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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

SLI1  -  Specific language impairment QTL, 1

Homo sapiens

 
 
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High impact information on SLI1

  • SLI-1 and c-Cbl may define a new class of proteins that modify receptor tyrosine kinase-mediated signal transduction [1].
  • SLI-1 and c-Cbl share approximately 55 percent amino acid identity over a stretch of 390 residues, which includes a C3HC4 zinc-binding motif known as the RING finger, and multiple consensus binding sites for Src homology 3 (SH3) domains [1].
  • In vitro, Cbl-N directly bound to PDGFR alpha derived from PDGF-AA-stimulated cells but not to that from unstimulated cells, and this binding was abrogated by a point mutation (G306E) corresponding to a loss-of-function mutation in SLI-1 [2].
  • A point mutation in Cbl-N, G306E, corresponding to a loss-of-function mutation in the Caenorhabditis elegans Cbl homologue, SLI-1, severely compromised Cbl-N/ZAP-70 binding [3].

References

  1. Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl. Yoon, C.H., Lee, J., Jongeward, G.D., Sternberg, P.W. Science (1995) [Pubmed]
  2. Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity. Bonita, D.P., Miyake, S., Lupher, M.L., Langdon, W.Y., Band, H. Mol. Cell. Biol. (1997) [Pubmed]
  3. A novel phosphotyrosine-binding domain in the N-terminal transforming region of Cbl interacts directly and selectively with ZAP-70 in T cells. Lupher, M.L., Reedquist, K.A., Miyake, S., Langdon, W.Y., Band, H. J. Biol. Chem. (1996) [Pubmed]
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