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AB196074

Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus)

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Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus) is a Human Fragment protein, in the 1362 to 2549 aa range, expressed in Baculovirus infected Sf9 cells, with >50%, suitable for SDS-PAGE, FuncS.

View Alternative Names

FRAP, FRAP1, FRAP2, RAFT1, RAPT1, MTOR, Serine/threonine-protein kinase mTOR, FK506-binding protein 12-rapamycin complex-associated protein 1, FKBP12-rapamycin complex-associated protein, Mammalian target of rapamycin, Mechanistic target of rapamycin, Rapamycin and FKBP12 target 1, Rapamycin target protein 1, Tyrosine-protein kinase mTOR, mTOR, KIAA1303, RAPTOR, RPTOR, Regulatory-associated protein of mTOR, Raptor, p150 target of rapamycin (TOR)-scaffold protein, GBL, LST8, MLST8, Target of rapamycin complex subunit LST8, TORC subunit LST8, G protein beta subunit-like, Mammalian lethal with SEC13 protein 8, Gable, Protein GbetaL, mLST8

2 Images
Functional Studies - Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus) (AB196074)
  • FuncS

Supplier Data

Functional Studies - Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus) (AB196074)

Activity assay using ab196074.

SDS-PAGE - Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus) (AB196074)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human mTOR + MLST8 + Raptor protein (DDDDK tag N-Terminus, His tag N-Terminus) (AB196074)

10% SDS-PAGE analysis of 3 μg ab196074 with Coomassie staining.

Key facts

Purity

>50% SDS-PAGE

Expression system

Baculovirus infected Sf9 cells

Tags

Tag free

Applications

SDS-PAGE, FuncS

applications

Biologically active

Yes

Biological activity

Specific Activity: 7.1pmol/min/μg.

Enzyme reaction is conducted in a buffer containing 50 mM HEPES (pH 7.5), 10 mM MgCl2, 1 mM EGTA, 200 μM ATP, 0.01% Brij-35 and 2 μM substrate at room temperature for 1 hour.

Accession

P42345

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.02% Potassium chloride

storage-buffer

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Complementary Products

Proteins & Peptides

AB114179

Recombinant Human mTOR protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human mTOR protein (GST tag N-Terminus) (AB114179)

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Proteins & Peptides

AB84769

Recombinant Human PI 3 Kinase p85 alpha protein

Western blot - Recombinant Human PI 3 Kinase p85 alpha protein (AB84769)

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Assay Kits

AB206311

Mouse mTOR ELISA Kit

Recombinant|SimpleStep

Sandwich ELISA - Mouse mTOR ELISA Kit (AB206311)

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Proteins & Peptides

AB112419

Recombinant Human Raptor protein (GST tag N-Terminus)

SDS-PAGE - Recombinant Human Raptor protein (GST tag N-Terminus) (AB112419)

  • 0
  • 0
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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

Complex of Human mTOR (GenBank Accession No. NM_004958), a.a. 1362-end, with N-terminal DDDDK tag, Human MLST8 (GenBank Accession No. NM_022372), a.a. 2-326 (end) with N-terminal His tag, and Human Raptor (GenBank Accession No. NM_020761), a.a. 2-1335 (end) with N-terminal His tag, co-expressed in a Baculovirus-infected Sf9 cell expression system.
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Sequence info

[{"sequence":"EFMEHSDKGPLPLRDDNGIVLLGERAAKCRAYAKALHYKELEFQKGPTPAILESLISINNKLQQPEAAAGVLEYAMKHFGELEIQATWYEKLHEWEDALVAYDKKMDTNKDDPELMLGRMRCLEALGEWGQLHQQCCEKWTLVNDETQAKMARMAAAAAWGLGQWDSMEEYTCMIPRDTHDGAFYRAVLALHQDLFSLAQQCIDKARDLLDAELTAMAGESYSRAYGAMVSCHMLSELEEVIQYKLVPERREIIRQIWWERLQGCQRIVEDWQKILMVRSLVVSPHEDMRTWLKYASLCGKSGRLALAHKTLVLLLGVDPSRQLDHPLPTVHPQVTYAYMKNMWKSARKIDAFQHMQHFVQTMQQQAQHAIATEDQQHKQELHKLMARCFLKLGEWQLNLQGINESTIPKVLQYYSAATEHDRSWYKAWHAWAVMNFEAVLHYKHQNQARDEKKKLRHASGANITNATTAATTAATATTTASTEGSNSESEAESTENSPTPSPLQKKVTEDLSKTLLMYTVPAVQGFFRSISLSRGNNLQDTLRVLTLWFDYGHWPDVNEALVEGVKAIQIDTWLQVIPQLIARIDTPRPLVGRLIHQLLTDIGRYHPQALIYPLTVASKSTTTARHNAANKILKNMCEHSNTLVQQAMMVSEELIRVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKQLPQLTSLELQYVSPKLLMCRDLELAVPGTYDPNQPIIRIQSIAPSLQVITSKQRPRKLTLMGSNGHEFVFLLKGHEDLRQDERVMQLFGLVNTLLANDPTSLRKNLSIQRYAVIPLSTNSGLIGWVPHCDTLHALIRDYREKKKILLNIEHRIMLRMAPDYDHLTLMQKVEVFEHAVNNTAGDDLAKLLWLKSPSSEVWFDRRTNYTRSLAVMSMVGYILGLGDRHPSNLMLDRLSGKILHIDFGDCFEVAMTREKFPEKIPFRLTRMLTNAMEVTGLDGNYRITCHTVMEVLREHKDSVMAVLEAFVYDPLLNWRLMDTNTKGNKRSRTRTDSYSAGQSVEILDGVELGEPAHKKTGTTVPESIHSFIGDGLVKPEALNKKAIQIINRVRDKLTGRDFSHDDTLDVPTQVELLIKQATSHENLCQCYIGWCPFW","proteinLength":"Fragment","predictedMolecularWeight":"137 kDa","actualMolecularWeight":null,"aminoAcidEnd":2549,"aminoAcidStart":1362,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P42345","tags":[{"tag":"DDDDK","terminus":"N-Terminus"}]},{"sequence":"ESEMLQSPLLGLGEEDEADLTDWNLPLAFMKKRHCEKIEGSKSLAQSWRMKDRMKTVSVALVLCLNVGVDPPDVVKTTPCARLECWIDPLSMGPQKALETIGANLQKQYENWQPRARYKQSLDPTVDEVKKLCTSLRRNAKEERVLFHYNGHGVPRPTVNGEVWVFNKNYTQYIPLSIYDLQTWMGSPSIFVYDCSNAGLIVKSFKQFALQREQELEVAAINPNHPLAQMPLPPSMKNCIQLAACEATELLPMIPDLPADLFTSCLTTPIKIALRWFCMQKCVSLVPGVTLDLIEKIPGRLNDRRTPLGELNWIFTAITDTIAWNVLPRDLFQKLFRQDLLVASLFRNFLLAERIMRSYNCTPVSSPRLPPTYMHAMWQAWDLAVDICLSQLPTIIEEGTAFRHSPFFAEQLTAFQVWLTMGVENRNPPEQLPIVLQVLLSQVHRLRALDLLGRFLDLGPWAVSLALSVGIFPYVLKLLQSSARELRPLLVFIWAKILAVDSSCQADLVKDNGHKYFLSVLADPYMPAEHRTMTAFILAVIVNSYHTGQEACLQGNLIAICLEQLNDPHPLLRQWVAICLGRIWQNFDSARWCGVRDSAHEKLYSLLSDPIPEVRCAAVFALGTFVGNSAERTDHSTTIDHNVAMMLAQLVSDGSPMVRKELVVALSHLVVQYESNFCTVALQFIEEEKNYALPSPATTEGGSLTPVRDSPCTPRLRSVSSYGNIRAVATARSLNKSLQNLSLTEESGGAVAFSPGNLSTSSSASSTLGSPENEEHILSFETIDKMRRASSYSSLNSLIGVSFNSVYTQIWRVLLHLAADPYPEVSDVAMKVLNSIAYKATVNARPQRVLDTSSLTQSAPASPTNKGVHIHQAGGSPPASSTSSSSLTNDVAKQPVSRDLPSGRPGTTGPAGAQYTPHSHQFPRTRKMFDKGPEQTADDADDAAGHKSFISATVQTGFCDWSARYFAQPVMKIPEEHDLESQIRKEREWRFLRNSRVRRQAQQVIQKGITRLDDQIFLNRNPGVPSVVKFHPFTPCIAVADKDSICFWDWEKGEKLDYFHNGNPRYTRVTAMEYLNGQDCSLLLTATDDGAIRVWKNFADLEKNPEMVTAWQGLSDMLPTTRGAGMVVDWEQETGLLMSSGDVRIVRIWDTDREMKVQDIPTGADSCVTSLSCDSHRSLIVAGLGDGSIRVYDRRMALSECRVMTYREHTAWVVKASLQKRPDGHIVSVSVNGDVRIFDPRMPESVNVLQIVKGLTALDIHPQADLIACGSVNQFTAIYNSSGELINNIKYYDGFMGQRVGAISCLAFHPHWPHLAVGSNDYYISVYSVEKRVR","proteinLength":"Full Length","predictedMolecularWeight":"150 kDa","actualMolecularWeight":null,"aminoAcidEnd":1335,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q8N122","tags":[{"tag":"His","terminus":"N-Terminus"}]},{"sequence":"NTSPGTVGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEVTPDRSMIAAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRWMYTGGEDCTARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDLKTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEVTQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTELSIKSGNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKREYGGHQKAVVCLAFNDSVLG","proteinLength":"Full Length","predictedMolecularWeight":"37 kDa","actualMolecularWeight":null,"aminoAcidEnd":326,"aminoAcidStart":2,"nature":"Recombinant","expressionSystem":"Baculovirus infected Sf9 cells","accessionNumber":"Q9BVC4","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
True
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The mTOR MLST8 and Raptor proteins together form a complex known as the mTORC1 complex. mTOR also called the mechanistic Target of Rapamycin is a serine/threonine kinase with a mass of about 289 kDa. It is expressed in various tissues including muscle liver and brain where it plays an important role in controlling cellular growth and metabolism. MLST8 also sometimes known as GβL is a regulatory binding partner within this complex. Raptor an adaptor protein assists the assembly of mTORC1 thereby facilitating its recruitment to substrates.
Biological function summary

The mTORC1 complex regulates processes of cell growth proliferation and autophagy in response to nutrient signals. mTORC1 integrates inputs from upstream growth factors and amino acid levels to influence cell cycle progression and protein synthesis. The complex localizes to the lysosomal surface where it becomes activated. This activation allows mTORC1 to control anabolic pathways ensuring that cells can increase their mass and function optimally in response to environmental cues.

Pathways

MTORC1 interacts with the PI3K/AKT signaling pathway which is essential for controlling metabolism and cellular survival. This pathway involves proteins such as AKT and TSC2 which serve as regulators of mTORC1 activity. Additionally mTORC1 influences the AMPK pathway which balances energy expenditure with availability. Through these interactions mTORC1 serves as a pivotal node that integrates nutrient and energy signals to coordinate cell growth and division.

The mTORC1 complex exhibits a significant connection to cancer and metabolic disorders. Dysregulation of mTORC1 activity often through mutations in related proteins such as PTEN contributes to uncontrolled cell proliferation and tumor formation. Moreover abnormal mTORC1 signaling can affect insulin sensitivity linking it to metabolic syndromes like diabetes. Understanding and targeting this complex holds therapeutic potential for these disorders as it touches upon key aspects of cellular metabolism and growth control.
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Specifications

Form

Liquid

Additional notes

Affinity purified.

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General info

Function

Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed : 12087098, PubMed : 12150925, PubMed : 12150926, PubMed : 12231510, PubMed : 12718876, PubMed : 14651849, PubMed : 15268862, PubMed : 15467718, PubMed : 15545625, PubMed : 15718470, PubMed : 18497260, PubMed : 18762023, PubMed : 18925875, PubMed : 20516213, PubMed : 20537536, PubMed : 21659604, PubMed : 23429703, PubMed : 23429704, PubMed : 25799227, PubMed : 26018084, PubMed : 29150432, PubMed : 29236692, PubMed : 31112131, PubMed : 31601708, PubMed : 32561715, PubMed : 34519269, PubMed : 37751742). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed : 15268862, PubMed : 15467718, PubMed : 17517883, PubMed : 18372248, PubMed : 18497260, PubMed : 18925875, PubMed : 20516213, PubMed : 21576368, PubMed : 21659604, PubMed : 23429704, PubMed : 30171069, PubMed : 29236692, PubMed : 37751742). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed : 15268862, PubMed : 15467718, PubMed : 18497260, PubMed : 18925875, PubMed : 20516213, PubMed : 21576368, PubMed : 21659604, PubMed : 23429704, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed : 12087098, PubMed : 12150925, PubMed : 12150926, PubMed : 12231510, PubMed : 12718876, PubMed : 14651849, PubMed : 15268862, PubMed : 15467718, PubMed : 15545625, PubMed : 15718470, PubMed : 18497260, PubMed : 18762023, PubMed : 18925875, PubMed : 20516213, PubMed : 20537536, PubMed : 21659604, PubMed : 23429703, PubMed : 23429704, PubMed : 25799227, PubMed : 26018084, PubMed : 29150432, PubMed : 29236692, PubMed : 31112131, PubMed : 34519269). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed : 24403073, PubMed : 29236692). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed : 12087098, PubMed : 12150925, PubMed : 18925875, PubMed : 29150432, PubMed : 29236692). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed : 23429703, PubMed : 23429704). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed : 20516213). Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation (PubMed : 36691768). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (PubMed : 23426360). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways : negatively regulates autophagy through phosphorylation of ULK1 (PubMed : 32561715). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed : 32561715). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed : 20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed : 30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed : 23524951, PubMed : 25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed : 21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed : 12231510). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed : 12150925, PubMed : 12150926, PubMed : 24403073, PubMed : 31695197). The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation (PubMed : 22343943, PubMed : 22576015, PubMed : 22692423, PubMed : 24448649, PubMed : 32612235, PubMed : 36608670, PubMed : 36697823). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed : 22343943, PubMed : 22576015, PubMed : 22692423, PubMed : 24448649, PubMed : 32612235, PubMed : 36608670). The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization (PubMed : 34289345). MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed : 15268862, PubMed : 15467718, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed : 15268862, PubMed : 15467718, PubMed : 21376236, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed : 15467718). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed : 15718470, PubMed : 21376236, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed : 18925875). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed : 15268862). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo (PubMed : 26584640). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity).

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Post-translational modifications

Autophosphorylates when part of mTORC1 or mTORC2 (PubMed:15467718, PubMed:20022946, PubMed:9434772). Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation (PubMed:19487463). Phosphorylated at Ser-2448 by RPS6KB1 (PubMed:15899889, PubMed:15905173, PubMed:19145465). Phosphorylation in the kinase domain modulates the interactions of MTOR with RPTOR and AKT1S1/PRAS40 and leads to increased intrinsic mTORC1 kinase activity (PubMed:15905173, PubMed:19145465, PubMed:21576368). Phosphorylation at Ser-2159 by TBK1 in response to growth factors and pathogen recognition receptors promotes mTORC1 activity (PubMed:29150432). Phosphorylation at Ser-2159 by TBK1 in response to EGF growth factor promotes mTORC2 activity, leading to AKT1 phosphorylation and activation (By similarity). Phosphorylation at Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity (PubMed:24247430).. Ubiquitinated at Lys-2066 by the SCF(FBXO22) complex via 'Lys-27'-linked ubiquitination prevents mTORC1 substrate recruitment.

Subcellular localisation

Lysosome membrane

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Product protocols

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Target data

Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed : 12087098, PubMed : 12150925, PubMed : 12150926, PubMed : 12231510, PubMed : 12718876, PubMed : 14651849, PubMed : 15268862, PubMed : 15467718, PubMed : 15545625, PubMed : 15718470, PubMed : 18497260, PubMed : 18762023, PubMed : 18925875, PubMed : 20516213, PubMed : 20537536, PubMed : 21659604, PubMed : 23429703, PubMed : 23429704, PubMed : 25799227, PubMed : 26018084, PubMed : 29150432, PubMed : 29236692, PubMed : 31112131, PubMed : 31601708, PubMed : 32561715, PubMed : 34519269, PubMed : 37751742). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed : 15268862, PubMed : 15467718, PubMed : 17517883, PubMed : 18372248, PubMed : 18497260, PubMed : 18925875, PubMed : 20516213, PubMed : 21576368, PubMed : 21659604, PubMed : 23429704, PubMed : 30171069, PubMed : 29236692, PubMed : 37751742). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed : 15268862, PubMed : 15467718, PubMed : 18497260, PubMed : 18925875, PubMed : 20516213, PubMed : 21576368, PubMed : 21659604, PubMed : 23429704, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed : 12087098, PubMed : 12150925, PubMed : 12150926, PubMed : 12231510, PubMed : 12718876, PubMed : 14651849, PubMed : 15268862, PubMed : 15467718, PubMed : 15545625, PubMed : 15718470, PubMed : 18497260, PubMed : 18762023, PubMed : 18925875, PubMed : 20516213, PubMed : 20537536, PubMed : 21659604, PubMed : 23429703, PubMed : 23429704, PubMed : 25799227, PubMed : 26018084, PubMed : 29150432, PubMed : 29236692, PubMed : 31112131, PubMed : 34519269). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed : 24403073, PubMed : 29236692). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed : 12087098, PubMed : 12150925, PubMed : 18925875, PubMed : 29150432, PubMed : 29236692). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed : 23429703, PubMed : 23429704). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed : 20516213). Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation (PubMed : 36691768). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (PubMed : 23426360). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways : negatively regulates autophagy through phosphorylation of ULK1 (PubMed : 32561715). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed : 32561715). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed : 20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed : 30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed : 23524951, PubMed : 25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed : 21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed : 12231510). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed : 12150925, PubMed : 12150926, PubMed : 24403073, PubMed : 31695197). The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation (PubMed : 22343943, PubMed : 22576015, PubMed : 22692423, PubMed : 24448649, PubMed : 32612235, PubMed : 36608670, PubMed : 36697823). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed : 22343943, PubMed : 22576015, PubMed : 22692423, PubMed : 24448649, PubMed : 32612235, PubMed : 36608670). The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization (PubMed : 34289345). MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed : 15268862, PubMed : 15467718, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed : 15268862, PubMed : 15467718, PubMed : 21376236, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957, PubMed : 35926713). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed : 15467718). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed : 15718470, PubMed : 21376236, PubMed : 24670654, PubMed : 29424687, PubMed : 29567957). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed : 18925875). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed : 15268862). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo (PubMed : 26584640). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity).
See full target information MTOR

Additional targets

RPTOR,MLST8
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