|
|
|
|
|
|
|
|
|||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 110, Issue 15 1741-1750, Copyright © 1997 by Company of Biologists
JOURNAL ARTICLES |
H Zinszner, J Sok, D Immanuel, Y Yin and D Ron
Skirball Institute of Biomolecular Medicine, the Deparment of Medicine, NYU Medical Center, New York 10016, USA.
TLS, the product of a gene commonly translocated in liposarcomas (TLS), is prototypical of a newly identified class of nuclear proteins that contain a C-terminal domain with a distinct RNA recognition motif (RRM) surrounded by Arg-Gly-Gly (RGG) repeats. Its unique N terminus serves as an essential transforming domain for a number of fusion oncoproteins in human sarcomas and leukemias. In this study we use an in vivo UV crosslinking procedure to probe the interactions of TLS with RNA. TLS is found to bind RNA in vivo and the association of TLS with RNA is rapidly diminished by treating cells with transcriptional inhibitors. This suggests that the species bound by TLS turns over rapidly. Surprisingly, the RRM was found to be dispensable for RNA binding by TLS in vivo, suggesting that at any one time most of the interactions between TLS and RNA in the cell are not sequence specific. Analysis of inter specific heterokaryons formed between human and mouse or Xenopus cells revealed that TLS engages in rapid nucleocytoplasmic shuttling, a finding confirmed by the ability of anti-TLS antibodies to trap TLS when injected into the cytoplasm of HeLa cells. Cellular fractionation experiments suggest that TLS binds to RNA in both the nucleus and cytoplasm and support the hypothesis that TLS functions as a heterogeneous ribonuclear protein (hnRNP)-like chaperone of RNA. These findings are discussed in the context of the role altered forms of TLS play in cellular transformation.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati 
Twitter What's this?
This article has been cited by other articles:
|
|
 |
|
  M. Neumann, R. Rademakers, S. Roeber, M. Baker, H. A. Kretzschmar, and I. R. A. Mackenzie A new subtype of frontotemporal lobar degeneration with FUS pathology Brain, November 1, 2009; 132(11): 2922 - 2931. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G. S. Pesiridis, V. M.-Y. Lee, and J. Q. Trojanowski Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis Hum. Mol. Genet., October 15, 2009; 18(R2): R156 - R162. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Ticozzi, V. Silani, A. L. LeClerc, P. Keagle, C. Gellera, A. Ratti, F. Taroni, T. J. Kwiatkowski Jr, D. M. McKenna-Yasek, P. C. Sapp, et al. Analysis of FUS gene mutation in familial amyotrophic lateral sclerosis within an Italian cohort Neurology, October 13, 2009; 73(15): 1180 - 1185. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 A. Y. Tan and J. L. Manley The TET Family of Proteins: Functions and Roles in Disease J Mol Cell Biol, September 24, 2009; (2009) mjp025v1. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Doi, K. Okamura, P. O. Bauer, Y. Furukawa, H. Shimizu, M. Kurosawa, Y. Machida, H. Miyazaki, K. Mitsui, Y. Kuroiwa, et al. RNA-binding Protein TLS Is a Major Nuclear Aggregate-interacting Protein in Huntingtin Exon 1 with Expanded Polyglutamine-expressing Cells J. Biol. Chem., March 7, 2008; 283(10): 6489 - 6500. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 W. J. Law, K. L. Cann, and G. G. Hicks TLS, EWS and TAF15: a model for transcriptional integration of gene expression Brief Funct Genomic Proteomic, March 1, 2006; 5(1): 8 - 14. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Fujii and T. Takumi TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines J. Cell Sci., December 15, 2005; 118(24): 5755 - 5765. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Barker, M. Weinfeld, J. Zheng, L. Li, and D. Murray Identification of Mammalian Proteins Cross-linked to DNA by Ionizing Radiation J. Biol. Chem., October 7, 2005; 280(40): 33826 - 33838. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Alex and K. A. W. Lee RGG-boxes of the EWS oncoprotein repress a range of transcriptional activation domains Nucleic Acids Res., March 2, 2005; 33(4): 1323 - 1331. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Lepourcelet, L. Tou, L. Cai, J.-i. Sawada, A. J. F. Lazar, J. N. Glickman, J. A. Williamson, A. D. Everett, M. Redston, E. A. Fox, et al. Insights into developmental mechanisms and cancers in the mammalian intestine derived from serial analysis of gene expression and study of the hepatoma-derived growth factor (HDGF) Development, January 15, 2005; 132(2): 415 - 427. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Iko, T. S. Kodama, N. Kasai, T. Oyama, E. H. Morita, T. Muto, M. Okumura, R. Fujii, T. Takumi, S.-i. Tate, et al. Domain Architectures and Characterization of an RNA-binding Protein, TLS J. Biol. Chem., October 22, 2004; 279(43): 44834 - 44840. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
G. Pinon-Lataillade, C. Masson, J. Bernardino-Sgherri, V. Henriot, P. Mauffrey, Y. Frobert, S. Araneda, and J. F. Angulo KIN17 encodes an RNA-binding protein and is expressed during mouse spermatogenesis J. Cell Sci., July 15, 2004; 117(16): 3691 - 3702. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. Deneen, S. M. Welford, T. Ho, F. Hernandez, I. Kurland, and C. T. Denny PIM3 Proto-Oncogene Kinase Is a Common Transcriptional Target of Divergent EWS/ETS Oncoproteins Mol. Cell. Biol., June 1, 2003; 23(11): 3897 - 3908. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Iervolino, G. Santilli, R. Trotta, C. Guerzoni, V. Cesi, A. Bergamaschi, C. Gambacorti-Passerini, B. Calabretta, and D. Perrotti hnRNP A1 Nucleocytoplasmic Shuttling Activity Is Required for Normal Myelopoiesis and BCR/ABL Leukemogenesis Mol. Cell. Biol., April 1, 2002; 22(7): 2255 - 2266. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. L. Rossow and R. Janknecht The Ewing's Sarcoma Gene Product Functions as a Transcriptional Activator Cancer Res., March 1, 2001; 61(6): 2690 - 2695. [Abstract] [Full Text]
|
|
|
|
|
|
A. T. Akhmedov and B. S. Lopez Human 100-kDa homologous DNA-pairing protein is the splicing factor PSF and promotes DNA strand invasion Nucleic Acids Res., August 15, 2000; 28(16): 3022 - 3030. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Yang, L. J. Embree, and D. D. Hickstein TLS-ERG Leukemia Fusion Protein Inhibits RNA Splicing Mediated by Serine-Arginine Proteins Mol. Cell. Biol., May 15, 2000; 20(10): 3345 - 3354. [Abstract] [Full Text]
|
|
|
|
|
|
H. Baechtold, M. Kuroda, J. Sok, D. Ron, B. S. Lopez, and A. T. Akhmedov Human 75-kDa DNA-pairing Protein Is Identical to the Pro-oncoprotein TLS/FUS and Is Able to Promote D-loop Formation J. Biol. Chem., November 26, 1999; 274(48): 34337 - 34342. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Lee, M. Neumann, R. Stearman, R. Stauber, A. Pause, G. N. Pavlakis, and R. D. Klausner Transcription-Dependent Nuclear-Cytoplasmic Trafficking Is Required for the Function of the von Hippel-Lindau Tumor Suppressor Protein Mol. Cell. Biol., February 1, 1999; 19(2): 1486 - 1497. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. Yang, L. J. Embree, S. Tsai, and D. D. Hickstein Oncoprotein TLS Interacts with Serine-Arginine Proteins Involved in RNA Splicing J. Biol. Chem., October 23, 1998; 273(43): 27761 - 27764. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Zhang, A. J. Paley, and G. Childs The Transcriptional Repressor ZFM1 Interacts with and Modulates the Ability of EWS to Activate Transcription J. Biol. Chem., July 17, 1998; 273(29): 18086 - 18091. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
U Atasoy, J Watson, D Patel, and J. Keene ELAV protein HuA (HuR) can redistribute between nucleus and cytoplasm and is upregulated during serum stimulation and T cell activation J. Cell Sci., January 11, 1998; 111(21): 3145 - 3156. [Abstract] [PDF]
|
|
|
|
|
|
K. K. C. Li and K. A. W. Lee Transcriptional Activation by the Ewing's Sarcoma (EWS) Oncogene Can Be Cis-repressed by the EWS RNA-binding Domain J. Biol. Chem., July 21, 2000; 275(30): 23053 - 23058. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Lerga, M. Hallier, L. Delva, C. Orvain, I. Gallais, J. Marie, and F. Moreau-Gachelin Identification of an RNA Binding Specificity for the Potential Splicing Factor TLS J. Biol. Chem., February 23, 2001; 276(9): 6807 - 6816. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. R. Saunders, D. J. Perkins, S. Balachandran, R. Michaels, R. Ford, A. Mayeda, and G. N. Barber Characterization of Two Evolutionarily Conserved, Alternatively Spliced Nuclear Phosphoproteins, NFAR-1 and -2, That Function in mRNA Processing and Interact with the Double-stranded RNA-dependent Protein Kinase, PKR J. Biol. Chem., August 17, 2001; 276(34): 32300 - 32312. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. KIM and J. PELLETIER Molecular genetics of chromosome translocations involving EWS and related family members Physiol Genomics, November 11, 1999; 1(3): 127 - 138. [Abstract] [Full Text] [PDF]
|
|
