RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.

Chiu, M I; Katz, H; Berlin, V

doi:10.1073/pnas.91.26.12574

Cited by 481PI3K/AKT/mTOR signaling in cancerSignaling Pathways in DiseaseFungal and yeast genetics research

RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.

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Chiu, M I, Katz, H, Berlin, V·1994·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.91.26.12574PMC PMC45481

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Abstract

Rapamycin is a potent immunosuppressant that blocks the G1/S transition in antigen-activated T cells and in yeast. The similar effects of rapamycin in animal cells and yeast suggest that the biochemical steps affected by rapamycin are conserved. Using a two-hybrid system we isolated mammalian clones that interact with the human FK506/rapamycin-binding protein (FKBP12) in the presence of rapamycin. Specific interactors, designated RAPT1, encode overlapping sequences homologous to yeast Tor, a putative novel phosphatidylinositol 3-kinase. A region of 133 amino acids of RAPT1 is sufficient for binding to the FKBP12/rapamycin complex. The corresponding region in yeast Tor contains the serine residue that when mutated to arginine confers resistance to rapamycin. Introduction of this mutation into RAPT1 abolishes its interaction with the FKBP12/rapamycin complex.

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From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Chiu et al., 1994

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Authors: Chiu, M. I., Katz, H., & Berlin, V
Affiliations: Mitotix, Inc., Cambridge, MA 02139.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1994-12-20
Volume: 91
Issue: 26
Pages: 12574-12578
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.91.26.12574
PMC: PMC45481
OpenAlex: W2120356140
Cited by: 481
References: 30
Citations by year: 2026: 7 · 2025: 4 · 2024: 9 · 2023: 5 · 2022: 12 · 2021: 14 · 2020: 13 · 2019: 9 · 2018: 14 · 2017: 17 · 2016: 17 · 2015: 13 · 2014: 10 · 2013: 20 · 2012: 12
FWCI: 5.32
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords: TOR kinase, FKBP12, rapamycin, protein-protein interaction, phosphatidylinositol 3-kinase, G1/S transition, T cell activation, rapamycin resistance, conserved signaling pathways, yeast homolog
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Carrier Proteins, Cloning, Molecular, DNA-Binding Proteins, Heat-Shock Proteins, Molecular Sequence Data, Polyenes, Protein Binding, RNA, Messenger, Structure-Activity Relationship, Tissue Distribution, Gene Expression, Mutagenesis, Site-Directed, Sequence Alignment, Sequence Homology, Amino Acid, Phosphotransferases (Alcohol Group Acceptor), DNA Primers, Phosphatidylinositol 3-Kinases, Sirolimus, Tacrolimus Binding Proteins, Macromolecular Substances, Mice, TOR Serine-Threonine Kinases

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RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex.

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