| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | ADVANCED SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Divisions of Oncology
2 Cellular and Molecular Biology, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
3 Department of Life Science and Human Technology, Nara Women's University, Kita-Uoya Nishimachi, Nara 630-8506, Japan
4 Depertment of Molecular Medicine, Faculty of Medicine, Osaka University, 2-2 Yamadaoka, Suita-shi, Osaka 565-0871, Japan
Tob is a member of an emerging family of anti-proliferative proteins that suppress cell growth when over-expressed. tob mRNA is highly expressed in anergic T cells and over-expression of Tob suppresses transcription of interleukin-2 (IL-2) through its interaction with Smads. Here, we identified two types of cDNA clones coding for poly(A)-binding protein (PABP) and inducible PABP (iPABP) by screening an expression cDNA library with the GST-Tob probe. Co-immunoprecipitation and GST-pull down experiments showed that Tob associated with the carboxyl-terminal region of iPABP. We then found that iPABP, like PABP, was involved in regulation of translation: iPABP enhanced translation of IL-2 mRNA in vitro. The enhanced translation of IL-2 mRNA required the 3'UTR and poly(A) sequences. Tob abrogated the enhancement of translation through its interaction with carboxyl-terminal region of iPABP in vitro. Consistently, over-expression of Tob in NIH3T3 cells, in which exogenous iPABP was stably expressed, resulted in suppression of IL-2 production from the simultaneously transfected IL-2 expression plasmid. Finally, Tob, whose expression was induced by anergic stimulation, was co-immunoprecipitated with iPABP in human T cells. These findings suggest that Tob is involved in the translational suppression of IL-2 mRNA in anergic T cells through its interaction with iPABP.
* Correspondence: E-mail: tyamamot{at}ims.u-tokyo.ac.jp
This article has been cited by other articles:
|
|
 |
|
  M. Horiuchi, K. Takeuchi, N. Noda, N. Muroya, T. Suzuki, T. Nakamura, J. Kawamura-Tsuzuku, K. Takahasi, T. Yamamoto, and F. Inagaki Structural Basis for the Antiproliferative Activity of the Tob-hCaf1 Complex J. Biol. Chem., May 8, 2009; 284(19): 13244 - 13255. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. M. Bonderoff, J. L. LaRey, and R. E. Lloyd Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Proteinase Inhibits Viral Internal Ribosome Entry Site-Mediated Translation J. Virol., October 1, 2008; 82(19): 9389 - 9399. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. M. Rowlett, C. A. Chrestensen, M. J. Schroeder, M. G. Harp, J. W. Pelo, J. Shabanowitz, R. DeRose, D. F. Hunt, T. W. Sturgill, and M. T. Worthington Inhibition of tristetraprolin deadenylation by poly(A) binding protein Am J Physiol Gastrointest Liver Physiol, September 1, 2008; 295(3): G421 - G430. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Funakoshi, Y. Doi, N. Hosoda, N. Uchida, M. Osawa, I. Shimada, M. Tsujimoto, T. Suzuki, T. Katada, and S.-i. Hoshino Mechanism of mRNA deadenylation: evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases Genes & Dev., December 1, 2007; 21(23): 3135 - 3148. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Ezzeddine, T.-C. Chang, W. Zhu, A. Yamashita, C.-Y. A. Chen, Z. Zhong, Y. Yamashita, D. Zheng, and A.-B. Shyu Human TOB, an Antiproliferative Transcription Factor, Is a Poly(A)-Binding Protein-Dependent Positive Regulator of Cytoplasmic mRNA Deadenylation Mol. Cell. Biol., November 15, 2007; 27(22): 7791 - 7801. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Oberle, N. Eberhardt, C. S. Falk, P. H. Krammer, and E. Suri-Payer Rapid Suppression of Cytokine Transcription in Human CD4+CD25 T Cells by CD4+Foxp3+ Regulatory T Cells: Independence of IL-2 Consumption, TGF-beta, and Various Inhibitors of TCR Signaling J. Immunol., September 15, 2007; 179(6): 3578 - 3587. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Siddiqui, D. A. Mangus, T.-C. Chang, J.-M. Palermino, A.-B. Shyu, and K. Gehring Poly(A) Nuclease Interacts with the C-terminal Domain of Polyadenylate-binding Protein Domain from Poly(A)-binding Protein J. Biol. Chem., August 24, 2007; 282(34): 25067 - 25075. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Dizin, C. Gressier, C. Magnard, H. Ray, D. Decimo, T. Ohlmann, and N. D. Venezia BRCA1 Interacts with Poly(A)-binding Protein: IMPLICATION OF BRCA1 IN TRANSLATION REGULATION J. Biol. Chem., August 25, 2006; 281(34): 24236 - 24246. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. S. Lim, G. Kozlov, T.-C. Chang, O. Groover, N. Siddiqui, L. Volpon, G. De Crescenzo, A.-B. Shyu, and K. Gehring Comparative Peptide Binding Studies of the PABC Domains from the Ubiquitin-protein Isopeptide Ligase HYD and Poly(A)-binding Protein: IMPLICATIONS FOR HYD FUNCTION J. Biol. Chem., May 19, 2006; 281(20): 14376 - 14382. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. E. Thompson, L. B. Lamont, and J. Kimble Germ-line induction of the Caenorhabditis elegans vulva PNAS, January 17, 2006; 103(3): 620 - 625. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M.C. DERRY, A. YANAGIYA, Y. MARTINEAU, and N. SONENBERG Regulation of Poly(A)-binding Protein through PABP-interacting Proteins Cold Spring Harb Symp Quant Biol, January 1, 2006; 71(0): 537 - 543. [Abstract] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | ADVANCED SEARCH | TABLE OF CONTENTS |
