Oliver's mTOR Atlas Evidence Platform
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Pathway link MTOR-MTORC2

mTOR mTORC2

mTOR required-for mTORC2.

mTORC2 is built from the very same mTOR enzyme as mTORC1 – it's the partner proteins around it that make the two complexes different.

mTORC2 is built around the same mTOR kinase as mTORC1 - the partner subunits, not the catalytic core, are what make the two complexes different.

The conditions it holds under

Cryo-EM structures of the complex from human cells and yeast (CHE2018, SCA2020, STU2018, KAR2017). Structural evidence shows how the complex is built, not how often or where it forms in living tissue.

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

Studies behind it

YearEvidenceStudy
2018 M Cryo-EM structure of human mTOR complex 2CHE2018 Cryo-EM structure of human mTORC2 defines its subunit organization and substrate access.
2020 M The 3.2-Å resolution structure of human mTORC2.SCA2020 The 3.2 A cryo-EM structure of human mTORC2 pinpoints Rictor's C-terminus as the source of rapamycin insensitivity.
2018 M Architecture of the human mTORC2 core complexSTU2018 Architecture of the human mTORC2 core complex (mTOR-Rictor-SIN1-mLST8).
2017 M Cryo-EM structure of Saccharomyces cerevisiae target of rapamycin complex 2KAR2017 Cryo-EM structure of yeast TORC2 reveals its overall architecture and rapamycin insensitivity.

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.

“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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