The screen identified copper metabolism MURR1 domaincontaining 1 (COMMD1) as a novel lamin A binding partner. Colocalization experiments using fluorescent confocal microscopy revealed that COMMD1 colocalized with lamin A in 293 cells.
This study has thus revealed a novel nuclear complex of F-actin DRR1 and COMMD1 that is involved in NF-kappaB degradation and cell cycle suppression in neuroblastoma cells.
The COMMD1 downregulation by miR-205 promotes tumor development by modulating a positive feedback loop that amplifies inflammatory- and stemness-associated properties of cancer cells.
IkappaB-alpha protein was stabilized by COMMD1 which attenuated NF-kappaB signaling during Toll-like receptor ligand and tumor necrosis factor alpha treatment and enhanced HIV-1 latency in latently HIV-1-infected cells.
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