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Gene Review

SIL1  -  Sil1p

Saccharomyces cerevisiae S288c

Synonyms: Nucleotide exchange factor SIL1, PER100, Protein SLS1, SLS1, YOL031C
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High impact information on SIL1

  • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum [1].
  • SIL1 is a non-essential gene but the Deltalhs1Deltasil1 double mutation is lethal and correlates with a complete block of protein translocation into the ER [1].
  • We report on the identification of Fes1p (yBR101cp) as a cytosolic homologue of Sls1p, an endoplasmic reticulum (ER) protein previously shown to act as a nucleotide exchange factor for yeast BiP (M. Kabani, J.-M. Beckerich, and C. Gaillardin, Mol. Cell. Biol. 20:6923-6934, 2000) [2].
  • Synthetic lethality was also observed with ER-associated degradation and folding-deficient kar2 mutants, strongly suggesting that Sls1p functions are not restricted to the translocation process [3].
  • Moreover, Sls1p is shown to promote the Sec63p-mediated activation of Kar2p's ATPase activity [3].

Anatomical context of SIL1

  • Sls1p was sedimented with membrane-rich organelles and was resistant to protease degradation without prior membrane solubilization [4].

Associations of SIL1 with chemical compounds

  • The yeast FES1 and SLS1 genes encode conserved nucleotide exchange factors that act on the cytoplasmic and endoplasmic reticulum luminal Hsp70s, Ssa1p and BiP, respectively [5].
  • We show that Sls1p stimulates in a dose-dependent manner the binding of ScKar2p on the lumenal J domain of Sec63p fused to glutathione S-transferase [3].

Other interactions of SIL1


Analytical, diagnostic and therapeutic context of SIL1


  1. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. Tyson, J.R., Stirling, C.J. EMBO J. (2000) [Pubmed]
  2. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Kabani, M., Beckerich, J.M., Brodsky, J.L. Mol. Cell. Biol. (2002) [Pubmed]
  3. Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Kabani, M., Beckerich, J.M., Gaillardin, C. Mol. Cell. Biol. (2000) [Pubmed]
  4. Sls1p, an endoplasmic reticulum component, is involved in the protein translocation process in the yeast Yarrowia lipolytica. Boisramé, A., Beckerich, J.M., Gaillardin, C. J. Biol. Chem. (1996) [Pubmed]
  5. HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. Kabani, M., McLellan, C., Raynes, D.A., Guerriero, V., Brodsky, J.L. FEBS Lett. (2002) [Pubmed]
  6. Interaction of Kar2p and Sls1p is required for efficient co-translational translocation of secreted proteins in the yeast Yarrowia lipolytica. Boisramé, A., Kabani, M., Beckerich, J.M., Hartmann, E., Gaillardin, C. J. Biol. Chem. (1998) [Pubmed]
  7. A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica. Kabani, M., Boisramé, A., Beckerich, J.M., Gaillardin, C. Gene (2000) [Pubmed]
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