title: Functional and physical interaction of the human ARF tumor suppressor with Tat-binding protein-1.
abstract: The p14ARF tumor suppressor is a key regulator of cellular proliferation, frequently inactivated in human cancer, whose mode of action is currently not completely understood. We report here that the so-called human immunodeficiency virus Tat-binding protein-1 (TBP-1), a component of the 19 S regulatory subunit of the proteasome 26 S, also involved in transcriptional regulation and with a supposed role in the control of cell proliferation, specifically interacts with ARF, both in yeast and mammalian cells. We present evidence that the overexpression of TBP-1 in various cell lines results in a sharp increase of both transfected and endogenous ARF protein levels. Moreover, this effect depends on the binding between the two proteins and, at least in part, is exerted at the post-translational level. We also show that the ARF increase following TBP-1 overexpression results in an increase in p53 protein levels and activity. Finally, our data underline a clear involvement of TBP-1 in the control of cell proliferation.
authors.affiliation: Department of Genetics, General and Molecular Biology, University of Naples Federico II, Via Mezzocannone 8, 80134 Naples, Italy.
authors.forename: Alessandra
authors.initials: A
authors.lastname: Pollice
authors.forename: Vittorio
authors.initials: V
authors.lastname: Nasti
authors.forename: Raffaele
authors.initials: R
authors.lastname: Ronca
authors.forename: Maria
authors.initials: M
authors.lastname: Vivo
authors.forename: Marco
authors.initials: M
authors.lastname: Lo Iacono
authors.forename: Raffaele
authors.initials: R
authors.lastname: Calogero
authors.forename: Viola
authors.initials: V
authors.lastname: Calabrò
authors.forename: Girolama
authors.initials: G
authors.lastname: La Mantia
mesh_terms: D000074183:ATPases Associated with Diverse Cellular Activities; D000818:Animals; D019556:COS Cells; D002455:Cell Division; D015500:Chloramphenicol O-Acetyltransferase / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry; D017931:DNA Primers / Q000737:chemistry; D018076:DNA, Complementary / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D005786:Gene Expression Regulation; D006367:HeLa Cells; D006801:Humans; D051379:Mice; D009097:Multienzyme Complexes / Q000737:chemistry; D041681:NIH 3T3 Cells; D010447:Peptide Hydrolases / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011233:Precipitin Tests; D046988:Proteasome Endopeptidase Complex; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013997:Time Factors; D014158:Transcription, Genetic; D014162:Transfection; D025803:Tumor Suppressor Protein p14ARF / Q000737:chemistry* / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism; D020798:Two-Hybrid System Techniques
chemical_list: D017931:DNA Primers; D018076:DNA, Complementary; D004268:DNA-Binding Proteins; D009097:Multienzyme Complexes; D011500:Protein Synthesis Inhibitors; D025803:Tumor Suppressor Protein p14ARF; D016159:Tumor Suppressor Protein p53; D015500:Chloramphenicol O-Acetyltransferase; D010447:Peptide Hydrolases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D000074183:ATPases Associated with Diverse Cellular Activities; C064757:PSMC3 protein, human