Oliver's mTOR Atlas Evidence Platform
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Pathway link SIN1-MTORC2

SIN1 / MAPKAP1 mTORC2

SIN1 / MAPKAP1 required-for mTORC2.

SIN1 holds mTORC2 together and positions its target – without it, mTORC2 can't switch Akt on.

SIN1 holds the complex together and positions the substrate; without it mTORC2 cannot phosphorylate Akt.

The conditions it holds under

Mammalian cell studies and a cryo-EM structure (JAC2006, FRI2006, YAN2006, STU2018). Cell and structural evidence; not tested in people by these sources.

Time it takes
always on
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
2006 M SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificityJAC2006 SIN1 maintains rictor-mTOR integrity and confers mTORC2 Akt-Ser473 kinase activity and substrate specificity.
2006 M mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2sFRI2006 mSin1 is required for mTORC2 assembly and Akt Ser473 phosphorylation; isoforms define distinct complexes.
2006 M Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activityYAN2006 Identified Sin1 as an essential TORC2 component required for Akt phosphorylation.
2018 M Architecture of the human mTORC2 core complexSTU2018 Architecture of the human mTORC2 core complex (mTOR-Rictor-SIN1-mLST8).

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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