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APOBEC3A  -  apolipoprotein B mRNA editing enzyme,...

Homo sapiens

Synonyms: A3A, ARP3, DNA dC->dU-editing enzyme APOBEC-3A, PHRBN, Phorbolin-1, ...
 
 
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Disease relevance of APOBEC3A

 

High impact information on APOBEC3A

  • Here, we demonstrate that APOBEC3A and APOBEC3B, two members of the APOBEC3 family of human innate antiretroviral resistance factors, can enter the nucleus, where LINE-1 and Alu reverse transcription occurs, and specifically inhibit both LINE-1 and Alu retrotransposition [4].
  • Using a retrotransposition reporter assay in HeLa cells, we demonstrate that in the presence of transiently transfected APOBEC3A, L1 retrotransposition frequency was reduced by up to 85% [5].
  • Transient expression of the phorbolin-1 cDNA in COS cells and by in vitro transcription/translation, yielded polypeptides that comigrated with phorbolins-1 and -2 [3].
  • Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1 [3].
  • Earlier studies of psoriatic and normal primary keratinocytes treated with phorbol 12-myristate-1-acetate identified two low-molecular-weight proteins, termed phorbolin-1 (20 kDa; pI 6.6) and phorbolin-2 (17.6 kDa; pI 6.5) [3].
 

Biological context of APOBEC3A

 

Anatomical context of APOBEC3A

  • In a cell-free system, RacG induced actin polymerization upon GTPgammaS stimulation, and this response could be blocked by an Arp3 antibody [7].
 

Other interactions of APOBEC3A

  • APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells [8].
  • While both APOBEC3G and APOBEC3B specifically interact with the IAP Gag protein in co-expressing cells, and induce extensive editing of IAP reverse transcripts, APOBEC3A fails to package detectably into IAP virus-like particles and does not edit IAP reverse transcripts [8].

References

  1. Identification of APOBEC3DE as Another Antiretroviral Factor from the Human APOBEC Family. Dang, Y., Wang, X., Esselman, W.J., Zheng, Y.H. J. Virol. (2006) [Pubmed]
  2. APOBEC3A is a potent inhibitor of adeno-associated virus and retrotransposons. Chen, H., Lilley, C.E., Yu, Q., Lee, D.V., Chou, J., Narvaiza, I., Landau, N.R., Weitzman, M.D. Curr. Biol. (2006) [Pubmed]
  3. Psoriasis upregulated phorbolin-1 shares structural but not functional similarity to the mRNA-editing protein apobec-1. Madsen, P., Anant, S., Rasmussen, H.H., Gromov, P., Vorum, H., Dumanski, J.P., Tommerup, N., Collins, J.E., Wright, C.L., Dunham, I., MacGinnitie, A.J., Davidson, N.O., Celis, J.E. J. Invest. Dermatol. (1999) [Pubmed]
  4. Cellular inhibitors of long interspersed element 1 and Alu retrotransposition. Bogerd, H.P., Wiegand, H.L., Hulme, A.E., Garcia-Perez, J.L., O'Shea, K.S., Moran, J.V., Cullen, B.R. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. APOBEC3 proteins inhibit human LINE-1 retrotransposition. Muckenfuss, H., Hamdorf, M., Held, U., Perkovic, M., Löwer, J., Cichutek, K., Flory, E., Schumann, G.G., Münk, C. J. Biol. Chem. (2006) [Pubmed]
  6. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Jarmuz, A., Chester, A., Bayliss, J., Gisbourne, J., Dunham, I., Scott, J., Navaratnam, N. Genomics (2002) [Pubmed]
  7. RacG Regulates Morphology, Phagocytosis, and Chemotaxis. Somesh, B.P., Vlahou, G., Iijima, M., Insall, R.H., Devreotes, P., Rivero, F. Eukaryotic Cell (2006) [Pubmed]
  8. APOBEC3A and APOBEC3B are potent inhibitors of LTR-retrotransposon function in human cells. Bogerd, H.P., Wiegand, H.L., Doehle, B.P., Lueders, K.K., Cullen, B.R. Nucleic Acids Res. (2006) [Pubmed]
 
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