Guanine nucleotide exchange factor subunit RIC1 (RIC1)

Guanine nucleotide exchange factor subunit RIC1 (RIC1) is a subunit of the Ric1-Rgp1 complex, a conserved guanine nucleotide exchange factor that activates Rab6A through catalyzing the exchange of GDP for GTP, thereby regulating membrane trafficking and organelle homeostasis, particularly at the Golgi apparatus[1][2][4]. The Ric1 protein contains two β-propeller domains and a C-terminal α-solenoid domain that interfaces with the nucleotide-binding site of Rab6, while the Rgp1 subunit has an arrestin fold that interacts with the unstructured hypervariable domain of Rab6[1][2][3]. Both Ric1 and Rgp1 are essential for Rab6 activation, and their depletion disrupts retrograde transport in cells[4]. RIC1 appears to be highly conserved across eukaryotes and is implicated in the regulation of cargo sorting and Golgi function, with emerging relevance to diseases linked to trafficking defects such as cancer and neurodegenerative disorders[1][2][4]. No direct clinical drugs or biomarkers are currently associated with RIC1 as a pharmacological target.

Other names

RIC1CIP150KIAA1432bA207C16.1Connexin-43-interacting protein of 150 kDaRAB6A-GEF complex partner protein 1Protein RIC1 homologCATIFARAB6A GEF complex partner 1

Drugs or ligands targeting RIC1 would potentially act by modulating guanine nucleotide exchange activity on Rab6A, affecting cargo trafficking and Golgi function. No drugs currently documented act via this mechanism for RIC1[1][2][4].