High impact information on ATG13

• This Apg1-Apg13 association is required for autophagy, but not for the cytoplasm-to-vacuole targeting (Cvt) pathway, another vesicular transport mechanism in which factors essential for autophagy (Apg proteins) are also employed under vegetative growth conditions [1].
• We also find that dephosphorylation of Apg13p, a signal transduction event that correlates with the onset of autophagy, is also independent of new protein synthesis [2].
• Taken together, these results indicate that Atg17-Atg13 complex formation plays an important role in normal autophagosome formation via binding to and activating the Atg1 kinase [3].
• Apg13p and Vac8p are part of a complex of phosphoproteins that are required for cytoplasm to vacuole targeting [4].
• Subcellular fractionation of API indicates that Vac8p and Apg13p are involved in the vesicle formation step of the Cvt pathway [4].

Biological context of ATG13

• In vivo phosphorylation experiments demonstrate that both Vac8p and Apg13p are phosphorylated proteins, and Apg13p phosphorylation is regulated by changing nutrient conditions [4].

Physical interactions of ATG13

• Vac8p and Apg13p may be part of a larger protein complex that includes Apg1p and additional interacting proteins [4].

Other interactions of ATG13

• Subcellular fractionation experiments indicate that Apg13p and a fraction of Apg1p are membrane-associated [4].

Analytical, diagnostic and therapeutic context of ATG13

• We have identified a protein-protein interaction between Vac8p and Apg13p by both two-hybrid and co-immunoprecipitation analysis [4].

References