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Search results 1 to 26 out of 26 for Mtor

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: TMEM127 modulates mTOR function in the endolysosome. Its interaction with early endosomal GTPase Rab5 to inhibit mTOR signalling seems to be related with its tumour-suppressive properties [].
Protein Domain
Type: Domain
Description: Transmembrane protein 127 (TMEM127) modulates mTOR function in the endolysosome. Its interaction with early endosomal GTPase Rab5 to inhibit mTOR signalling seems to be related with its tumour-suppressing properties [, ]. This entry represents the transmembrane region of this protein and similar animal sequences.
Protein Domain
Type: Domain
Description: DEP domain-containing mTOR-interacting protein (DEPTOR) is an mTOR inhibitor that plays pivotal roles in the pathogenesis and progression of many tumours [, ].This entry represents the first DEP domain of DEPTOR. Its function is not clear.
Protein Domain
Type: Domain
Description: DEP domain-containing mTOR-interacting protein (DEPTOR) is an mTOR inhibitor that plays pivotal roles in the pathogenesis and progression of many tumours [, ].This entry represents the second DEP domain of DEPTOR. Its function is not clear.
Protein Domain
Type: Family
Description: Ragulator complex protein LAMTOR3 (for lysosomal adaptor and MAPK and MTOR activator 3) is a regulator of the TOR pathway, which is a signalling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids [].
Protein Domain
Type: Family
Description: Lamtor4 is a component of the Ragulator complex, a complex that functions as a guanine nucleotide exchange factor for the Rag GTPases that signal amino acid levels to mTORC1. The mTOR Complex 1 (mTORC1) pathway regulates cell growth in response to numerous cues. Lamtor4 is required for mTORC1 activation by amino acids []. The Rag-Ragulator complex also has functions independent of mTOR signaling; RagA and Lamtor4 are essential regulators of lysosomes in microglia [].
Protein Domain
Type: Family
Description: WIPI1 is a homologue of the yeast Atg18 protein that also contains the multiple WD40 repeat domains, which allows it to bind to phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate [, ]. It plays a role in autophagy and is involved in the MTOR signalling in melanogenesis [, ].
Protein Domain
Type: Family
Description: Serine/threonine-protein kinase SMG1 is a phosphatidylinositol kinase-related protein that acts as an mRNA-surveillance protein and is a key component of nonsense-mediated decay (NMD) [, , , ]. In C.elegans, SMG1 is a key regulator of growth. Loss of SMG1 leads to hyperactive responses to injury and subsequent growth that continues out of control. It has an antagonistic role to mTOR signalling in worms []and possibly also in higher eukaryotes.
Protein Domain
Type: Domain
Description: The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. Rictor (rapamycin-insensitive companion of mTOR) is a component of mTORC2 []. There is a regulatory link between the two mTOR complexes, whereby Rictor phosphorylation by mTORC1 regulates mTORC2 signalling []. Over-expression of Rictor increases mTORC2 activity and promotes cell growth and motility [].This domain is the N-terminal conserved section that may include several individual domains.
Protein Domain
Type: Domain
Description: This domain is found at the C terminus of many regulatory proteins, including the yeast proteasomal subunit Rpn11 and eukaryotic initiation factor 3 subunit F (eIF3f). The Rpn11 C-terminal domain is necessary for normal mitochondrial morphology and function and is thought to regulate the mitochondrial fission and tubulation processes []. The eIF3f C-terminal domain is critical for proper eIF3f activity in skeletal muscle through its interaction with mTOR (also known as FRAP, RAFT1 or RAPT) [, ].
Protein Domain
Type: Domain
Description: CLEC16A (C-Type Lectin Domain Containing 16A) has an inhibitory role in autophagy, probably by activating the mTOR pathway []. It also has a role in beta-cells as a regulator of mitophagy [].GFS9/TT9 (TRANSPARENT TESTA 9) is a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles. It contributes to intracellular membrane trafficking and flavonoid accumulation [].This entry represents a domain found at the N terminus of CLEC16A and GFS9/TT9.
Protein Domain
Type: Family
Description: Proline-rich AKT1 substrate 1 protein (AKT1S1, PRAS40) is part of the mammalian target of rapamycin complex 1 (mTORC1, contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR), which regulates cell growth and survival in response to nutrient and hormonal signals []. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. AKT1S1 is a substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. It may also play a role in nerve growth factor-mediated neuroprotection [, ].
Protein Domain
Type: Domain
Description: This domain is found in the more conserved central section of Rictor (rapamycin-insensitive companion of mTOR) that may include several individual domains. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. Rictor is a component of mTORC2 []. There is a regulatory link between the two mTOR complexes, whereby Rictor phosphorylation by mTORC1 regulates mTORC2 signalling []. Over-expression of Rictor increases mTORC2 activity and promotes cell growth and motility [].
Protein Domain
Type: Domain
Description: This entry represent the conserved domain 5 of the Rictor (Rapamycin-insensitive companion of mTOR) protein. The mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. Rictor (rapamycin-insensitive companion of mTOR) is a component of mTORC2 []. There is a regulatory link between the two mTOR complexes, whereby Rictor phosphorylation by mTORC1 regulates mTORC2 signalling []. Over-expression of Rictor increases mTORC2 activity and promotes cell growth and motility [].
Protein Domain
Type: Domain
Description: This entry represents the domain 4 of the Rictor (rapamycin-insensitive companion of mTOR) protein. It is found in the more conserved central section that may include several individual domainsThe mammalian target of rapamycin (mTOR) is a conserved Ser/Thr kinase that forms two functionally distinct complexes, mTROC1 and mTORC2, important for nutrient and growth-factor signalling. Rictor (rapamycin-insensitive companion of mTOR) is a component of mTORC2 []. There is a regulatory link between the two mTOR complexes, whereby Rictor phosphorylation by mTORC1 regulates mTORC2 signalling []. Over-expression of Rictor increases mTORC2 activity and promotes cell growth and motility [].
Protein Domain
Type: Family
Description: CLEC16A (C-Type Lectin Domain Containing 16A) an evolutionarily conserved endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. It is required for mitophagy, autophagy and endosome maturation [, ]. This protein has been identified as a susceptibility gene for autoimmune diseases like type 1 diabetes, multiple sclerosis and adrenal dysfunction []. It has an inhibitory role in autophagy, probably by activating the mTOR pathway [].GFS9/TT9 (TRANSPARENT TESTA 9) is a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles. It contributes to intracellular membrane trafficking and flavonoid accumulation [].
Protein Domain
Type: Family
Description: This entry represents a group of F-box only proteins, including FBXO9/48 from animals, Pof7/Hrt3 from yeasts and GID2/SKIP32 from plants.Hrt3 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins []. FBXO9 is a substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of TTI1 and TELO2 in a CK2-dependent manner, thereby directly regulating mTOR signalling []. GID2 (also known as SLEEPY 1) is an essential component of the SCF-type E3 ligase complex, SCF(GID2), a complex that positively regulates the gibberellin signalling pathway [].
Protein Domain
Type: Domain
Description: This entry represents a domain found at the C terminus of CLEC16A and TT9. CLEC16A (C-Type Lectin Domain Containing 16A) an evolutionarily conserved endosomal membrane protein required for trafficking of fluid-phase and receptor-mediated endocytic cargos. It is required for mitophagy, autophagy and endosome maturation [, ]. This protein has been identified as a susceptibility gene for autoimmune diseases like type 1 diabetes, multiple sclerosis and adrenal dysfunction []. It has an inhibitory role in autophagy, probably by activating the mTOR pathway [].GFS9/TT9 (TRANSPARENT TESTA 9) is a protein from Arabidopsis required for vacuolar development through membrane fusion at vacuoles. It contributes to intracellular membrane trafficking and flavonoid accumulation [].
Protein Domain
Type: Family
Description: LAMTOR1 is a family of eukaryotic proteins that have otherwise been referred to as Lipid raft adaptor protein p18, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 1, and Protein associated with DRMs and endosomes.LAMTOR1 regulates the mTOR (mammalian target of rapamycin) pathway, a signaling cascade that promotes cell growth in response to growth factors, energy levels, and amino acids. LAMTOR1 is part of the Ragulator complex, recruits the Rag GTPases and the mTORC1 complex to lysosomes, a key step in activation of the TOR signaling cascade by amino acids []. LAMTOR1 is responsible for anchoring the Ragulator complex to membranes. It may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes []. It may be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. It may also play a role in RHOA activation [, ].This family also includes Saccharomyces cerevisiae MEH1 (Ego1), a component of the EGO complex. The EGO complex and the Rag-Ragulator complex are structurally related []. The yeast EGO complex consists of Gtr1, Gtr2, Ego1, and Ego3, localises to the endosomal and vacuolar membranes, and plays a crucial role in cell growth and autophagy regulation through amino acid signals that activate TORC1 []. MEH1 (GSE2) is also a component of the GSE complex, which is required for proper sorting of amino acid permease Gap1 [].
Protein Domain
Type: Family
Description: This entry represents target of rapamycin complex subunit LST8 (MLST8 or GbetaL), a component of both mTORC1 and mTORC2, complexes that regulate cell growth in response to nutrients. The mTORC1 complex consists of MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. The mTORC2 complex contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR []. In mTORC1, MLST8 interacts directly with MTOR and enhances its kinase activity [].This entry also includes the target of rapamycin complex subunit wat1 (pop3 or wat1) from Schizosaccharomyces pombe, which is also a component of yeast TORC1 and TORC2 complexes. The subunits of TORC1 in fission yeasts are known as mip1, pop3/wat1, tco89, toc1 and tor2; and the subunits of the TORC2 complex are bit61, pop3/wat1, sin1, ste20 and tor1 [].
Protein Domain
Type: Family
Description: This family consists of Raptor (regulatory associated protein of TOR) and its orthologs which includes Kog1p of Saccharomyces cerevisiae (Baker's yeast), a highly conserved 150kDa TOR-binding protein [, , ]. The target-of-rapamycin (TOR) proteins are protein kinases that were first identified in S. cerevisiae through mutants that conferred resistance to growth inhibition induced by the immunosuppressive macrolide rapamycin [].All Raptor orthologs contain a unique conserved region in their N-terminal half (raptor N-terminal conserved, also called the RNC domain) followed by three HEAT (huntingtin, elongation factor 3, A subunit of protein phosphatase 2A and TOR1) repeats and seven WD-40 repeats near the C terminus. Research on mammalian Raptor suggests that its association with mTOR promotes the phosphorylation of downstream effectors in nutrient-stimulated cells [, ]. In concordance with these observations, the binding of TOR to Raptor or to Kog1p []is necessary for TOR signalling in vivo in Caenorhabditis elegans and S. cerevisiae [, ].The RNC domain consists of 3 blocks with at least 67 to 79% sequence similarity and is predicted to have a high propensity to form alpha helices. The RNC domain is characterised by the presence of invariant catalytic Cys-His dyad, which is structurally and evolutionarily related to known caspases, suggesting that the raptor proteins may have protease activity [].
Protein Domain
Type: Domain
Description: This entry represents the non-structural protein 6 (NSP6) from betacoronavirus. Recently, it was reported that SARS-CoV-2 NSP6 binds TANK binding kinase 1 (TBK1) to suppress interferon regulatory factor 3 (IRF3) phosphorylation which suppresses IFN-I signalling and production more efficiently than SARS-CoV and MERS-CoV [].Coronaviruses (CoV) redirect and rearrange host cell membranes as part of the viral genome replication and transcription machinery; they induce the formation of double-membrane vesicles in infected cells. CoV non-structural protein 6 (NSP6), a transmembrane-containing protein, together with NSP3 and NSP4, have the ability to induce double-membrane vesicles that are similar to those observed in severe acute respiratory syndrome (SARS) coronavirus-infected cells []. By itself, NSP6 can generate autophagosomes from the endoplasmic reticulum. Autophagosomes are normally generated as a cellular response to starvation to carry cellular organelles and long-lived proteins to lysosomes for degradation. Degradation through autophagy may provide an innate defense against virus infection, or conversely, autophagosomes can promote infection by facilitating the assembly of replicase proteins []. In additionto initiating autophagosome formation, NSP6 also limits autophagosome expansion regardless of how they were induced, i.e. whether they were induced directly by NSP6, or indirectly by starvation or chemical inhibition of MTOR signalling. This may favour coronavirus infection by compromising the ability of autophagosomes to deliver viral components to lysosomes for degradation [].
Protein Domain
Type: Domain
Description: This entry represents the non-structural protein 6 (NSP6) from gammacoronavirus.Coronaviruses (CoV) redirect and rearrange host cell membranes as part of the viral genome replication and transcription machinery; they induce the formation of double-membrane vesicles in infected cells. CoV non-structural protein 6 (NSP6), a transmembrane-containing protein, together with NSP3 and NSP4, have the ability to induce double-membrane vesicles that are similar to those observed in severe acute respiratory syndrome (SARS) coronavirus-infected cells []. By itself, NSP6 can generate autophagosomes from the endoplasmic reticulum. Autophagosomes are normally generated as a cellular response to starvation to carry cellular organelles and long-lived proteins to lysosomes for degradation. Degradation through autophagy may provide an innate defense against virus infection, or conversely, autophagosomes can promote infection by facilitating the assembly of replicase proteins []. In addition to initiating autophagosome formation, NSP6 also limits autophagosome expansion regardless of how they were induced, i.e. whether they were induced directly by NSP6, or indirectly by starvation or chemical inhibition of MTOR signalling. This may favour coronavirus infection by compromising the ability of autophagosomes to deliver viral components to lysosomes for degradation [].
Protein Domain
Type: Domain
Description: This entry represents the non-structural protein 6 (NSP6) from alphacoronavirus.Coronaviruses (CoV) redirect and rearrange host cell membranes as part of the viral genome replication and transcription machinery; they induce the formation of double-membrane vesicles in infected cells. CoV non-structural protein 6 (NSP6), a transmembrane-containing protein, together with NSP3 and NSP4, have the ability to induce double-membrane vesicles that are similar to those observed in severe acute respiratory syndrome (SARS) coronavirus-infected cells []. By itself, NSP6 can generate autophagosomes from the endoplasmic reticulum. Autophagosomes are normally generated as a cellular response to starvation to carry cellular organelles and long-lived proteins to lysosomes for degradation. Degradation through autophagy may provide an innate defense against virus infection, or conversely, autophagosomes can promote infection by facilitating the assembly of replicase proteins []. In addition to initiating autophagosome formation, NSP6 also limits autophagosome expansion regardless of how they were induced, i.e. whether they were induced directly by NSP6, or indirectly by starvation or chemical inhibition of MTOR signalling. This may favour coronavirus infection by compromising the ability of autophagosomes to deliver viral components to lysosomes for degradation [].
Protein Domain
Type: Family
Description: This entry represents ribosomal protein S6 kinase (or p70S6K). S6 kinase is a serine/threonine kinase (STK) that catalyses the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. It contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). S6 kinase is part of the mammalian target of rapamycin (mTOR) pathway, which is a key regulator of cell growth via the regulation of protein synthesis. Both S6 kinase and eukaryotic initiation factor 4E-binding protein 1 (4EBP-1) are key mTOR effectors of cell growth [, , , ]. S6 kinase specifically phosphorylates ribosomal protein S6 in response to insulin or several classes of mitogens. S6 kinase is activated by serine/threonine phosphorylation and protein kinase C, and is inactivated by type 2A phosphatase []. S6 kinase interacts with PPP1R9A/neurabin-1 []. S6 kinase also plays a pivotal role glucose homeostasis. Its targets include the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of S6 kinase, named S6K1 and S6K2 (or S6K-beta). S6 kinase is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.
Protein Domain
Type: Family
Description: Birt-Hogg-Dube' syndrome, a disorder characterised by benign tumours of the hair follicle, lung cysts and renal neoplasia, is caused by germline mutations in the BHD(FLCN) gene; this encodes a tumour suppressor protein, folliculin (FLCN), of unknown function []. The folliculin- interacting protein, FNIP1, has also been identified and shown to interact with 5' AMP-activated protein kinase (AMPK), which plays a vital role in energy sensing []. Together, then, it is thought that folliculin (mutated in Birt-Hogg-Dube' syndrome) and its interaction partner, FNIP1, may be involved in energy and/or nutrient sensing via the AMPK and mTOR signalling pathways.FNIP1 has a homologue, FNIP2, which also interacts with FLCN and AMPK. C-terminally-deleted FLCN mutants, like those produced by germline mutations in BHD patients, do not bind FNIP2, suggesting that FLCN tumour-suppressor function may be facilitated by interactions with both FNIP1 and FNIP2 via its C terminus []. FNIP1 and FNIP2 are able to form homo- or heteromeric multimers, and may hence function either independently or cooperatively with FLCN [].This entry represents the FNIP family, including FNIP1 and FNIP2.