Ral guanine nucleotide dissociation stimulator-like 1 (RGL1)

Ral guanine nucleotide dissociation stimulator-like 1 (RGL1) is a human protein that functions as a ras effector protein with guanine nucleotide exchange factor (GEF) activity for Ral GTPases[1][2]. It participates in Ras protein signal transduction and is involved in multiple cellular signaling cascades, including the MAPK family pathway[2]. RGL1 is thought to localize to the cytosol and plasma membrane, where it mediates signal transduction from active Ras to downstream targets such as RalB and participates in processes including regulation of cell invasion and transcriptional regulation, particularly in the context of cancer biology[1][2]. Its only closely related human paralog is RALGDS[2]. RGL1 interacts with Ras isoforms such as KRAS, and structural studies have shown it binds to KRAS via its RA (Ras association) domain, similar to other RalGDS-family proteins, forming complexes that mediate signal relay[1]. Diseases associated with RGL1 include certain optic neuropathies and metabolic disorders; it also plays a role in cancer progression associated with KRAS mutations[1][2]. Currently, there are no approved drugs known to directly target RGL1, nor are there established mechanisms of action or biomarkers related specifically to this molecule. Safety concerns specific to RGL1 as a therapeutic target have not been reported in current literature[2].

Other names

RGL1KIAA0959RGLralGDS-like 1ral guanine nucleotide dissociation stimulator-like 1