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10.1074/jbc.M114.621730 http://scihub22266oqcxt.onion/10.1074/jbc.M114.621730 C4481205!4481205 !25940091     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25940091 &cmd=llinks): Failed to open stream: HTTP request failed! 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La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1) |pdf=|usr=}}{{25940091 }} gab.com Text La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1) JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25940091 #FOAvip The mammalian target of rapamycin complex 1 (mTORC1) is a critical regulator of protein synthesis. The best studied targets of mTORC1 in translation are the eukaryotic initiation factor-binding protein 1 (4E-BP1) and ribosomal protein S6 kinase 1 (S6K1). In this study, we identify the La-related protein 1 (LARP1) as a key novel target of mTORC1 with a fundamental role in terminal oligopyrimidine (TOP) mRNA translation. Recent genome-wide studies indicate that TOP and TOP-like mRNAs compose a large portion of the mTORC1 translatome, but the mechanism by which mTORC1 controls TOP mRNA translation is incompletely understood. Here, we report that LARP1 functions as a key repressor of TOP mRNA translation downstream of mTORC1. Our data show the following: (i) LARP1 associates with mTORC1 via RAPTOR; (ii) LARP1 interacts with TOP mRNAs in an mTORC1-dependent manner; (iii) LARP1 binds the 5'TOP motif to repress TOP mRNA translation; and (iv) LARP1 competes with the eukaryotic initiation factor (eIF) 4G for TOP mRNA binding. Importantly, from a drug resistance standpoint, our data also show that reducing LARP1 protein levels by RNA interference attenuates the inhibitory effect of rapamycin, Torin1, and amino acid deprivation on TOP mRNA translation. Collectively, our findings demonstrate that LARP1 functions as an important repressor of TOP mRNA translation downstream of mTORC1. Twit Text FOAVip La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1) ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25940091 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25940091 #FOAvip English Wikipedia <ref>{{Cite pmid|25940091 }}</ref> La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1) #MMPMID25940091 Fonseca BD ; Zakaria C ; Jia JJ ; Graber TE ; Svitkin Y ; Tahmasebi S ; Healy D ; Hoang HD ; Jensen JM ; Diao IT ; Lussier A ; Dajadian C ; Padmanabhan N ; Wang W ; Matta-Camacho E ; Hearnden J ; Smith EM ; Tsukumo Y ; Yanagiya A ; Morita M ; Petroulakis E ; González JL ; Hernández G ; Alain T ; Damgaard CK J Biol Chem 2015[Jun]; 290 (26 ): 15996-6020 PMID25940091 show ga The mammalian target of rapamycin complex 1 (mTORC1) is a critical regulator of protein synthesis. The best studied targets of mTORC1 in translation are the eukaryotic initiation factor-binding protein 1 (4E-BP1) and ribosomal protein S6 kinase 1 (S6K1). In this study, we identify the La-related protein 1 (LARP1) as a key novel target of mTORC1 with a fundamental role in terminal oligopyrimidine (TOP) mRNA translation. Recent genome-wide studies indicate that TOP and TOP-like mRNAs compose a large portion of the mTORC1 translatome, but the mechanism by which mTORC1 controls TOP mRNA translation is incompletely understood. Here, we report that LARP1 functions as a key repressor of TOP mRNA translation downstream of mTORC1. Our data show the following: (i) LARP1 associates with mTORC1 via RAPTOR; (ii) LARP1 interacts with TOP mRNAs in an mTORC1-dependent manner; (iii) LARP1 binds the 5'TOP motif to repress TOP mRNA translation; and (iv) LARP1 competes with the eukaryotic initiation factor (eIF) 4G for TOP mRNA binding. Importantly, from a drug resistance standpoint, our data also show that reducing LARP1 protein levels by RNA interference attenuates the inhibitory effect of rapamycin, Torin1, and amino acid deprivation on TOP mRNA translation. Collectively, our findings demonstrate that LARP1 functions as an important repressor of TOP mRNA translation downstream of mTORC1. |*Down-Regulation [MESH] |*Protein Biosynthesis [MESH] |Adaptor Proteins, Signal Transducing/genetics/metabolism [MESH] |Autoantigens/genetics/*metabolism [MESH] |Eukaryotic Initiation Factor-4E/genetics/metabolism [MESH] |Humans [MESH] |Mechanistic Target of Rapamycin Complex 1 [MESH] |Membrane Glycoproteins/genetics/*metabolism [MESH] |Multiprotein Complexes/genetics/metabolism [MESH] |Protein Binding [MESH] |RNA, Long Noncoding [MESH] |RNA, Messenger/chemistry/*genetics/metabolism [MESH] |Regulatory-Associated Protein of mTOR [MESH] |Ribonucleoproteins/genetics/*metabolism [MESH] |SS-B Antigen [MESH]La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) (epmc).pdf DeepDyve Pubget Overpricing