High impact information on ZNF346

• Thus, JAZ is a novel negative regulator of cell growth by positively regulating p53 [1].
• JAZ mediates G1 cell-cycle arrest and apoptosis by positively regulating p53 transcriptional activity [1].
• Now, we report that the stress of IL-3 growth factor withdrawal up-regulates JAZ expression in hematopoietic cells in association with p53 activation and induction of cell death [1].
• We previously identified JAZ as a novel zinc finger (ZF) protein by screening a murine interleukin-3 (IL-3)-dependent NFS/N1.H7 myeloid cell cDNA library [1].
• JAZ also binds to ILF3, and surprisingly, this interaction is RNA independent, even though it requires the dsRNA binding domains of ILF3 [2].

Biological context of ZNF346

• JAZ possesses an unusual dsRNA binding domain consisting of multiple C2H2 zinc fingers [2].
• Recombinant exportin-5 also stimulates nuclear export of JAZ in permeabilized cells [2].
• Exportin-5 stimulates JAZ shuttling, and gene silencing of exportin-5 reduces shuttling [2].
• Furthermore, forced expression of JAZ potently induces apoptosis in murine fibroblast cells [3].
• Thus, JAZ may belong to a class of zinc finger proteins that features dsRNA binding and may regulate cell growth via the unique dsRNA binding properties [3].

Anatomical context of ZNF346

• JAZ does not contain a classical nuclear localization signal, and in digitonin-permeabilized cells, nuclear accumulation of JAZ does not require energy or cytosol [2].

Physical interactions of ZNF346

• We found that JAZ binds to exportin-5 in a Ran-GTP- and dsRNA-dependent manner [2].

Other interactions of ZNF346

• Together, these data suggest that JAZ is exported by exportin-5 but translocates back into nuclei by a facilitated diffusion mechanism [2].

References