BAIT

ATG8

APG8, AUT7, CVT5, ubiquitin-like protein ATG8, L000004607, L000004604, YBL078C
Component of autophagosomes and Cvt vesicles; regulator of Atg1p, targets it to autophagosomes; binds the Atg1p-Atg13p complex, triggering its vacuolar degradation; unique ubiquitin-like protein whose conjugation target is lipid phosphatidylethanolamine (PE); Atg8p-PE is anchored to membranes, is involved in phagophore expansion, and may mediate membrane fusion during autophagosome formation; deconjugation of Atg8p-PE is required for efficient autophagosome biogenesis
Saccharomyces cerevisiae (S288c)
PREY

TBC1D5

TBC1 domain family, member 5
Autophagy Project
Parkinson's Disease Project
Homo sapiens

Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

An inter-species protein-protein interaction network across vast evolutionary distance.

Zhong Q, Pevzner SJ, Hao T, Wang Y, Mosca R, Menche J, Taipale M, TaÅŸan M, Fan C, Yang X, Haley P, Murray RR, Mer F, Gebreab F, Tam S, MacWilliams A, Dricot A, Reichert P, Santhanam B, Ghamsari L, Calderwood MA, Rolland T, Charloteaux B, Lindquist S, Barabasi AL, Hill DE, Aloy P, Cusick ME, Xia Y, Roth FP, Vidal M

In cellular systems, biophysical interactions between macromolecules underlie a complex web of functional interactions. How biophysical and functional networks are coordinated, whether all biophysical interactions correspond to functional interactions, and how such biophysical-versus-functional network coordination is shaped by evolutionary forces are all largely unanswered questions. Here, we investigate these questions using an "inter-interactome" approach. We systematically probed the yeast and ... [more]

Mol. Syst. Biol. Apr. 22, 2016; 12(4);865 [Pubmed: 27107014]

Throughput

  • High Throughput

Curated By

  • BioGRID