Zinc finger C3H1 domain-containing protein 1 (ZFC3H1)

Zinc finger C3H1 domain-containing protein 1 (ZFC3H1) is a large nuclear and cytosolic protein characterized by a central C3H1-type zinc finger domain, multiple coiled-coil regions, tetratricopeptide repeats (TPR), and half-TPR repeats[1][2]. It functions as a key RNA-binding molecule involved in the nuclear retention and degradation of polyadenylated RNAs, playing a vital role in quality control of RNA export by preventing the trafficking of certain RNAs to nuclear speckles and subsequently to the cytoplasm[2]. ZFC3H1 is a core component of the poly(A) tail exosome targeting (PAXT) complex, participating in RNA surveillance by promoting degradation of aberrant or excess RNAs and, upon dysfunction, forming nuclear condensates to further sequester these RNAs[2][3]. ZFC3H1 also regulates the expression of inflammatory cytokines, such as IL-8, and is a direct binding target of the small molecule immune modulator Celastramycin A[1]. Thus, ZFC3H1 serves critical roles in gene expression regulation, RNA quality control, and the modulation of inflammatory responses.

Other names

CCDC131KIAA0546PSRC2MGC23401CSRC2Coiled-coil domain-containing protein 131Proline/serine-rich coiled-coil protein 2

Binding of small molecule (Celastramycin A) to ZFC3H1 inhibits IL-8 transcription by interfering with its function in inflammatory signaling[1]