Golgi-associated ATPase Enhancer of 16 kDa (GATE-16), also known as Apg8p2 and GABARAPL2, is a 117 amino acid (aa) polypeptide and a member of the Autophagy-related 8 (Atg8) family of proteins. GATE-16/Apg8p2 is best known for its role in autophagy. GATE-16/Apg8p2 covalently attaches to phosphatidylethanolamine (PE) the phagophore (autophagosome precursor) membrane using a Ubiquitin-like conjugation system that includes Ubiquitin-activating (E1)-, Ubiquitin-conjugating (E2)-, and Ubiquitin Ligase (E3)-like enzymes. Here it is involved in the later stages of autophagosome formation. It may also be involved in cargo recruitment to autophagosomes.
This N-terminal HA-tagged Apg8 protein is a potent, irreversible and specific inhibitor of Agp8-specific isopeptidases. Apg84B activities include the processing of Apg8 precursor proteins and the removal of Apg8 proteins that are conjugated to phosphatidylethanolamine during autophagy. These processes can be inhibited by this vinyl sulfone derivative which reacts with the Apg84B active site cysteine. The HA peptide sequence (YPYDVPDYA) is derived from the influenza hemagglutin in protein. This epitope allows for the sensitive identification or purification of such deconjugating activities since it is specifically recognized by anti-HA antibodies and/or anti-HA-agarose.
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