Run domain Beclin-1-interacting and cysteine-rich domain-containing protein (Rubicon) also known as Beclin-1 associated RUN domain containing protein (Baron) or KIAA0226, is a negative regulator of endosomes maturation and endocytic trafficking.1-2 Rubicon knockdown studies showed enhanced autophagosome maturation and endocytosis.1 It also have a critical role in the LC3-associated phagocytosis (LAP) a noncanonical autophagy process which can be induced through the activation of extracellular receptor by different stimulators including pathogens, immune complexes and dying cells.4-5
Synonyms: Beclin-1 associated RUN domain containing protein; KIAA0226; RUBCN; Run domain Beclin-1-interacting and cysteine-rich domain-containing protein; SCAR15
Storage: -20C
Application: The antibody may be used in various immunochemical techniques including Immunoblotting and Immunofluorescence. Detection of the Rubicon band by Immunoblotting is specifically inhibited by the immunogen.
Biochem Physiol Actions: The mammalian class III phosphatidylinositol 3-kinase (PtdIns3K) complex consists of three core proteins, catalytic VPS34, the adaptor VPS15 (p150) and the recruiter Beclin-1 (ATG6); these endocytosis regulators were reported to stably bind Beclin-1 ATG14, UVRAG and Rubicon.1-3 The complex Rubicon-UVRAG–Beclin-1/PtdIns3K can be found both in early and in late endosomes or lysosomes. Rubicon was described as the mediator for the recruitment of the UVRAG-Beclin-1-VPS34 complex and of ATG7 and LC3-II LAPosome.4-5 Furthermore, Rubicon has been identified as a key modulator of the inflammatory response and viral replication, during several viral infections such as hepatitis B virus (HBV). Rubicon expression is induced in negative regulation of the innate immune response resulting in enhances viral replication and possibly supporting viral immune evasion mechanism.4