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IID00599
UniprotQ9BVC4
ProteinTarget of rapamycin complex subunit LST8
GeneMLST8
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
326
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-326 Hetero trimer : IID00598Complex,Q96B36
 Evidence X-RAY 5wby C Reference
       Region 5wby C 1-7 disorder
       Region 5wby C 8-324 order
       Region 5wby C 325-326 disorder
 Evidence X-RAY 5wby D Reference
       Region 5wby D 1-7 disorder
       Region 5wby D 8-324 order
       Region 5wby D 325-326 disorder
Seq 1-326 Hetero dimer : IID00598Complex
 Evidence X-RAY 4jsn C Reference
       Region 4jsn C 1-7 disorder
       Region 4jsn C 8-324 order
       Region 4jsn C 325-326 disorder
 Evidence X-RAY 4jsn D Reference
       Region 4jsn D 1-7 disorder
       Region 4jsn D 8-324 order
       Region 4jsn D 325-326 disorder
 Evidence X-RAY 4jsp C Reference
       Region 4jsp C 1-7 disorder
       Region 4jsp C 8-324 order
       Region 4jsp C 325-326 disorder
 Evidence X-RAY 4jsp D Reference
       Region 4jsp D 1-7 disorder
       Region 4jsp D 8-324 order
       Region 4jsp D 325-326 disorder
 Evidence X-RAY 4jsv C Reference
       Region 4jsv C 1-7 disorder
       Region 4jsv C 8-324 order
       Region 4jsv C 325-326 disorder
 Evidence X-RAY 4jsv D Reference
       Region 4jsv D 1-7 disorder
       Region 4jsv D 8-324 order
       Region 4jsv D 325-326 disorder
 Evidence X-RAY 4jsx C Reference
       Region 4jsx C 1-7 disorder
       Region 4jsx C 8-324 order
       Region 4jsx C 325-326 disorder
 Evidence X-RAY 4jsx D Reference
       Region 4jsx D 1-7 disorder
       Region 4jsx D 8-324 order
       Region 4jsx D 325-326 disorder
 Evidence X-RAY 4jt5 C Reference
       Region 4jt5 C 1-7 disorder
       Region 4jt5 C 8-323 order
 Evidence X-RAY 4jt5 D Reference
       Region 4jt5 D 1-7 disorder
       Region 4jt5 D 8-323 order
 Evidence X-RAY 4jt6 C Reference
       Region 4jt6 C 1-7 disorder
       Region 4jt6 C 8-324 order
       Region 4jt6 C 325-326 disorder
 Evidence X-RAY 4jt6 D Reference
       Region 4jt6 D 1-7 disorder
       Region 4jt6 D 8-324 order
       Region 4jt6 D 325-326 disorder
Seq 1-326 Hetero trimer : IID00598Complex,Q96B36
 Evidence X-RAY 5wbu C Reference
       Region 5wbu C 1-7 disorder
       Region 5wbu C 8-324 order
       Region 5wbu C 325-326 disorder
 Evidence X-RAY 5wbu D Reference
       Region 5wbu D 1-7 disorder
       Region 5wbu D 8-324 order
       Region 5wbu D 325-326 disorder
Seqphosphorylation
    7-7 Phosphoserine
    51-51 Phosphothreonine; by CDK1
Seqacetylation
    1-1 N-acetylmethionine
    1-1 N-acetylmethionine
 
Prediction
NeProc
Order 1-326
AlphaFold
Disorder 1-11,263-270,324-326
Order 12-262,271-323
Pfam Hmmer
PF00400 75-113 6.2e-06
PF00400 119-156 0.00073
PF00400 210-248 3e-08
Function
Function in SwissProt
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'.
Biological Process
See also
Diagram with PDB data
MTOR/MLST8/AKT1S1Crystal structure of mTOR(deltaN)-mLST8-PRAS40(alpha-helix & beta-strand) complex