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Leucine-rich repeat-containing protein 25 (LRRC25) is a cytosolic protein characterized by leucine-rich repeat domains. It functions as a negative regulator of key innate immune signaling pathways, including the NF-κB pathway and RIG-I-like receptor (RLR)-mediated type I interferon signaling. LRRC25 mediates the selective autophagic degradation of signal transducers such as p65/RelA (NF-κB) and RIG-I by interacting with the autophagic cargo receptor p62/SQSTM1, thus maintaining immune homeostasis and preventing excessive inflammatory responses. LRRC25 is expressed in monocytes and plasmacytoid dendritic cells, contributes to wound healing and inflammatory response, and may play roles in infectious and inflammatory diseases. Its modulation has been proposed as a novel approach for antiviral and possible anticancer therapies, but it is not currently an established therapeutic target or clinical biomarker.
Not established; LRRC25 itself is not yet a drug target for approved therapeutics but theoretically could serve as a target for small molecule modulators or biologics to regulate autophagy-dependent immune signaling
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