Recombinant human mTOR + MLST8 + Raptor protein is a Human Fragment protein, in the 1362 to 2549 aa range, expressed in Baculovirus infected Sf9, with >50% purity and suitable for SDS-PAGE, FuncS.
Images
Key facts
- Purity
- >50% SDS-PAGE
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- DDDDK tag N-Terminus His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Sequence
This product is comprised of multiple sequences see
Amino acid sequence 1
E F M E H S D K G P L P L R D D N G I V L L G E R A A K C R A Y A K A L H Y K E L E F Q K G P T P A I L E S L I S I N N K L Q Q P E A A A G V L E Y A M K H F G E L E I Q A T W Y E K L H E W E D A L V A Y D K K M D T N K D D P E L M L G R M R C L E A L G E W G Q L H Q Q C C E K W T L V N D E T Q A K M A R M A A A A A W G L G Q W D S M E E Y T C M I P R D T H D G A F Y R A V L A L H Q D L F S L A Q Q C I D K A R D L L D A E L T A M A G E S Y S R A Y G A M V S C H M L S E L E E V I Q Y K L V P E R R E I I R Q I W W E R L Q G C Q R I V E D W Q K I L M V R S L V V S P H E D M R T W L K Y A S L C G K S G R L A L A H K T L V L L L G V D P S R Q L D H P L P T V H P Q V T Y A Y M K N M W K S A R K I D A F Q H M Q H F V Q T M Q Q Q A Q H A I A T E D Q Q H K Q E L H K L M A R C F L K L G E W Q L N L Q G I N E S T I P K V L Q Y Y S A A T E H D R S W Y K A W H A W A V M N F E A V L H Y K H Q N Q A R D E K K K L R H A S G A N I T N A T T A A T T A A T A T T T A S T E G S N S E S E A E S T E N S P T P S P L Q K K V T E D L S K T L L M Y T V P A V Q G F F R S I S L S R G N N L Q D T L R V L T L W F D Y G H W P D V N E A L V E G V K A I Q I D T W L Q V I P Q L I A R I D T P R P L V G R L I H Q L L T D I G R Y H P Q A L I Y P L T V A S K S T T T A R H N A A N K I L K N M C E H S N T L V Q Q A M M V S E E L I R V A I L W H E M W H E G L E E A S R L Y F G E R N V K G M F E V L E P L H A M M E R G P Q T L K E T S F N Q A Y G R D L M E A Q E W C R K Y M K S G N V K D L T Q A W D L Y Y H V F R R I S K Q L P Q L T S L E L Q Y V S P K L L M C R D L E L A V P G T Y D P N Q P I I R I Q S I A P S L Q V I T S K Q R P R K L T L M G S N G H E F V F L L K G H E D L R Q D E R V M Q L F G L V N T L L A N D P T S L R K N L S I Q R Y A V I P L S T N S G L I G W V P H C D T L H A L I R D Y R E K K K I L L N I E H R I M L R M A P D Y D H L T L M Q K V E V F E H A V N N T A G D D L A K L L W L K S P S S E V W F D R R T N Y T R S L A V M S M V G Y I L G L G D R H P S N L M L D R L S G K I L H I D F G D C F E V A M T R E K F P E K I P F R L T R M L T N A M E V T G L D G N Y R I T C H T V M E V L R E H K D S V M A V L E A F V Y D P L L N W R L M D T N T K G N K R S R T R T D S Y S A G Q S V E I L D G V E L G E P A H K K T G T T V P E S I H S F I G D G L V K P E A L N K K A I Q I I N R V R D K L T G R D F S H D D T L D V P T Q V E L L I K Q A T S H E N L C Q C Y I G W C P F W
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
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: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). 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 may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). mTORC2 plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (PubMed:15718470). 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). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). 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).
Additional Targets
RPTOR, MLST8
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, mTOR
Recommended products
Recombinant human mTOR + MLST8 + Raptor protein is a Human Fragment protein, in the 1362 to 2549 aa range, expressed in Baculovirus infected Sf9, with >50% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >50% SDS-PAGE
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- DDDDK tag N-Terminus His tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- 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
- P42345-1
- Animal free
- No
- Species
- Human
- Concentration
- Storage buffer
pH: 8
Constituents: 10% Glycerol (glycerin, glycerine), 0.72% Sodium chloride, 0.71% Tris HCl, 0.02% Potassium chloride
Sequence info
Amino acid sequence 1
- E F M E H S D K G P L P L R D D N G I V L L G E R A A K C R A Y A K A L H Y K E L E F Q K G P T P A I L E S L I S I N N K L Q Q P E A A A G V L E Y A M K H F G E L E I Q A T W Y E K L H E W E D A L V A Y D K K M D T N K D D P E L M L G R M R C L E A L G E W G Q L H Q Q C C E K W T L V N D E T Q A K M A R M A A A A A W G L G Q W D S M E E Y T C M I P R D T H D G A F Y R A V L A L H Q D L F S L A Q Q C I D K A R D L L D A E L T A M A G E S Y S R A Y G A M V S C H M L S E L E E V I Q Y K L V P E R R E I I R Q I W W E R L Q G C Q R I V E D W Q K I L M V R S L V V S P H E D M R T W L K Y A S L C G K S G R L A L A H K T L V L L L G V D P S R Q L D H P L P T V H P Q V T Y A Y M K N M W K S A R K I D A F Q H M Q H F V Q T M Q Q Q A Q H A I A T E D Q Q H K Q E L H K L M A R C F L K L G E W Q L N L Q G I N E S T I P K V L Q Y Y S A A T E H D R S W Y K A W H A W A V M N F E A V L H Y K H Q N Q A R D E K K K L R H A S G A N I T N A T T A A T T A A T A T T T A S T E G S N S E S E A E S T E N S P T P S P L Q K K V T E D L S K T L L M Y T V P A V Q G F F R S I S L S R G N N L Q D T L R V L T L W F D Y G H W P D V N E A L V E G V K A I Q I D T W L Q V I P Q L I A R I D T P R P L V G R L I H Q L L T D I G R Y H P Q A L I Y P L T V A S K S T T T A R H N A A N K I L K N M C E H S N T L V Q Q A M M V S E E L I R V A I L W H E M W H E G L E E A S R L Y F G E R N V K G M F E V L E P L H A M M E R G P Q T L K E T S F N Q A Y G R D L M E A Q E W C R K Y M K S G N V K D L T Q A W D L Y Y H V F R R I S K Q L P Q L T S L E L Q Y V S P K L L M C R D L E L A V P G T Y D P N Q P I I R I Q S I A P S L Q V I T S K Q R P R K L T L M G S N G H E F V F L L K G H E D L R Q D E R V M Q L F G L V N T L L A N D P T S L R K N L S I Q R Y A V I P L S T N S G L I G W V P H C D T L H A L I R D Y R E K K K I L L N I E H R I M L R M A P D Y D H L T L M Q K V E V F E H A V N N T A G D D L A K L L W L K S P S S E V W F D R R T N Y T R S L A V M S M V G Y I L G L G D R H P S N L M L D R L S G K I L H I D F G D C F E V A M T R E K F P E K I P F R L T R M L T N A M E V T G L D G N Y R I T C H T V M E V L R E H K D S V M A V L E A F V Y D P L L N W R L M D T N T K G N K R S R T R T D S Y S A G Q S V E I L D G V E L G E P A H K K T G T T V P E S I H S F I G D G L V K P E A L N K K A I Q I I N R V R D K L T G R D F S H D D T L D V P T Q V E L L I K Q A T S H E N L C Q C Y I G W C P F W
- Accession
- P42345
- Protein length
- Fragment
- Predicted molecular weight
- 137 kDa
- Amino acids
- 1362 to 2549
- Nature
- Recombinant
- Tags
- DDDDK tag N-Terminus
Amino acid sequence 2
- E S E M L Q S P L L G L G E E D E A D L T D W N L P L A F M K K R H C E K I E G S K S L A Q S W R M K D R M K T V S V A L V L C L N V G V D P P D V V K T T P C A R L E C W I D P L S M G P Q K A L E T I G A N L Q K Q Y E N W Q P R A R Y K Q S L D P T V D E V K K L C T S L R R N A K E E R V L F H Y N G H G V P R P T V N G E V W V F N K N Y T Q Y I P L S I Y D L Q T W M G S P S I F V Y D C S N A G L I V K S F K Q F A L Q R E Q E L E V A A I N P N H P L A Q M P L P P S M K N C I Q L A A C E A T E L L P M I P D L P A D L F T S C L T T P I K I A L R W F C M Q K C V S L V P G V T L D L I E K I P G R L N D R R T P L G E L N W I F T A I T D T I A W N V L P R D L F Q K L F R Q D L L V A S L F R N F L L A E R I M R S Y N C T P V S S P R L P P T Y M H A M W Q A W D L A V D I C L S Q L P T I I E E G T A F R H S P F F A E Q L T A F Q V W L T M G V E N R N P P E Q L P I V L Q V L L S Q V H R L R A L D L L G R F L D L G P W A V S L A L S V G I F P Y V L K L L Q S S A R E L R P L L V F I W A K I L A V D S S C Q A D L V K D N G H K Y F L S V L A D P Y M P A E H R T M T A F I L A V I V N S Y H T G Q E A C L Q G N L I A I C L E Q L N D P H P L L R Q W V A I C L G R I W Q N F D S A R W C G V R D S A H E K L Y S L L S D P I P E V R C A A V F A L G T F V G N S A E R T D H S T T I D H N V A M M L A Q L V S D G S P M V R K E L V V A L S H L V V Q Y E S N F C T V A L Q F I E E E K N Y A L P S P A T T E G G S L T P V R D S P C T P R L R S V S S Y G N I R A V A T A R S L N K S L Q N L S L T E E S G G A V A F S P G N L S T S S S A S S T L G S P E N E E H I L S F E T I D K M R R A S S Y S S L N S L I G V S F N S V Y T Q I W R V L L H L A A D P Y P E V S D V A M K V L N S I A Y K A T V N A R P Q R V L D T S S L T Q S A P A S P T N K G V H I H Q A G G S P P A S S T S S S S L T N D V A K Q P V S R D L P S G R P G T T G P A G A Q Y T P H S H Q F P R T R K M F D K G P E Q T A D D A D D A A G H K S F I S A T V Q T G F C D W S A R Y F A Q P V M K I P E E H D L E S Q I R K E R E W R F L R N S R V R R Q A Q Q V I Q K G I T R L D D Q I F L N R N P G V P S V V K F H P F T P C I A V A D K D S I C F W D W E K G E K L D Y F H N G N P R Y T R V T A M E Y L N G Q D C S L L L T A T D D G A I R V W K N F A D L E K N P E M V T A W Q G L S D M L P T T R G A G M V V D W E Q E T G L L M S S G D V R I V R I W D T D R E M K V Q D I P T G A D S C V T S L S C D S H R S L I V A G L G D G S I R V Y D R R M A L S E C R V M T Y R E H T A W V V K A S L Q K R P D G H I V S V S V N G D V R I F D P R M P E S V N V L Q I V K G L T A L D I H P Q A D L I A C G S V N Q F T A I Y N S S G E L I N N I K Y Y D G F M G Q R V G A I S C L A F H P H W P H L A V G S N D Y Y I S V Y S V E K R V R
- Accession
- Q8N122
- Protein length
- Full Length
- Predicted molecular weight
- 150 kDa
- Amino acids
- 2 to 1335
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Amino acid sequence 3
- N T S P G T V G S D P V I L A T A G Y D H T V R F W Q A H S G I C T R T V Q H Q D S Q V N A L E V T P D R S M I A A A G Y Q H I R M Y D L N S N N P N P I I S Y D G V N K N I A S V G F H E D G R W M Y T G G E D C T A R I W D L R S R N L Q C Q R I F Q V N A P I N C V C L H P N Q A E L I V G D Q S G A I H I W D L K T D H N E Q L I P E P E V S I T S A H I D P D A S Y M A A V N S T G N C Y V W N L T G G I G D E V T Q L I P K T K I P A H T R Y A L Q C R F S P D S T L L A T C S A D Q T C K I W R T S N F S L M T E L S I K S G N P G E S S R G W M W G C A F S G D S Q Y I V T A S S D N L A R L W C V E T G E I K R E Y G G H Q K A V V C L A F N D S V L G
- Accession
- Q9BVC4
- Protein length
- Full Length
- Predicted molecular weight
- 37 kDa
- Amino acids
- 2 to 326
- Nature
- Recombinant
- Tags
- His tag N-Terminus
Specifications
- Form
- Liquid
- Additional notes
Affinity purified.
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: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). 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 may regulate other cellular processes including survival and organization of the cytoskeleton (PubMed:15268862, PubMed:15467718). mTORC2 plays a critical role in the phosphorylation at 'Ser-473' of AKT1, a pro-survival effector of phosphoinositide 3-kinase, facilitating its activation by PDK1 (PubMed:15718470). 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). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). 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:9434772). Phosphorylation at Ser-1261, Ser-2159 and Thr-2164 promotes autophosphorylation (PubMed:19487463). 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 Thr-2173 in the ATP-binding region by AKT1 strongly reduces kinase activity (PubMed:24247430).
- Subcellular localisation
- Mitochondrion outer membrane, Lysosome, Nucleus, PML body, Lysosome membrane
Storage
- 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
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Notes
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.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
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.
- Associated diseases and disorders
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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2 product images
SDS-PAGE - Recombinant human mTOR + MLST8 + Raptor protein (ab196074)
10% SDS-PAGE analysis of 3 μg ab196074 with Coomassie staining.
Functional Studies - Recombinant human mTOR + MLST8 + Raptor protein (ab196074)
Activity assay using ab196074.
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