Molecular Biology of the Cell

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E02-03-0161 on September 24, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E02-03-0161v1
13/11/3822    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Strehblow, A.
Right arrow Articles by Jantsch, M. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Strehblow, A.
Right arrow Articles by Jantsch, M. F.

Vol. 13, Issue 11, 3822-3835, November 2002

Nucleocytoplasmic Distribution of Human RNA-editing Enzyme ADAR1 Is Modulated by Double-stranded RNA-binding Domains, a Leucine-rich Export Signal, and a Putative Dimerization Domain

Alexander Strehblow, Martina Hallegger, and Michael F. Jantsch*

Department of Cell Biology and Genetics, Institute of Botany, University of Vienna, A-1030 Vienna, Austria

The human RNA-editing enzyme adenosine deaminase that acts on RNA (ADAR1) is expressed in two versions. A longer 150-kDa protein is interferon inducible and can be found both in the nucleus and cytoplasm. An amino-terminally truncated 110-kDa version, in contrast, is constitutively expressed and predominantly nuclear. In the absence of transcription, however, the shorter protein is also cytoplasmic and thus displays the hallmarks of a shuttling protein. The nuclear localization signal (NLS) of human hsADAR1 is atypical and overlaps with its third double-stranded RNA-binding domain (dsRBD). Herein, we identify regions in hsADAR1 that interfere with nuclear localization and mediate cytoplasmic accumulation. We show that interferon-inducible hsADAR1 contains a Crm1-dependent nuclear export signal in its amino terminus. Most importantly, we demonstrate that the first dsRBD of hsADAR1 interferes with nuclear localization of a reporter construct containing dsRBD3 as an active NLS. The same effect can be triggered by several other, but not all dsRBDs. Active RNA binding of either the inhibitory dsRBD1 or the NLS bearing dsRBD3 is required for cytoplasmic accumulation. Furthermore, hsADAR1's dsRBD1 has no effect on other NLSs, suggesting RNA-mediated cross talk between dsRBDs, possibly leading to masking of the NLS. A model, incorporating these findings is presented. Finally, we identify a third region located in the C terminus of hsADAR1 that also interferes with nuclear accumulation of this protein.

* Corresponding author. E-mail address: michael.jantsch{at}univie.ac.at.

Molecular Biology of the Cell
Vol. 13, 3822-3835, November 2002
Copyright © 2002 by The American Society for Cell Biology


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
V. K. Schoft, S. Schopoff, and M. F. Jantsch
Regulation of glutamate receptor B pre-mRNA splicing by RNA editing
Nucleic Acids Res., June 28, 2007; 35(11): 3723 - 3732.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
N. B. Sallacz and M. F. Jantsch
Chromosomal Storage of the RNA-editing Enzyme ADAR1 in Xenopus Oocytes
Mol. Biol. Cell, July 1, 2005; 16(7): 3377 - 3386.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. X. George, M. V. Wagner, and C. E. Samuel
Expression of Interferon-inducible RNA Adenosine Deaminase ADAR1 during Pathogen Infection and Mouse Embryo Development Involves Tissue-selective Promoter Utilization and Alternative Splicing
J. Biol. Chem., April 15, 2005; 280(15): 15020 - 15028.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
Q. Wang and G. G. Carmichael
Effects of Length and Location on the Cellular Response to Double-Stranded RNA
Microbiol. Mol. Biol. Rev., September 1, 2004; 68(3): 432 - 452.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
P. Macchi, A. M. Brownawell, B. Grunewald, L. DesGroseillers, I. G. Macara, and M. A. Kiebler
The Brain-specific Double-stranded RNA-binding Protein Staufen2: NUCLEOLAR ACCUMULATION AND ISOFORM-SPECIFIC EXPORTIN-5-DEPENDENT EXPORT
J. Biol. Chem., July 23, 2004; 279(30): 31440 - 31444.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
A. N. Ladd and T. A. Cooper
Multiple domains control the subcellular localization and activity of ETR-3, a regulator of nuclear and cytoplasmic RNA processing events
J. Cell Sci., July 15, 2004; 117(16): 3519 - 3529.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y. Nie, Q. Zhao, Y. Su, and J.-H. Yang
Subcellular Distribution of ADAR1 Isoforms Is Synergistically Determined by Three Nuclear Discrimination Signals and a Regulatory Motif
J. Biol. Chem., March 26, 2004; 279(13): 13249 - 13255.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. DeSousa, M. Mukhopadhyay, P. Pelka, X. Zhao, B. K. Dey, V. Robert, A. Pelisson, A. Bucheton, and A. R. Campos
A Novel Double-stranded RNA-binding Protein, Disco Interacting Protein 1 (DIP1), Contributes to Cell Fate Decisions during Drosophila Development
J. Biol. Chem., September 26, 2003; 278(39): 38040 - 38050.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
Y.-G. Kim, M. Muralinath, T. Brandt, M. Pearcy, K. Hauns, K. Lowenhaupt, B. L. Jacobs, and A. Rich
A role for Z-DNA binding in vaccinia virus pathogenesis
PNAS, June 10, 2003; 100(12): 6974 - 6979.
[Abstract] [Full Text] [PDF]

Home page
 JCBHome page
M. Doyle and M. F. Jantsch
Distinct in vivo roles for double-stranded RNA-binding domains of the Xenopus RNA-editing enzyme ADAR1 in chromosomal targeting
J. Cell Biol., April 28, 2003; 161(2): 309 - 319.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]