|Other Names||Target of rapamycin complex subunit LST8, TORC subunit LST8, G protein beta subunit-like, Gable, Protein GbetaL, Mammalian lethal with SEC13 protein 8, mLST8, MLST8, GBL, LST8|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8200c was selected from the Center region of human GBL. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1- mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient- poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum- induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.|
|Tissue Location||Broadly expressed, with highest levels in skeletal muscle, heart and kidney.|
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Provided below are standard protocols that you may find useful for product applications.
G锟淟 (G protein beta protein subunit-like) is a member of a signaling pathway that regulates mammalian cell growth in response to the presence of nutrients and growth factors. It binds to the kinase domain of TOR (Target of rapamycin, also known as mTOR), an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. Rapamycin inhibits TOR resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. TOR is normally associated with G锟淟 and an additional regulatory protein RAPTOR, allowing TOR to control protein biosynthesis. The binding of G锟淟 to TOR stimulates TOR's kinase activity towards downstream proteins such as RPS6K (ribosomal protein S6 kinase) and the translation factor 4E-BP1 which leads to increased protein translation and cell growth.
Ota, T., et al., Nat. Genet. 36(1):40-45 (2004).
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