Cullin-associated NEDD8-dissociated protein 2 (CAND2)

Cullin-associated NEDD8-dissociated protein 2 (CAND2) is a regulatory protein predominantly found in mammals, with tissue enrichment in cardiac and skeletal muscle cells. It is a homolog of CAND1 and functions by binding to Cullin-1, facilitating the dynamic exchange of F-box proteins in the SCF (SKP1–CUL1–F-box protein) E3 ubiquitin ligase complexes, thereby promoting selective protein degradation within the cell. CAND2 is less globally efficient than CAND1 but is selectively important in specific tissues. Its disruption modifies the turnover of hundreds of proteins, impacting cellular and organismal health, with genetic links to heart disease and metabolic disorders. The protein’s molecular mechanism, expression patterns, and disease associations suggest roles as a risk modifier and candidate biomarker, but as of now there are no approved drugs directly targeting CAND2.

Other names

CAND2Cullin-associated NEDD8-dissociated protein 2KIAA0667TIP120BTBP-interacting protein 120BTp120bEpididymis tissue protein Li 169p120 CAND2

Not applicable; no existing drugs known to directly target CAND2. Hypothetically, future molecules could inhibit or enhance CAND2-mediated SCF assembly, thus affecting ubiquitin-dependent protein degradation and downstream cellular signaling