This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Green, P L Articles by Chen, I S Search for Related Content PubMed PubMed Citation Articles by Green, P L Articles by Chen, I S

Phosphorylation regulates RNA binding by the human T-cell leukemia virus Rex protein.

Department of Medicine, University of California, School of Medicine, Los Angeles.

ABSTRACT

The Rex protein of human T-cell leukemia virus types I (HTLV-I) and II (HTLV-II) regulates the expression of the viral structural genes and is critical for viral replication. Rex acts by specifically binding to RNAs containing sequences of the R region of the 5' long terminal repeat. Two forms of Rex detected in HTLV-II-infected cells, p26rex and p24rex, differ in the extent of serine phosphorylation. Two-dimensional phosphopeptide analysis indicates that p26rex is extensively phosphorylated at multiple sites. Using a sensitive immunobinding assay, we show that the phosphorylation state of Rex determines the efficiency of binding of Rex to HTLV-II target RNAs. Thus, the phosphorylation state of Rex in the infected cell may be a switch that determines whether virus exists in a latent or productive state. These studies also suggest that phosphorylation of RNA-binding regulatory proteins is a more general mechanism of gene regulation.

This article has been cited by other articles:

• Modrof, J., Lymperopoulos, K., Roy, P. (2005). Phosphorylation of Bluetongue Virus Nonstructural Protein 2 Is Essential for Formation of Viral Inclusion Bodies. J. Virol. 79: 10023-10031 [Abstract] [Full Text]  
• Narayan, M., Younis, I., D'Agostino, D. M., Green, P. L. (2003). Functional Domain Structure of Human T-Cell Leukemia Virus Type 2 Rex. J. Virol. 77: 12829-12840 [Abstract] [Full Text]  
• Wootton, S. K., Rowland, R. R. R., Yoo, D. (2002). Phosphorylation of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Protein. J. Virol. 76: 10569-10576 [Abstract] [Full Text]  
• Narayan, M., Kusuhara, K., Green, P. L. (2001). Phosphorylation of Two Serine Residues Regulates Human T-Cell Leukemia Virus Type 2 Rex Function. J. Virol. 75: 8440-8448 [Abstract] [Full Text]  
• Liu, Q., Hobom, G. (2000). Agnoprotein-1a of avian polyomavirus budgerigar fledgling disease virus: identification of phosphorylation sites and functional importance in the virus life-cycle. J. Gen. Virol. 81: 359-367 [Abstract] [Full Text]  
• Kusuhara, K., Anderson, M., Pettiford, S. M., Green, P. L. (1999). Human T-Cell Leukemia Virus Type 2 Rex Protein Increases Stability and Promotes Nuclear to Cytoplasmic Transport of gag/pol and env RNAs. J. Virol. 73: 8112-8119 [Abstract] [Full Text]  
• Kucerova, L., Altanerova, V., Altaner, C., Boris-Lawrie, K. (1999). Bovine Leukemia Virus Structural Gene Vectors Are Immunogenic and Lack Pathogenicity in a Rabbit Model. J. Virol. 73: 8160-8166 [Abstract] [Full Text]  
• Heger, P., Rosorius, O., Koch, C., Casari, G., Grassmann, R., Hauber, J. (1998). Multimer Formation Is Not Essential for Nuclear Export of Human T-Cell Leukemia Virus Type 1 Rex trans-Activator Protein. J. Virol. 72: 8659-8668 [Abstract] [Full Text]  
• Donald, R., Ballard, D. W., Hawiger, J. (1995). Proteolytic Processing of NF-kappaB/IkappaB in Human Monocytes. J. Biol. Chem. 270: 9-12 [Abstract] [Full Text]