Ras and Rab interactor-like protein (RINL)

Ras and Rab interactor-like protein (RINL) is a ubiquitously expressed cytoplasmic protein characterized by a VPS9 domain essential for its guanine nucleotide exchange factor (GEF) activity toward the Rab5 subfamily of small GTPases, notably Rab5, Rab21, Rab22, and Rab31[1]. RINL stimulates the formation of GTP-bound, active forms of these GTPases, thereby facilitating intracellular membrane trafficking, especially endocytosis and early-to-late endosome dynamics[1]. Structurally, RINL shares SH2, RH, and VPS9 domains with other RIN family proteins but lacks proline-rich and Ras association domains[1]. It forms multimers or complexes with other proteins, particularly odin (Anks1a), and participates in ternary complexes leading to regulated degradation of EphA8, a receptor tyrosine kinase[1]. While not directly linked to specific diseases or therapeutic modulation, RINL is implicated in cellular pathways involved in receptor turnover and trafficking, making it a potential but as yet unrealized therapeutic target in pathways involving endocytic regulation[1]. No approved drugs directly target RINL; its research significance currently lies in fundamental cell biology and protein trafficking mechanisms.

Other names

RINLFLJ45909

Drugs would likely act by modulating its GEF activity for Rab5/Rab22 subfamily GTPases or perturbing its protein-protein interactions, but no drugs are established.