CLINT1 (clathrin interactor 1) is an ENTH domain-containing cargo adaptor protein that functions in vesicle trafficking and membrane organization. Functionally, CLINT1 binds to phosphatidylinositol 4,5-bisphosphate (PIP2)-enriched membranes and directly recognizes SNARE proteins, particularly the H(abc) domain of Vti1b, facilitating their sorting into clathrin-coated vesicles 1. This interaction mediates bidirectional Golgi-to-endosome trafficking and stimulates clathrin assembly 2. Mechanistically, CLINT1 is phosphorylated by the kinase BIKE at threonine 294, a modification that enhances its binding to viral and cellular proteins and regulates its trafficking functions 2. Clinically, CLINT1 dysfunction is associated with multiple disease states. Loss-of-function mutations in zebrafish cause psoriasis-like phenotypes including epithelial hyperproliferation, chr5 inflammation, and impaired hemidesmosome formation 3. CLINT1 is identified as a target gene regulated by GWAS variants associated with atopic dermatitis and psoriasis 4. Additionally, CLINT1 expression is modulated in fibrotic conditions and is associated with nintedanib treatment in idiopathic pulmonary fibrosis 5. CLINT1 also plays a role in dengue virus infection by mediating viral assembly and egress through BIKE-dependent phosphorylation 2, suggesting potential significance in viral pathogenesis.