Cleavage stimulation factor subunit 2 (CSTF2, also known as CstF-64) is a member of cleavage stimulation factor complex (CSTF), which is necessary for efficient and accurate polyadenylation of most mRNAs. It is necessary for correct histone mRNA 3' end processing as well as maintenance of pluripotency in mouse embryonic stem cells []. In response to epidermal growth factor (EGF), it serves as a major regulator of 3'UTR shortening [].
The C-terminal section of cleavage stimulation and termination factor CstF-64 (CSTF2) and its yeast orthologue Rna15 form a discrete structure that is crucial for mRNA 3'-end processing []. This domain interacts with Pcf11 and possibly PC4, thus linking CSTF2 to transcription, transcriptional termination, and cell growth [].
The C-terminal section of cleavage stimulation and termination factor CstF-64 (CSTF2) and its yeast orthologue Rna15 form a discreet structure that is crucial for mRNA 3'-end processing []. This domain interacts with Pcf11 and possibly PC4, thus linking CSTF2 to transcription, transcriptional termination, and cell growth [].Proteins containing this domain also include Pti1 protein from budding yeast. Pti1 is an essential component of CPF (cleavage and polyadenylation factor) involved in 3' end formation of snoRNA and mRNA [].
The hinge domain of cleavage stimulation factor subunit 2 proteins, CSTF2, is necessary for binding to the subunit CstF-77 within the polyadenylation complex and subsequent nuclear localisation. This suggests that nuclear import of a pre-formed CSTF complex is an essential step in polyadenylation. Accurate and efficient polyadenylation is essential for transcriptional termination, nuclear export, translation, and stability of eukaryotic mRNAs. CSTF2 is an important regulatory subunit of the polyadenylation complex [].
