Abstract
The ubiquitin pathway in the cell is an elegant system for targeting unwanted proteins for degradation. Three enzymes, E1, E2, and E3, are responsible for attaching the ubiquitin tag to proteins destined to be chopped up. In their Perspective, Joazeiro and Hunter discuss new structural findings that reveal the part played by an E3 called c-Cbl in this ubiquitinating process.
MeSH terms
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Amino Acid Motifs
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Binding Sites
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Ligases / chemistry
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Ligases / metabolism*
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Models, Molecular
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Phosphorylation
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Phosphotyrosine / metabolism
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Proteins / metabolism*
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Proto-Oncogene Proteins / chemistry*
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-cbl
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Receptor Protein-Tyrosine Kinases / metabolism
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Substrate Specificity
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Ubiquitin-Conjugating Enzymes*
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Ubiquitin-Protein Ligases
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Ubiquitins / metabolism*
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src Homology Domains
Substances
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Proteins
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Proto-Oncogene Proteins
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Ubiquitins
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Phosphotyrosine
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UBE2L3 protein, human
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Ubiquitin-Conjugating Enzymes
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Proto-Oncogene Proteins c-cbl
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Ubiquitin-Protein Ligases
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Receptor Protein-Tyrosine Kinases
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Ligases
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CBL protein, human