Ribosomal protein S27-like (RPS27L)

Ribosomal protein S27-like (RPS27L) is a highly conserved protein that serves as a part of the small 40S ribosomal subunit and shares 96% sequence similarity with ribosomal protein S27. RPS27L is a direct transcriptional target of p53, is subject to MDM2-mediated ubiquitination and degradation, and acts as an important regulator of the p53-MDM2 axis. Physiologically, RPS27L orchestrates cell fate decisions following DNA damage by regulating p53 stability, enhancing p21-mediated cell cycle arrest, and protecting cells from apoptosis. It also plays a role in autophagy regulation via the mTORC1 pathway and may modulate genome stability through tetraploidy checkpoint regulation. RPS27L may have context-dependent effects in cancer—acting either as a tumor suppressor or promoter, depending on the integrity of the p53 pathway. Disruption of RPS27L can induce p53-dependent cell depletion or drive tumorigenesis when p53 is dysfunctional[1][2][3][4][5].

Other names

Ribosomal protein eS27-like40S ribosomal protein S27-likeSmall ribosomal subunit protein eS27-likeRPS27L

Not applicable (no specific drugs known to target RPS27L). Mechanistic insights suggest that altering RPS27L expression modulates p53 and cell cycle/apoptosis signaling pathways.