RUN and FYVE domain-containing protein 2 (RUFY2)

RUN and FYVE domain-containing protein 2 (RUFY2) is a multidomain regulatory protein comprised of an N-terminal RUN domain, two central coiled-coil domains, and a C-terminal FYVE zinc finger domain. It is found predominantly in the cytoplasm and nucleus, where it regulates intracellular vesicle trafficking, endocytosis, and cytoskeletal network dynamics through interactions with small GTPases such as Rab33A, and potentially binds phosphatidylinositol-3-phosphate at endosomal membranes. RUFY2 participates in autophagy, is modulated by microRNAs (miR-155), and is frequently mutated in certain cancers, suggesting roles in cellular homeostasis, cancer, neurodegeneration, and immunity, although it is not yet established as a direct therapeutic target. The protein does not have transmembrane domains or signal peptides, but binds to partners via its RUN and FYVE domains and SH3-binding sites.

Other names

KIAA1537RABIP4RFLJ10063ZFYVE13Rab4-interacting protein relatedantigen MU-RMS-40.17Run- and FYVE-domain containing protein

No specific mechanisms, as no therapeutics directly target RUFY2. Regulatory modulation may be indirect, e.g., via miR-155 influencing RUFY2 expression in immune processes.