BAIT

ATG15

AUT5, CVT17, triglyceride lipase ATG15, L000004767, L000004751, YCR068W
Lipase required for intravacuolar lysis of autophagic and Cvt bodies; targeted to intravacuolar vesicles during autophagy via the multivesicular body (MVB) pathway
Saccharomyces cerevisiae (S288c)
PREY

ATG14

APG14, CVT12, L000004763, L000004641, YBR128C
Autophagy-specific subunit of phosphatidylinositol 3-kinase complex I; Atg14p targets complex I to the phagophore assembly site (PAS); required for localizing additional ATG proteins to the PAS; required for overflow degradation of misfolded proteins when ERAD is saturated; homolog of human Barkor; other members are Vps34, Vps15, and Vps30p
Saccharomyces cerevisiae (S288c)

Phenotypic Suppression

A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Publication

A defect of the vacuolar putative lipase Atg15 accelerates degradation of lipid droplets through lipolysis.

Maeda Y, Oku M, Sakai Y

Lipid droplets (LDs) are the conserved organelles for the deposit of neutral lipids, and function as reservoirs of membrane and energy sources. To date, functional links between autophagy and LD dynamics have not been fully elucidated. Here, we report that a vacuolar putative lipase, Atg15, required for degradation of autophagic bodies, is crucial for the maintenance of LD amount in ... [more]

Autophagy Jun. 10, 2015; 0(0);0 [Pubmed: 26061644]

Throughput

  • Low Throughput

Ontology Terms

  • phenotype: chemical compound accumulation (APO:0000095)

Additional Notes

  • Deletion of macroautophagy genes suppresses deficiency of lipid droplets in atg15 cells
  • Figure 3

Curated By

  • BioGRID