Huntingtin-interacting protein 1 (HIP1)

Huntingtin-interacting protein 1 (HIP1) is a multidomain cytoplasmic protein that plays a key role as an accessory factor in **clathrin-mediated endocytosis**, where it dynamically associates with clathrin at the plasma membrane and is involved in the formation and maturation of coated vesicles[2][3]. Structurally, it contains an N-terminal ENTH (Epsin N-terminal homology) domain, a central coiled-coil region, and a C-terminal actin-binding domain, facilitating its interactions with the plasma membrane, clathrin-coated pits, and the actin cytoskeleton[3]. HIP1 is also known to interact with huntingtin protein, and its dissociation from huntingtin is implicated in the pathogenesis of Huntington’s disease, triggering downstream apoptotic pathways via the recruitment of HIPPI and activation of caspase-8[1]. It has been shown that HIP1 is essential for proper vesicle trafficking and endocytosis, and dysregulation of its function may contribute to neurodegeneration and possibly cancer due to altered cell survival signaling[1][2][3]. No clinically approved drugs are currently known to directly target HIP1, nor is it established as a routine biomarker or direct therapeutic target.

Other names

HIP1HIP-1HIP-IILWEQHuntingtin-interacting protein ISHONSHONbetaSHONgamma