Cullin-associated NEDD8-dissociated protein 1 (CAND1)

Cullin-associated NEDD8-dissociated protein 1 (CAND1) is an essential regulator of cullin-RING ubiquitin ligases (CRLs), particularly the SCF (Skp1–Cullin1–F-box protein) E3 ligase complexes responsible for targeted protein ubiquitination and proteasomal degradation. CAND1 acts as a "substrate receptor exchange factor," binding to unneddylated cullin scaffolds and displacing the Skp1–F-box protein complex, thereby recycling the cullin scaffold and allowing exchange for new F-box substrate receptors. This process is critical for protein homeostasis, timely cell cycle progression, and cellular adaptation to changing substrate pools. CAND1 dysfunction impairs proteostasis, leading to defective development, increased cell death in certain contexts, and is linked to various human diseases including cancer, metabolic, and cardiovascular disorders. No direct therapeutic drugs target CAND1, but its modulation is being explored for disease treatment and its altered expression is associated with several pathological states.

Other names

Cullin-associated NEDD8-dissociated protein 1CAND1KIAA0829TIP120TIP120ATBP-interacting protein 120ADKFZp434M1414p120 CAND1