MLST8

Protein-coding gene in humans
MLST8
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4JSN, 4JSP, 4JSV, 4JSX, 4JT5, 4JT6, 5FLC

Identifiers
AliasesMLST8, GBL, GbetaL, LST8, POP3, WAT1, MTOR associated protein, LST8 homolog
External IDsOMIM: 612190; MGI: 1929514; HomoloGene: 6833; GeneCards: MLST8; OMA:MLST8 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for MLST8
Genomic location for MLST8
Band16p13.3Start2,204,248 bp[1]
End2,209,453 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for MLST8
Genomic location for MLST8
Band17|17 A3.3Start24,692,525 bp[2]
End24,698,052 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right hemisphere of cerebellum

  • right frontal lobe

  • prefrontal cortex

  • anterior cingulate cortex

  • muscle of thigh

  • apex of heart

  • Brodmann area 9

  • amygdala

  • nucleus accumbens

  • left testis
Top expressed in
  • granulocyte

  • neural layer of retina

  • Ileal epithelium

  • genital tubercle

  • ventricular zone

  • dentate gyrus of hippocampal formation granule cell

  • spermatocyte

  • primary visual cortex

  • muscle of thigh

  • cerebellar cortex
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein binding
  • protein serine/threonine kinase activator activity
Cellular component
  • cytoplasm
  • nucleoplasm
  • cytosol
  • TORC1 complex
  • TORC2 complex
Biological process
  • positive regulation of actin filament polymerization
  • regulation of actin cytoskeleton organization
  • regulation of GTPase activity
  • positive regulation of peptidyl-tyrosine phosphorylation
  • regulation of cellular response to heat
  • TORC1 signaling
  • positive regulation of protein serine/threonine kinase activity
  • regulation of macroautophagy
  • activation of protein kinase B activity
  • TOR signaling
  • positive regulation of TOR signaling
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

64223

56716

Ensembl

ENSG00000167965

ENSMUSG00000024142

UniProt

Q9BVC4

Q9DCJ1

RefSeq (mRNA)
NM_001199173
NM_001199174
NM_001199175
NM_022372
NM_001352057

NM_001352059
NM_001352060

NM_001252463
NM_001252464
NM_001252465
NM_019988

RefSeq (protein)
NP_001186102
NP_001186103
NP_001186104
NP_071767
NP_001338986

NP_001338988
NP_001338989

NP_001239392
NP_001239393
NP_001239394
NP_064372

Location (UCSC)Chr 16: 2.2 – 2.21 MbChr 17: 24.69 – 24.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Target of rapamycin complex subunit LST8, also known as mammalian lethal with SEC13 protein 8 (mLST8) or TORC subunit LST8 or G protein beta subunit-like (GβL or Gable), is a protein that in humans is encoded by the MLST8 (MTOR associated protein, LST8 homolog) gene.[5] It is a subunit of both mTORC1 and mTORC2, complexes that regulate cell growth and survival in response to nutrient, energy, redox, and hormonal signals.[6] It is upregulated in several human colon and prostate cancer cell lines and tissues. Knockdown of mLST8 prevented mTORC formation and inhibited tumor growth and invasiveness.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167965 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024142 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Entrez Gene: MTOR associated protein".
  6. ^ "UniProtKB – Q9BVC4 (LST8_HUMAN)".
  7. ^ Kakumoto K, Ikeda J, Okada M, Morii E, Oneyama C (23 Apr 2015). "mLST8 Promotes mTOR-Mediated Tumor Progression". PLOS ONE. 10 (4): e0119015. Bibcode:2015PLoSO..1019015K. doi:10.1371/journal.pone.0119015. PMC 4408021. PMID 25906254.

Further reading

  • Ali SM, Sabatini DM (2005). "Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site". J. Biol. Chem. 280 (20): 19445–8. doi:10.1074/jbc.C500125200. PMID 15809305.
  • Rodgers BD, Levine MA, Bernier M, Montrose-Rafizadeh C (2001). "Insulin regulation of a novel WD-40 repeat protein in adipocytes". J. Endocrinol. 168 (2): 325–32. doi:10.1677/joe.0.1680325. PMID 11182770.
  • Long X, Lin Y, Ortiz-Vega S, et al. (2005). "Rheb binds and regulates the mTOR kinase". Curr. Biol. 15 (8): 702–13. Bibcode:2005CBio...15..702L. doi:10.1016/j.cub.2005.02.053. PMID 15854902. S2CID 3078706.
  • Kaizuka T, Hara T, Oshiro N, et al. (2010). "Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly". J. Biol. Chem. 285 (26): 20109–16. doi:10.1074/jbc.M110.121699. PMC 2888423. PMID 20427287.
  • Loewith R, Jacinto E, Wullschleger S, et al. (2002). "Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control". Mol. Cell. 10 (3): 457–68. doi:10.1016/S1097-2765(02)00636-6. PMID 12408816.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Sarbassov DD, Sabatini DM (2005). "Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex". J. Biol. Chem. 280 (47): 39505–9. doi:10.1074/jbc.M506096200. PMID 16183647.
  • Oshiro N, Yoshino K, Hidayat S, et al. (2004). "Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function". Genes Cells. 9 (4): 359–66. doi:10.1111/j.1356-9597.2004.00727.x. hdl:20.500.14094/D1002969. PMID 15066126. S2CID 24814691.
  • Inoki K, Ouyang H, Li Y, Guan KL (2005). "Signaling by target of rapamycin proteins in cell growth control". Microbiol. Mol. Biol. Rev. 69 (1): 79–100. doi:10.1128/MMBR.69.1.79-100.2005. PMC 1082789. PMID 15755954.
  • Behrends C, Sowa ME, Gygi SP, Harper JW (2010). "Network organization of the human autophagy system". Nature. 466 (7302): 68–76. Bibcode:2010Natur.466...68B. doi:10.1038/nature09204. PMC 2901998. PMID 20562859.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Kawai S, Enzan H, Hayashi Y, et al. (2003). "Vinculin: a novel marker for quiescent and activated hepatic stellate cells in human and rat livers". Virchows Arch. 443 (1): 78–86. doi:10.1007/s00428-003-0804-4. PMID 12719976. S2CID 21552704.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Kim DH, Sarbassov DD, Ali SM, et al. (2003). "GbetaL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR". Mol. Cell. 11 (4): 895–904. doi:10.1016/S1097-2765(03)00114-X. PMID 12718876.
  • Jacinto E, Loewith R, Schmidt A, et al. (2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive". Nat. Cell Biol. 6 (11): 1122–8. doi:10.1038/ncb1183. PMID 15467718. S2CID 13831153.
  • Sarbassov DD, Guertin DA, Ali SM, Sabatini DM (2005). "Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex". Science. 307 (5712): 1098–101. Bibcode:2005Sci...307.1098S. doi:10.1126/science.1106148. PMID 15718470. S2CID 45837814.


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