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

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.

authors

Chiu MI,Katz H,Berlin V

doi

10.1073/pnas.91.26.12574

subject

Has Abstract

pub_date

1994-12-20 00:00:00

pages

12574-8

issue

26

eissn

0027-8424

issn

1091-6490

journal_volume

91

pub_type

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