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Gene Review

LST8  -  TOR complex subunit LST8

Saccharomyces cerevisiae S288c

Synonyms: Lethal with SEC13 protein 8, N2005, TORC subunit LST8, Target of rapamycin complex subunit LST8, YNL006W
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High impact information on LST8

  • Like tor2 mutants, lst8 mutants also have cell wall integrity defects [1].
  • Further, we show that a sublethal concentration of rapamycin mimics the Gap1p sorting defect of an lst8 mutant [1].
  • Finally, the different effects of lst8 alleles on the activation of either the Rtg1/3p or Gln3p transcription factors reveal that these two pathways constitute distinct, genetically separable outputs of the Tor-Lst8 regulatory complex [1].
  • Here we report that some mutations [lst8-(2-5)] in LST8, an essential gene encoding a seven WD40-repeat protein required for targeting of amino acid permeases (AAPs) to the plasma membrane, bypass the requirement for Rtg2p and abolish glutamate repression of RTG-dependent gene expression [2].
  • We also showed that Lst8p, a component of the TOR1/2 complexes and a negative regulator of the RTG pathway, has multiple roles in the regulation of RTG- and NCR-sensitive genes [3].

Anatomical context of LST8


Physical interactions of LST8

  • LST8 binds separately to the C-terminal kinase domain region in TOR2 and appears to modulate both the integrity and kinase activity of TORC2 [4].

Analytical, diagnostic and therapeutic context of LST8


  1. LST8 negatively regulates amino acid biosynthesis as a component of the TOR pathway. Chen, E.J., Kaiser, C.A. J. Cell Biol. (2003) [Pubmed]
  2. RTG-dependent mitochondria to nucleus signaling is negatively regulated by the seven WD-repeat protein Lst8p. Liu, Z., Sekito, T., Epstein, C.B., Butow, R.A. EMBO J. (2001) [Pubmed]
  3. Retrograde response to mitochondrial dysfunction is separable from TOR1/2 regulation of retrograde gene expression. Giannattasio, S., Liu, Z., Thornton, J., Butow, R.A. J. Biol. Chem. (2005) [Pubmed]
  4. Molecular organization of target of rapamycin complex 2. Wullschleger, S., Loewith, R., Oppliger, W., Hall, M.N. J. Biol. Chem. (2005) [Pubmed]
  5. Tor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae. Wedaman, K.P., Reinke, A., Anderson, S., Yates, J., McCaffery, J.M., Powers, T. Mol. Biol. Cell (2003) [Pubmed]
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