Molecular Biology of the Cell track citations

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


     

Originally published as MBC in Press, 10.1091/mbc.02-05-0083 on August 6, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
02-05-0083v1
13/10/3576    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 Chen, M.
Right arrow Articles by von Mikecz, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, M.
Right arrow Articles by von Mikecz, A.

Vol. 13, Issue 10, 3576-3587, October 2002

Subcellular Recruitment of Fibrillarin to Nucleoplasmic Proteasomes: Implications for Processing of a Nucleolar Autoantigen

Min Chen,* Thomas Rockel,* Gabriele Steinweger,* Peter Hemmerich,dagger Jakob Risch,Dagger and Anna von Mikecz*§

 *Junior Research Group of Molecular Cell Biology, Institute of Environmental Health Research, Heinrich-Heine-University, Düsseldorf, Germany;  dagger Department of Molecular Biology, Institute of Molecular Biotechnology, Jena, Germany; and  Dagger Computing Center, Technical University, Aachen, Germany

A prerequisite for proteins to interact in a cell is that they are present in the same intracellular compartment. Although it is generally accepted that proteasomes occur in both, the cytoplasm and the nucleus, research has been focusing on cytoplasmic protein breakdown and antigen processing, respectively. Thus, little is known on the functional organization of the proteasome in the nucleus. Here we report that within the nucleus 20S and 26S proteasomes occur throughout the nucleoplasm and partially colocalize with splicing factor-containing speckles. Because proteasomes are absent from the nucleolus, a recruitment system was used to analyze the molecular fate of nucleolar protein fibrillarin: Subtoxic concentrations of mercuric chloride (HgCl2) induce subcellular redistribution of fibrillarin and substantial colocalization (33%) with nucleoplasmic proteasomes in different cell lines and in primary cells isolated from mercury-treated mice. Accumulation of fibrillarin and fibrillarin-ubiquitin conjugates in lactacystin-treated cells suggests that proteasome-dependent processing of this autoantigen occurs upon mercury induction. The latter observation might constitute the cell biological basis of autoimmune responses that specifically target fibrillarin in mercury-mouse models and scleroderma.

§ Corresponding author. E-mail address: mikecz{at}uni-duesseldorf.de.

Molecular Biology of the Cell
Vol. 13, 3576-3587, October 2002
Copyright © 2002 by The American Society for Cell Biology


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
V. Baldin, M. Militello, Y. Thomas, C. Doucet, W. Fic, S. Boireau, I. Jariel-Encontre, M. Piechaczyk, E. Bertrand, J. Tazi, et al.
A Novel Role for PA28{gamma}-Proteasome in Nuclear Speckle Organization and SR Protein Trafficking
Mol. Biol. Cell, April 1, 2008; 19(4): 1706 - 1716.
[Abstract] [Full Text] [PDF]

Home page
 Hum ReprodHome page
V. Y. Rawe, E. S. Diaz, R. Abdelmassih, C. Wojcik, P. Morales, P. Sutovsky, and H. E. Chemes
The role of sperm proteasomes during sperm aster formation and early zygote development: implications for fertilization failure in humans
Hum. Reprod., March 1, 2008; 23(3): 573 - 580.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. S. Philips, J. C. Kwok, and B. H. Chong
Analysis of the Signals and Mechanisms Mediating Nuclear Trafficking of GATA-4: LOSS OF DNA BINDING IS ASSOCIATED WITH LOCALIZATION IN INTRANUCLEAR SPECKLES
J. Biol. Chem., August 24, 2007; 282(34): 24915 - 24927.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
D. A. Stavreva, M. Kawasaki, M. Dundr, K. Koberna, W. G. Muller, T. Tsujimura-Takahashi, W. Komatsu, T. Hayano, T. Isobe, I. Raska, et al.
Potential Roles for Ubiquitin and the Proteasome during Ribosome Biogenesis.
Mol. Cell. Biol., July 1, 2006; 26(13): 5131 - 5145.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
A. von Mikecz
The nuclear ubiquitin-proteasome system
J. Cell Sci., May 15, 2006; 119(10): 1977 - 1984.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
T. D. Rockel, D. Stuhlmann, and A. von Mikecz
Proteasomes degrade proteins in focal subdomains of the human cell nucleus
J. Cell Sci., November 15, 2005; 118(22): 5231 - 5242.
[Abstract] [Full Text] [PDF]

Home page
 Ann. N. Y. Acad. Sci.Home page
M. CHEN and A. von MIKECZ
Xenobiotic-Induced Recruitment of Autoantigens to Nuclear Proteasomes Suggests a Role for Altered Antigen Processing in Scleroderma
Ann. N.Y. Acad. Sci., June 1, 2005; 1051(1): 382 - 389.
[Abstract] [Full Text] [PDF]

Home page
 Biol. Reprod.Home page
P. Sutovsky, G. Manandhar, T. C. McCauley, J. N. Caamano, M. Sutovsky, W. E. Thompson, and B. N. Day
Proteasomal Interference Prevents Zona Pellucida Penetration and Fertilization in Mammals
Biol Reprod, November 1, 2004; 71(5): 1625 - 1637.
[Abstract] [Full Text] [PDF]


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