title: Identification of the novel interacting partners of the mammalian target of rapamycin complex 1 in human CCRF-CEM and HEK293 cells.
abstract: The present study was undertaken to identify proteins that interact with the mammalian target of rapamycin complex 1 (mTORC1) to enable it to carry out its crucial cell signaling functions. Endogenous and myc-tag mTORC1 was purified, in-gel tryptic digested and then identified by nano-LC ESI Q-TOF MS/MS analysis. A total of nine novel interacting proteins were identified in both endogenous and myc-tag mTORC1 purifications. These new mTORC1 interacting partners include heterogeneous nuclear ribonucleoproteins A2/B1, enhancer of mRNA decapping protein 4, 60S acidic ribosomal protein, P0, nucleolin, dynamin 2, glyceraldehyde 3 phosphate dehydrogenase, 2-oxoglutarate dehydrogenase, glycosyl transferase 25 family member 1 and prohibitin 2. Furthermore hnRNP A2/B1 and dynamin 2 interaction with mTORC1 was confirmed on immunoblotting. The present study has for the first time identified novel interacting partners of mTORC1 in human T lymphoblasts (CCRF-CEM) and human embryonic kidney (HEK293) cells. These new interacting proteins may offer new targets for therapeutic interventions in human diseases caused by perturbed mTORC1 signaling.
authors.affiliation: Institute for Clinical Chemistry/UMG-Laboratories, University Medical Centre, Robert-Koch-Str. 40, Goettingen 37075, Germany. hazir.rahman@med.uni-goettingen.de.
authors.forename: Hazir
authors.initials: H
authors.lastname: Rahman
authors.affiliation: Institute for Clinical Chemistry/UMG-Laboratories, University Medical Centre, Robert-Koch-Str. 40, Goettingen 37075, Germany. muhammad.qasim@med.uni-goettingen.de.
authors.forename: Muhammad
authors.initials: M
authors.lastname: Qasim
authors.affiliation: Institute for Clinical Chemistry/UMG-Laboratories, University Medical Centre, Robert-Koch-Str. 40, Goettingen 37075, Germany. michael.oellerich@med.uni-goettingen.de.
authors.forename: Michael
authors.initials: M
authors.lastname: Oellerich
authors.affiliation: Institute for Clinical Chemistry/UMG-Laboratories, University Medical Centre, Robert-Koch-Str. 40, Goettingen 37075, Germany. asif@med.uni-goettingen.de.
authors.forename: Abdul R
authors.initials: AR
authors.lastname: Asif
mesh_terms: D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism*; D045744:Cell Line, Tumor; D002853:Chromatography, Liquid; D057809:HEK293 Cells; D006801:Humans; D015151:Immunoblotting; D047468:Immunoprecipitation; D013058:Mass Spectrometry / Q000379:methods; D000076222:Mechanistic Target of Rapamycin Complex 1; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism*; D036103:Nanotechnology / Q000379:methods; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D014162:Transfection
chemical_list: D002352:Carrier Proteins; D046912:Multiprotein Complexes; D000076222:Mechanistic Target of Rapamycin Complex 1; D058570:TOR Serine-Threonine Kinases