mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70S6k
Mechanical stretch induces phosphorylation of the hydrophobic motif site Thr(389) in p70S6k 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 consid...
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Veröffentlicht in: | FEBS letters 2007-10, Vol.581 (24), p.4562-4566 |
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creator | Hornberger, Troy Alan Sukhija, Kunal Balu Wang, Xiao-Rong Chien, Shu |
description | Mechanical stretch induces phosphorylation of the hydrophobic motif site Thr(389) in p70S6k 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 p70S6k(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. |
doi_str_mv | 10.1016/j.febslet.2007.08.045 |
format | Article |
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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 p70S6k(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.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2007.08.045</identifier><identifier>PMID: 17825298</identifier><language>eng</language><subject>Exercise ; Growth ; Hypertrophy ; JNK2 ; jun N-terminal kinase 2 ; mammalian target of rapamycin ; Mechanotransduction ; mTOR ; p70S6k ; phosphatidic acid ; phospholipase D ; phosphotidylinositol-3-kinase ; PI3K ; PKB ; PLD ; protein kinase B ; rapamycin-resistant kinase-dead mTOR ; rapamycin-resistant mTOR ; ribosomal S6 kinase 1 ; RR-mTOR ; RRKD-mTOR ; Ser ; serine ; Skeletal muscle ; Thr ; threonine</subject><ispartof>FEBS letters, 2007-10, Vol.581 (24), p.4562-4566</ispartof><rights>FEBS Letters 581 (2007) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2007.08.045$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2Fj.febslet.2007.08.045$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1416,1432,27923,27924,45573,45574,46408,46832</link.rule.ids></links><search><creatorcontrib>Hornberger, Troy Alan</creatorcontrib><creatorcontrib>Sukhija, Kunal Balu</creatorcontrib><creatorcontrib>Wang, Xiao-Rong</creatorcontrib><creatorcontrib>Chien, Shu</creatorcontrib><title>mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70S6k</title><title>FEBS letters</title><description>Mechanical stretch induces phosphorylation of the hydrophobic motif site Thr(389) in p70S6k 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 p70S6k(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.</description><subject>Exercise</subject><subject>Growth</subject><subject>Hypertrophy</subject><subject>JNK2</subject><subject>jun N-terminal kinase 2</subject><subject>mammalian target of rapamycin</subject><subject>Mechanotransduction</subject><subject>mTOR</subject><subject>p70S6k</subject><subject>phosphatidic acid</subject><subject>phospholipase D</subject><subject>phosphotidylinositol-3-kinase</subject><subject>PI3K</subject><subject>PKB</subject><subject>PLD</subject><subject>protein kinase B</subject><subject>rapamycin-resistant kinase-dead mTOR</subject><subject>rapamycin-resistant mTOR</subject><subject>ribosomal S6 kinase 1</subject><subject>RR-mTOR</subject><subject>RRKD-mTOR</subject><subject>Ser</subject><subject>serine</subject><subject>Skeletal muscle</subject><subject>Thr</subject><subject>threonine</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNpVkc1q3TAQhUVpaW5u-ggBLduFnZHkH3lTaEP-IBBobtZiLMmxbmzZWE6Cd3mBQJ4xTxLdJhS6GIaZOecs5iPkkEHKgBVH27SxdejsnHKAMgWZQpZ_IismS5GIrJCfyQqAZUleVmKP7IewhThLVn0le6yUPOeVXJHnfnP1h7pA59bSCUfsF-3869NLsD642T1Yeuc8BhsFOFM9-MZOgfZWt-idxq5both5c6-toWM7hFjT0uHsBk-H5m9uu5hpiPvaadoPs2tojLZ0007fhax-UOfpWMJ1cXdAvjTYBfvto6_JzenJ5vg8ubw6uzj-dZmMrCh5UlXA6hoAQYg80wY4Zrk1iJXRVkMhOBqDRW5EYaRhUlsOBhrMDcvKwnKxJj_fc8f7urfR5OcJOzVOrsdpUQM69f_Fu1bdDg-Kg8wgfnhNzt8DHl1nl39GBmoHR23VBxy1g6NAqghHnZ785tc7JjskUAJUnHPxBvZYjqk</recordid><startdate>20071002</startdate><enddate>20071002</enddate><creator>Hornberger, Troy Alan</creator><creator>Sukhija, Kunal Balu</creator><creator>Wang, Xiao-Rong</creator><creator>Chien, Shu</creator><scope>5PM</scope></search><sort><creationdate>20071002</creationdate><title>mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70S6k</title><author>Hornberger, Troy Alan ; Sukhija, Kunal Balu ; Wang, Xiao-Rong ; Chien, Shu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p1672-9901bb00a03354cd02a45edaa9dcec0632adda65d36d8d18ce20d0fa5d1476e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Exercise</topic><topic>Growth</topic><topic>Hypertrophy</topic><topic>JNK2</topic><topic>jun N-terminal kinase 2</topic><topic>mammalian target of rapamycin</topic><topic>Mechanotransduction</topic><topic>mTOR</topic><topic>p70S6k</topic><topic>phosphatidic acid</topic><topic>phospholipase D</topic><topic>phosphotidylinositol-3-kinase</topic><topic>PI3K</topic><topic>PKB</topic><topic>PLD</topic><topic>protein kinase B</topic><topic>rapamycin-resistant kinase-dead mTOR</topic><topic>rapamycin-resistant mTOR</topic><topic>ribosomal S6 kinase 1</topic><topic>RR-mTOR</topic><topic>RRKD-mTOR</topic><topic>Ser</topic><topic>serine</topic><topic>Skeletal muscle</topic><topic>Thr</topic><topic>threonine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hornberger, Troy Alan</creatorcontrib><creatorcontrib>Sukhija, Kunal Balu</creatorcontrib><creatorcontrib>Wang, Xiao-Rong</creatorcontrib><creatorcontrib>Chien, Shu</creatorcontrib><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hornberger, Troy Alan</au><au>Sukhija, Kunal Balu</au><au>Wang, Xiao-Rong</au><au>Chien, Shu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70S6k</atitle><jtitle>FEBS letters</jtitle><date>2007-10-02</date><risdate>2007</risdate><volume>581</volume><issue>24</issue><spage>4562</spage><epage>4566</epage><pages>4562-4566</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Mechanical stretch induces phosphorylation of the hydrophobic motif site Thr(389) in p70S6k 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 p70S6k(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.</abstract><pmid>17825298</pmid><doi>10.1016/j.febslet.2007.08.045</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; ScienceDirect Journals (5 years ago - present); Wiley Online Library All Journals; Alma/SFX Local Collection |
subjects | Exercise Growth Hypertrophy JNK2 jun N-terminal kinase 2 mammalian target of rapamycin Mechanotransduction mTOR p70S6k phosphatidic acid phospholipase D phosphotidylinositol-3-kinase PI3K PKB PLD protein kinase B rapamycin-resistant kinase-dead mTOR rapamycin-resistant mTOR ribosomal S6 kinase 1 RR-mTOR RRKD-mTOR Ser serine Skeletal muscle Thr threonine |
title | mTOR is the rapamycin‐sensitive kinase that confers mechanically‐induced phosphorylation of the hydrophobic motif site Thr(389) in p70S6k |
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