Function
Cullin-associated NEDD8-disassociated protein 1 (CAND1) is a protein exchange factor that accelerates the rate at which cullin1-Rbx1 equilibrates with multiple F-box proteins and thus controls the SCF ubiquitin ligase repertoire[1]. CAND1 plays a vital role in cullin-RING E3 ligase ubiquitin proteasome systems which control protein degradation.
Disease
Relevance
In plants, silencing CAND1 expression results in dwarfing, early flowering, low seed germination percentage and delayed germination[2]. CAND1 protects against cardiac hypertrophy and heart failure by inducing the degradation of calcineurin[3].
CAND1 mitigates nonalcoholic fatty liver disease[4].
Structural highlights
The 3D structure of the complex between CAND1, cullin1 and RBX as well as other 3D structures of the SCF ubiquitin E3 ligases provide a mechanism of multiprotein complex assembly that averts supply chain problems and rapidly establishes protein degradation pathways needed for cellular regulation[5].
3D structures of cullin-associated NEDD8-disassociated protein 1
CAND1 3D structures