Ras suppressor protein 1 (RSU1)

Ras suppressor protein 1 (RSU1) is an evolutionarily conserved, leucine-rich repeat (LRR) scaffold protein that participates in key cellular processes such as cell adhesion, migration, survival, growth inhibition, and differentiation[1][4][6][11]. RSU1 is localized at focal adhesions, where it stabilizes the PINCH1–ILK–Parvin complex (“IPP”), regulating integrin signaling and cytoskeletal dynamics[4][5][9]. Originally discovered as a suppressor of Ras-transforming activity, RSU1 modulates Ras-triggered signal transduction, frequently impacting the MAPK and JNK pathways[4]. Its role is complex in cancer, with evidence for both suppression of tumorigenesis and promotion of metastatic behavior, dependent on cellular context and isoform expression[1][2][5]. Alternative splicing of RSU1 yields truncated forms relevant to glioma pathology[1]. Despite its critical cellular role, RSU1 lacks catalytic activity and is being explored as a scaffold/adhesome target in anti-metastatic strategies, especially in liver and breast cancer settings[5]. Direct drug modulators of RSU1 are not known, but its expression and interaction partners may serve as novel biomarker or therapeutic avenues[5][11].

Other names

RSU1RSP1RSP-1Rsu-1FLJ31034Ras suppressor protein 1rsu-1

Experimental targeting approaches (anti-metastatic strategies in liver and breast cancer)[5]. Targeting RSU1 expression or RSU1–PINCH1 interaction to modulate cell adhesion and migration[1][4][5].