[7] Rubicon is recruited to its sites of action through interaction with the small GTPase Rab7,[7][8] and impairs the autophagosome-lysosome fusion step of autophagy through inhibition of PI3KC3-C2 (class III phosphatidylinositol 3-kinase complex 2).

[11] Rubicon has also been shown to negatively regulate the innate immune response through direct interaction with multiple downstream regulatory molecules.

[9] This activity prevents PI3KC3-directed generation of phosphatidylinositol 3-phosphate (PI3P) at the autophagosome membrane, and a resulting failure to recruit machinery that directs autophagosome-lysosome fusion.

[12] Rubicon suppresses cytokine responses through interaction with NF-κB essential modulator (NEMO),[12] interferon regulatory factor 3 (IRF3)[14] and caspase recruitment domain-containing protein 9 (CARD9).

[10] Since reduced autophagy is associated with aging and age-related diseases, modulation of Rubicon has been identified as a potential therapeutic target.

[20] Age-dependent decline of Rubicon expression in adipose tissues may exacerbate metabolic disorders due to excessive autophagic activity.