APOBEC-1 and AID are nucleo-cytoplasmic trafficking proteins but APOBEC3G cannot traffic

• Published in: Biochemical and biophysical research communications Vol. 350; no. 1; pp. 214 - 219
• Main Authors: Bennett, Ryan P., Diner, Elie, Sowden, Mark P., Lees, Joshua A., Wedekind, Joseph E., Smith, Harold C.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 10.11.2006
• Subjects: AID; Amino Acid Sequence; APOBEC-1; APOBEC-1 Deaminase; APOBEC3G; Cell Nucleus - metabolism; Cytidine Deaminase - chemistry; Cytidine Deaminase - genetics; Cytidine Deaminase - metabolism; Cytoplasm - metabolism; HeLa Cells; Human immunodeficiency virus 1; Humans; Leucine - genetics; Leucine - metabolism; Molecular Sequence Data; NES; NLS; Protein Transport; Retrovirus; Sequence Alignment; Sequence Homology, Amino Acid; Trafficking; APOBEC3G; APOBEC-1; NLS; AID; NES; Trafficking
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2006.09.032

Human APOBEC3G (hA3G) is a member of the APOBEC-1 related protein (ARP) family of cytidine deaminases. hA3G functions as a natural defense against endogenous retrotransposons and a multitude of retroviruses, most notably human immunodeficiency virus type 1 (HIV-1). Nothing is known about the cellular function of hA3G, however, upon HIV-1 infection hA3G functions as an antiviral factor by mutating viral single-stranded DNA during reverse transcription. Whereas homologous deaminases such as APOBEC-1 and AID act on RNA and DNA, respectively, in the cell nucleus, hA3G mutagenic activity appears to be restricted to the cytoplasm. We demonstrate that hA3G is not a nucleo-cytoplasmic shuttling protein like APOBEC-1 and AID, but is strongly retained in the cytoplasm through a mechanism that involves both the N and C-terminal regions of the protein.