Raptor Protein Contains a Caspase-Like Domain

Trends Biochem Sci. 2004 Oct;29(10):522-4. doi: 10.1016/j.tibs.2004.08.006.

Abstract

Using state-of-the-art sequence analysis and structure-prediction methods a caspase-like domain in the N-terminal region of raptor proteins has been identified. This domain, which is characterized by the presence of invariant catalytic Cys-His dyad, is evolutionarily and structurally related to known caspases and might have protease activity. This finding suggests several unexpected aspects of raptor function in the target of rapamycin (TOR) signaling pathway.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Amino Acid Motifs*
  • Amino Acid Sequence
  • Animals
  • Caspases / chemistry*
  • Caspases / genetics
  • Caspases / metabolism
  • Catalysis
  • Cysteine / chemistry
  • Histidine / chemistry
  • Humans
  • Molecular Sequence Data
  • Peptide Hydrolases / metabolism
  • Proteins / chemistry*
  • Proteins / genetics
  • Proteins / metabolism
  • Regulatory-Associated Protein of mTOR
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Sirolimus / metabolism

Substances

  • Adaptor Proteins, Signal Transducing
  • Proteins
  • RPTOR protein, human
  • Regulatory-Associated Protein of mTOR
  • Histidine
  • Peptide Hydrolases
  • Caspases
  • Cysteine
  • Sirolimus