Oliver's mTOR Atlas Evidence Platform
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Pathway link MTORC1-ULK1

mTORC1 ULK1

mTORC1 inhibits ULK1.

Active mTORC1 tags ULK1 to hold it back, keeping the cell's self-cleanup process (autophagy) switched off while nutrients are plentiful.

Active mTORC1 phosphorylates ULK1 at an inhibitory site, holding autophagy shut while nutrients are plentiful.

The conditions it holds under

Mammalian and human/mouse cell studies (HOS2009, GAN2009, KIM2011, NAZ2013). Cell-culture biochemistry; the whole-animal and human consequence is not shown by these sources.

Time it takes
minutes
Step
direct (one molecule acts on the other)
Measured in
mammalian cells
Where in the cell
cytosol
Reaches people?
plausible in people, not shown directly
How settled
settled in the literature

Studies behind it

YearEvidenceStudy
2009 M Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagyHOS2009 Showed the DIRECT brake mTORC1 uses on autophagy: when nutrients are plentiful, mTORC1 physically joins the ULK1-Atg13-FIP200 complex (the autophagy-starter kinase) and phosphorylates ULK1 to keep it off. Starvation or rapamycin releases this brake and autophagy begins.
2009 M ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential for autophagyGAN2009 The ULK1-ATG13-FIP200 complex transmits mTOR signalling to initiate autophagy.
2011 M AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1KIM2011 Revealed the tug-of-war over ULK1: the energy sensor AMPK phosphorylates ULK1 at activating sites to turn autophagy ON when energy is low, while mTORC1 phosphorylates a different site (Ser757) to keep it OFF and even blocks AMPK from reaching ULK1. Two opposing kinases wired to the same switch.
2013 M mTOR inhibits autophagy by controlling ULK1 ubiquitylation, self-association and function through AMBRA1 and TRAF6NAZ2013 mTOR restrains autophagy by controlling ULK1 ubiquitylation and stability via AMBRA1/TRAF6.

Points the other way

No study in the Atlas contradicts this link. That means none in this curated set, not none in the literature.

Who has checked this

Checked by
No researcher outside the project has checked this link yet.
Curator sign-off
Not signed off yet. This link was drafted with AI help and has not been reviewed link by link; treat it as a proposal until it is.
Curated by
Oliver Barton, with AI help for drafting; see how links are checked.

“Inhibits” describes the effect on the target's activity, not on how much of it there is.

“How settled” describes how far researchers in the field agree. It is not the same as the sign-off above, which only says whether a named curator has checked this page.

If this link rests on your own work: a click on “This looks right” below, or a short note through “Report an error”, helps us more than anything else on this page.

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