RUN domain-containing protein 1 (RUNDC1)

RUN domain-containing protein 1 (RUNDC1) is a cytoplasmic protein primarily characterized by the presence of both a RUN domain and a coiled-coil domain. It serves as a negative regulator of autophagy by impeding the fusion of autophagosomes with lysosomes through modulation of SNARE complex assembly—specifically, it stabilizes the ATG14-STX17-SNAP29 complex to prevent VAMP8 association, thereby inhibiting autolysosome formation. RUNDC1 is important for cellular adaptation to nutrient-deprived conditions and has functions highly conserved from zebrafish to mammals. It has also been implicated in the regulation of p53-mediated tumor suppression. To date, RUNDC1 is not classified as a classical therapeutic target such as a receptor, enzyme, or transporter, and no direct pharmacological modulators have been described [1][3].

Other names

RUNDC1RUND1LP5161DKFZp761H0421

not currently a recognized drug target; mechanistic studies relate to its inhibition of autophagosome-lysosome fusion and regulation of protein complexes involved in autophagy