RAPT1, A MAMMALIAN HOMOLOG OF YEAST TOR, INTERACTS WITH THE FKBP12 RAPAMYCIN COMPLEX

被引：382

作者：

CHIU, MI ^{[1
]}

KATZ, H ^{[1
]}

BERLIN, V ^{[1
]}

机构：

[1] MITOTIX INC,CAMBRIDGE,MA 02139

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1994年 / 91卷 / 26期

关键词：

PHOSPHATIDYLINOSITOL; 3-KINASE;

D O I：

10.1073/pnas.91.26.12574

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Rapamycin is a potent immunosuppressant that blocks the G(1)/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.

引用

页码：12574 / 12578

页数：5

共 30 条

[1]

ALBERS MW, 1993, J BIOL CHEM, V268, P22825

[2]

BERLIN V, 1995, IN PRESS CELL CYCLE

[3] PROBING IMMUNOSUPPRESSANT ACTION WITH A NONNATURAL IMMUNOPHILIN LIGAND [J].