High impact information on ATG14

• Although Vps30p is known to interact with Apg14p, its precise role remains unclear [1].
• The localization of these components to the PAS was Atg14p dependent but not dependent on Vps38p [2].
• Atg14p is only integrated into complex I, likely facilitating the function of complex I in autophagy [2].
• Conversely, localization of these proteins to endosomes required Vps38p but not Atg14p [2].
• Atg14p localized to pre-autophagosomal structure (PAS) and vacuolar membranes, whereas Vps38p, a component specific to complex II, localized to endosomes and vacuolar membranes [2].

Biological context of ATG14

• We found that overproduction of Apg14p partially reversed the defect in autophagy induced by the apg6-1 mutation [3].
• To identify other genes under the control of Gln3p, we searched for the Gln3p-binding GATAA motifs within 500 base pairs of the promoter sequences upstream of the yeast open reading frames in the Saccharomyces Genome Database. APG14, a gene essential for autophagy, was found to have the most GATAA motifs [4].

Physical interactions of ATG14

• Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex [3].

Other interactions of ATG14

• Subcellular fractionation indicated that Apg14p and Apg6p peripherally associated with a membrane structure(s) [3].
• The expression of APG14 is dependent on Gln3p; deletion of Gln3p severely reduced its induction by rapamycin, whereas depletion of Ure2p caused its constitutive expression [4].

References