Helicase with zinc finger domain (HELZ)

Helicase with zinc finger domain (HELZ) is a member of the superfamily 1 (SF1) RNA helicases that contains an N-terminal CCCH-type zinc finger motif and operates primarily in regulation of RNA metabolism[2]. HELZ is implicated in mRNA stability, translational repression, mRNA decay, and deadenylation, notably via direct binding to the CCR4–NOT deadenylase complex[2]. The C-terminal region of HELZ binds the NOT module within CCR4–NOT and triggers deadenylation and decapping-dependent decay of associated mRNAs[2]. HELZ can also stimulate translation and interacts with polyadenylate-binding protein 1 (PABPC1), influencing the fate of polyadenylated RNAs. HELZ is widely expressed, including during embryonic development, and regulates the abundance of transcripts involved in neurogenesis and nervous system development[2]. There is evidence for its down-regulation in various cancers, but it is not currently characterized as a direct therapeutic target, and no drugs are known to interact with this protein. Though its mechanistic functions overlap with those of canonical mRNA repressors, it is not classified as a traditional receptor or classic drug target.

Other names

HELZDRHCKIAA0054HUMORF5DHRCDown-regulated in human cancers proteinprobable helicase with zinc finger domainputative helicase with zinc finger domainhelicase with zinc fingerdown-regulated in human cancers