GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
PMID:10508157
| Citation |
Shintani, T, Mizushima, N, Ogawa, Y, Matsuura, A, Noda, T and Ohsumi, Y (1999) Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast. EMBO J. 18:5234-41 |
|---|---|
| Abstract |
Autophagy is a cellular process for bulk degradation of cytoplasmic components. The attachment of Apg12p, a modifier with no significant similarity to ubiquitin, to Apg5p is crucial for autophagy in yeast. This reaction proceeds in a ubiquitination-like manner, and requires Apg7p and Apg10p. Apg7p exhibits a considerable similarity to ubiquitin-activating enzyme (E1) and is found to activate Apg12p with ATP hydrolysis. Apg10p, on the other hand, shows no significant similarity to other proteins whose functions are known. Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester. Cells expressing Apg10p(C133S) do not generate the Apg12p-Apg5p conjugate, which leads to defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase I. These findings indicate that Apg10p is a new type of protein-conjugating enzyme that functions in the Apg12p-Apg5p conjugation pathway. |
| Links |
PubMed PMC1171594 Online version:10.1093/emboj/18.19.5234 |
| Keywords |
Amino Acid Sequence; Autophagy; Base Sequence; Cloning, Molecular; Cysteine/metabolism; DNA Primers; Fungal Proteins/chemistry; Fungal Proteins/genetics; Fungal Proteins/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/physiology |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| edit table |
See also
References
See Help:References for how to manage references in GONUTS.
