Protein function and interaction

RQCD1 was identified as part of the CCR4–NOT transcription complex. CCR4-NOT is an evolutionarily conserved complex known to be involved in mRNA transcription and degradation (Chen et al., 2001 PMID: 11733989). A yeast two-hybrid screen identified the interaction between RCD1 and NIF-1 (NRC-interacting factor). This interaction potentiates nuclear receptor activity (Garapaty et al., 2008 PMID: 18180299).

RQCD1 acts as a transcriptional cofactor that mediates retinoic acid-induced cell differentiation. RCD1 was identified as a component of the DRF transcriptional complex, which consists of p300/CBP, ATF-2, and retinoic acid (Hiroi et al., 2002 PMID: 12356739 by similarity).

GST-pull down assay and co-immunoprecipitation assays showed the interaction of RQCD1 with Grb10 interacting GYF protein 1 (GIGYF1) and 2 (GIGYF2) proteins, which have critical roles in phosphatidylinositol-3-kinase (PI3K)/Akt signaling pathway (Ajiro et al., 2009 PMID: 19724902).

RQCD1 shows “in vitro” nucleic acid binding properties (Garces et al., 2007 PMID: 17189474).