Oliver's mTOR Atlas Evidence Platform
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Pathway link ULK1-FNIP1

ULK1 FLCN / FNIP1/2

ULK1 inhibits FLCN / FNIP1/2.

ULK1 tags FNIP1, which turns FLCN off and lets TFEB escape mTORC1's grip.

When lysosomes are stressed, ULK1 (or its relative TBK1) phosphorylates FNIP1 at S296 on the lysosome. This switches the FLCN-FNIP complex off, so mTORC1 can no longer hold TFEB in the cytoplasm and TFEB moves into the nucleus.

The conditions it holds under

Human cell lines and ATP6V1B2-mutant follicular lymphoma samples; a nutrient-independent lysosomal-stress route, and TBK1 can substitute for ULK1. Single study.

Time it takes
minutes
Step
direct (one molecule acts on the other)
Measured in
human cells
Where in the cell
lysosome
Reaches people?
plausible in people, not shown directly
How settled
emerging, few independent studies

Studies behind it

YearEvidenceStudy
2026 M A TBK1/ULK1 signalling axis couples lysosomal stress to TFEB activation.ESP2026 Identifies a nutrient-independent lysosomal pathway in which v-ATPase recruits TBK1/ULK1 to phosphorylate FNIP1, inhibiting the FLCN:FNIP complex and releasing TFEB for nuclear translocation; recurrent ATP6V1B2 mutations found in follicular lymphoma patients constitutively hyperactivate this axis, driving TFEB-dependent tumor proliferation.

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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