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mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70 S6k
Author(s) -
Hornberger Troy Alan,
Sukhija Kunal Balu,
Wang Xiao-Rong,
Chien Shu
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.045
Subject(s) - p70 s6 kinase 1 , pi3k/akt/mtor pathway , phosphorylation , chemistry , mechanistic target of rapamycin , microbiology and biotechnology , biophysics , biochemistry , biology , signal transduction
Mechanical stretch induces phosphorylation of the hydrophobic motif site Thr(389) in p70 S6k through a rapamycin‐sensitive (RS) pathway that involves a unique PI3K‐independent mechanism. Rapamycin is considered to be a highly specific inhibitor of the protein kinase mTOR; however, mTOR is also considered to be a PI3K‐dependent signaling molecule. Thus, questions remain as to whether mTOR is the RS element that confers mechanically‐induced signaling to p70 S6k (389). In this study, rapamycin‐resistant mutants of mTOR along with mechanical stretch were used to address this question. The results indicate that mTOR is the RS element and reveal that mTOR signaling can be activated through a PI3K‐independent mechanism.