Golgi-associated ATPase Enhancer of 16 kDa (GATE-16), also known as GABARAPL2, is a 117 amino acid (aa) polypeptide and a member of the Autophagy-related 8 (ATG8) family of proteins (1). GATE-16 has 100% aa sequence identity with its mouse and rat orthologs, and is orthologous to the yeast ATG8. ATG8 family members show structural similarity with Ubiquitin, but lack aa sequence similarity. GATE-16 is best known for its role in autophagy (2,3). GATE-16 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 (4,5). It may also be involved in cargo recruitment to autophagosomes (1).
This is a fluorogenic substrate for ATG8-specific C-terminal hydrolases such as ATG4B (Catalog # E-400) based on the C-terminal derivatization of ATG8 with 7-amido-4-methylcoumarin (AMC). ATG8-AMC is useful for studying such enzyme activities when detection sensitivity or continuous monitoring of activity is essential. NOTE: this protein has an N-terminal HA tag.
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