The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1

Oshiro N, Takahashi R, Yoshino K, Tanimura K, Nakashima A, Eguchi S, Miyamoto T, Hara K, Takehana K, Avruch J, Kikkawa U, Yonezawa K · 2007 · The Journal of biological chemistry · Atlas ID OSH2007

What this study shows

PRAS40 is a physiological raptor-bound substrate and inhibitor of mTORC1.

Abstract

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The proline-rich Akt substrate of 40 kilodaltons (PRAS40) was identified as a raptor-binding protein that is phosphorylated directly by mammalian target of rapamycin (mTOR) complex 1 (mTORC1) but not mTORC2 in vitro, predominantly at PRAS40 (Ser(183)). The binding of S6K1 and 4E-BP1 to raptor requires a TOR signaling (TOS) motif, which contains an essential Phe followed by four alternating acidic and small hydrophobic amino acids. PRAS40 binding to raptor was severely inhibited by mutation of PRAS40 (Phe(129) to Ala).

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At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Mammalian cells) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Mammalian cells
Journal	The Journal of biological chemistry
Year	2007
Peer reviewed	Yes
Record last updated	2026-10-01
Source	DOI 10.1074/jbc.M702636200 · PMID 17517883 · Free full text (PMC3199301)

Extracted findings

These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.

Intervention	Biochemical (PRAS40)
Target	mTORC1 / PRAS40
Model	Mammalian cells
Effect	PRAS40 is a raptor-binding physiological mTORC1 substrate (phosphorylated at Ser183)

In the Atlas

Links in the pathway map

Supports Akt/PKB inhibits PRAS40

Cite this paper

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Oshiro, N., Takahashi, R., Yoshino, K., Tanimura, K., Nakashima, A., Eguchi, S., Miyamoto, T., Hara, K., Takehana, K., Avruch, J., Kikkawa, U., & Yonezawa, K. (2007). The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1. The Journal of biological chemistry. https://doi.org/10.1074/jbc.M702636200

@article{OSH2007,
  author       = {Oshiro, N. and Takahashi, R. and Yoshino, K. and Tanimura, K. and Nakashima, A. and Eguchi, S. and Miyamoto, T. and Hara, K. and Takehana, K. and Avruch, J. and Kikkawa, U. and Yonezawa, K.},
  title        = {{The proline-rich Akt substrate of 40 kDa (PRAS40) is a physiological substrate of mammalian target of rapamycin complex 1}},
  journal      = {The Journal of biological chemistry},
  year         = {2007},
  doi          = {10.1074/jbc.M702636200},
  note         = {PMID: 17517883},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record OSH2007) [Data set]. https://mtor-atlas.org/study/OSH2007/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_OSH2007,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record OSH2007},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/OSH2007/},
  doi          = {10.5281/zenodo.22059963}
}

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