116051

a(CHEBI:"amyloid-beta polypeptide 42") decreases act(p(FPLX:AMPK)) View Subject | View Object

Sixth, Aβ42 compro- mises the function of AMPK to impede initiation of the ALN 67 . PubMed:30116051

a(CHEBI:"methylene blue") increases act(p(FPLX:AMPK)) View Subject | View Object

Other compounds that act through AMPK acti- vation include the antiaggregant methylene blue (Supplementary Box 1), which elevated levels of beclin  1, p62 and LC3, induced autophagy and suppressed tau in organotypic neuronal cultures and a mouse model of FTD 101,102 . PubMed:30116051

a(CHEBI:calcitriol) increases act(p(FPLX:AMPK)) View Subject | View Object

In addition, calcitriol (the active metabolite of vitamin D 3 ) elicited AMPK-dependent autophagy in a neurochemical lesion-induced model of PD 129. PubMed:30116051

a(CHEBI:metformin) increases act(p(FPLX:AMPK)) View Subject | View Object

The antidiabetic drug metformin, a prototypical activator of AMPK, induced autophagy and increased longevity in mice 116 . PubMed:30116051

a(CHEBI:resveratrol) increases act(p(FPLX:AMPK)) View Subject | View Object

Resveratrol can stimulate SIRT1 via AMPK (see above), and it also possesses an AMPK-independent mode of SIRT1 recruitment that participates in blunting the neurotoxicity of Aβ25–35 fragments in PC12 cells 160 . PubMed:30116051

a(CHEBI:selenomethionine) increases act(p(FPLX:AMPK)) View Subject | View Object

Selenium deficits have been linked to AD, and thus it is interesting that seleno- methionine boosted ALN flux, from AMPK recruit- ment through autophagosome formation to lysosomal degradation, in the 3×Tg AD mouse model 112 . PubMed:30116051

a(PUBCHEM:54708532) increases act(p(FPLX:AMPK)) View Subject | View Object

Another direct facilitator of AMPK, A769662, elicited autophagy and reduced the burden of Htt in a striatal cell line derived from knock-in mice expressing a humanized form of mutant Htt (exon 1 containing seven polyglutamine repeats) 111 . PubMed:30116051

p(HGNC:SESN2) increases act(p(FPLX:AMPK)) View Subject | View Object

Supporting the relevance of sestrin 2, it has been shown to protect dopaminergic neurons from the neurotoxin rotenone via AMPK-transduced autophagy 247 . PubMed:30116051

Out-Edges 15

p(FPLX:AMPK) increases bp(GO:macroautophagy) View Subject | View Object

The heterotrimeric serine/threonine kinase 5ʹ‑AMP‑ activated protein kinase (AMPK) and mammalian target of rapamycin complex 1 (mTORC1) trigger autophagy and repress mitophagy 3,10,20–23 (BOX 2; FIG. 3) . PubMed:30116051

p(FPLX:AMPK) decreases bp(GO:mitophagy) View Subject | View Object

The heterotrimeric serine/threonine kinase 5ʹ‑AMP‑ activated protein kinase (AMPK) and mammalian target of rapamycin complex 1 (mTORC1) trigger autophagy and repress mitophagy 3,10,20–23 (BOX 2; FIG. 3) . PubMed:30116051

p(FPLX:AMPK) increases p(HGNC:ULK1, pmod(Ph, Ser, 317)) View Subject | View Object

AMPK is central to several mechanisms that trigger autophagy — most importantly, activating phosphoryla- tion of ULK1 (Ser317 and Ser777) and inhibitory phos- phorylation of mTORC1 (REFS21,31) . PubMed:30116051

p(FPLX:AMPK) increases p(HGNC:ULK1, pmod(Ph, Ser, 777)) View Subject | View Object

AMPK is central to several mechanisms that trigger autophagy — most importantly, activating phosphoryla- tion of ULK1 (Ser317 and Ser777) and inhibitory phos- phorylation of mTORC1 (REFS21,31) . PubMed:30116051

p(FPLX:AMPK) increases p(FPLX:mTORC1, pmod(Ph)) View Subject | View Object

AMPK is central to several mechanisms that trigger autophagy — most importantly, activating phosphoryla- tion of ULK1 (Ser317 and Ser777) and inhibitory phos- phorylation of mTORC1 (REFS21,31) . PubMed:30116051

p(FPLX:AMPK) increases a(CHEBI:"NAD(+)") View Subject | View Object

SIRT1 is activated by AMPK- mediated increases in nicotinamide, and it drives the ALN by inhibiting mTORC1, inducing FOXO1 and FOXO3 and activating key regulatory proteins such as ATG5, ATG7 and LC3. PubMed:30116051

act(p(FPLX:AMPK)) increases bp(GO:autophagy) View Subject | View Object

The aminoimidazole derivative 5-aminoimidazole- 4-carboxamide ribonucleotide (AICAR) undergoes intra- cellular transformation to an AMP analogue that triggers AMPK-mediated autophagy 21,108 . PubMed:30116051

act(p(FPLX:AMPK)) increases bp(GO:autophagy) View Subject | View Object

The di-glucose derivative trehalose inhibits the sol- ute carrier 2A (SLC2A) family of glucose transporters to promote AMPK-induced autophagy and reduce neurotoxic protein load, although it also exerts other actions downstream in the ALN 4,120 . PubMed:30116051

act(p(FPLX:AMPK)) increases act(p(HGNC:SIRT1)) View Subject | View Object

Resveratrol can stimulate SIRT1 via AMPK (see above), and it also possesses an AMPK-independent mode of SIRT1 recruitment that participates in blunting the neurotoxicity of Aβ25–35 fragments in PC12 cells 160 . PubMed:30116051

p(FPLX:AMPK) increases bp(GO:autophagy) View Subject | View Object

The mammalian target of rapamycin (mTOR) kinase negatively modulates autophagy by phosphorylating Atg1, an autophagy initiating factor, while adenosine monophosphate-activated protein kinase (AMPK), a major sensor for the cellular energy status, activates autophagy through inhibiting mTOR signaling as well as by direct phosphorylation of Atg1 (Egan et al., 2011; Kim et al., 2011). Increased mTOR activity results in autophagy downregulation and tau accumulation. PubMed:23528736

p(FPLX:AMPK) decreases act(p(FPLX:mTORC1)) View Subject | View Object

The mammalian target of rapamycin (mTOR) kinase negatively modulates autophagy by phosphorylating Atg1, an autophagy initiating factor, while adenosine monophosphate-activated protein kinase (AMPK), a major sensor for the cellular energy status, activates autophagy through inhibiting mTOR signaling as well as by direct phosphorylation of Atg1 (Egan et al., 2011; Kim et al., 2011). Increased mTOR activity results in autophagy downregulation and tau accumulation. PubMed:23528736

p(FPLX:AMPK) increases p(HGNC:ULK1, pmod(Ph)) View Subject | View Object

The mammalian target of rapamycin (mTOR) kinase negatively modulates autophagy by phosphorylating Atg1, an autophagy initiating factor, while adenosine monophosphate-activated protein kinase (AMPK), a major sensor for the cellular energy status, activates autophagy through inhibiting mTOR signaling as well as by direct phosphorylation of Atg1 (Egan et al., 2011; Kim et al., 2011). Increased mTOR activity results in autophagy downregulation and tau accumulation. PubMed:23528736

p(FPLX:AMPK) increases p(HGNC:ULK1, pmod(Ph)) View Subject | View Object

For instance, adenosine monophosphate- activated protein kinase (AMPK) phosphorylates ULK1 and inactivates mTOR through the raptor and tuberous sclerosis complex (TSC2). PubMed:29758300

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BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.