Oliver's mTOR Atlas Evidence Platform
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Pathway link GRB10-IGF1

Grb10 Growth hormone / IGF-1 axis

Grb10 inhibits Growth hormone / IGF-1 axis.

Grb10 dampens insulin/IGF-1 signalling – which is why blocking mTOR can paradoxically make Akt more active.

Stabilised Grb10 damps insulin/IGF-1 receptor signalling. This is one of two feedback arms behind the paradox that blocking mTORC1 raises Akt activity; the other is the S6K1-IRS-1 loop.

The conditions it holds under

Two mammalian cell studies (HSU2011, YUX2011). The feedback is shown in cultured cells. Its size in living tissue and in people, and how it compares with the S6K1-IRS-1 loop, are not measured.

Time it takes
hours
Step
indirect (through steps not drawn here)
Measured in
mammalian cells
Where in the cell
plasma membrane
Reaches people?
plausible in people, not shown directly
How settled
settled in the literature

Studies behind it

YearEvidenceStudy
2011 M The mTOR-regulated phosphoproteome reveals a mechanism of mTORC1-mediated inhibition of growth factor signalingHSU2011 mTOR-dependent phosphoproteomics reveal Grb10 as a substrate mediating feedback inhibition of PI3K.
2011 M Phosphoproteomic analysis identifies Grb10 as an mTORC1 substrate that negatively regulates insulin signalingYUX2011 Phosphoproteomics identify Grb10 as an mTORC1 substrate driving negative feedback on insulin/PI3K.

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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