ATG14 Protein, Human (Myc, His)

ATG14 is essential for both basal and inducible autophagy, playing a pivotal role in determining the localization of the autophagy-specific PI3-kinase complex PI3KC3-C1. This protein contributes to autophagosome formation and MAP1LC3/LC3 conjugation to phosphatidylethanolamine while facilitating BECN1 translocation from the trans-Golgi network to autophagosomes. ATG14 enhances PIK3C3 activity in a BECN1-dependent manner and is crucial for the autophagy-dependent phosphorylation of BECN1. It stimulates BECN1 phosphorylation but suppresses PIK3C3 phosphorylation by AMPK. Additionally, ATG14 binds to the STX17-SNAP29 binary t-SNARE complex on autophagosomes, priming it for VAMP8 interaction to promote autophagosome-endolysosome fusion. Homooligomerization of ATG14 is vital for its roles in membrane tethering and enhancement of SNARE-mediated fusion. As a component of the PI3K complex I, ATG14 is associated with the catalytic subunit PIK3C3, regulatory subunit PIK3R4, and BECN1, displaying a V-shaped architecture. ATG14 interacts with various partners, including PIK3CB, BECN2, the STX17-SNAP29 binary t-SNARE complex, and NRBF2, underscoring its multifaceted involvement in autophagic processes and cellular functions. Interactions with PIK3C3 and BECN1 are influenced by the absence of TMEM39A, emphasizing the intricate regulatory network of ATG14 in autophagy.