Staufen homolog 2 is a member of the family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. Staufen homolog 2 shares 48.5% and 59.9% similarity with drosophila and human staufen, respectively. The exact function of Staufen homolog 2 is not known, but since it contains 3 copies of conserved dsRNA binding domain, it could be involved in double-stranded RNA binding events.[6] Expression of Stau2 was sufficient to increase eye size, suggesting a novel biological role of Stau2 in eye morphogenesis.[7]
Acting as a HIV-1 dependency factor, Staufen-2 promotes HIV-1 proliferation by positively regulating RNA export activity of viral protein Rev [8] and recently it was reported that Staufen-2 is incorporated into HIV-1 particles and boost viral infectivity[9]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Buchner G, Bassi MT, Andolfi G, Ballabio A, Franco B (November 1999). "Identification of a novel homolog of the Drosophila staufen protein in the chromosome 8q13-q21.1 region". Genomics. 62 (1): 113–8. doi:10.1006/geno.1999.6015. PMID10585778.
Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (October 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID16964243. S2CID14294292.
Duchaîne TF, Hemraj I, Furic L, Deitinghoff A, Kiebler MA, DesGroseillers L (August 2002). "Staufen2 isoforms localize to the somatodendritic domain of neurons and interact with different organelles". Journal of Cell Science. 115 (Pt 16): 3285–95. doi:10.1242/jcs.115.16.3285. PMID12140260.