JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M101205200 on May 7, 2001

J. Biol. Chem., Vol. 276, Issue 28, 26324-26331, July 13, 2001
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
276/28/26324    most recent
M101205200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 Hamilton, M. H.
Right arrow Articles by McDonnell, D. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hamilton, M. H.
Right arrow Articles by McDonnell, D. P.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Nuclear Import/Export of hRPF1/Nedd4 Regulates the Ubiquitin- dependent Degradation of Its Nuclear Substrates*

Maria Huacani HamiltonDagger , Irina TcherepanovaDagger , Jon M. Huibregtse§, and Donald P. McDonnellDagger

From the Dagger  Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, North Carolina 27710 and the § Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712

The ubiquitin-protein ligase (E3), hRPF1/Nedd4, is a component of the ubiquitin-proteasome pathway responsible for substrate recognition and specificity. Although previously characterized as a regulator of the stability of cytoplasmic proteins, hRPF1/Nedd4 has also been suggested to have a role in the nucleus. However, in light of the cytoplasmic localization of hRPF1/Nedd4, it is unclear whether bona fide nuclear substrates of hRPF1/Nedd4 exist, and if so, what mechanism may allow a cytoplasmic ubiquitin ligase to manifest nuclear activity. Our search for nuclear substrates led to the identification of the human proline-rich transcript, brain-expressed (hPRTB) protein, the ubiquitination and degradation of which is regulated by hRPF1/Nedd4. Interestingly, hPRTB colocalizes with the splicing factor SC35 in nuclear speckles. Finally, we demonstrate that hRPF1/Nedd4 is indeed capable of entering the nucleus; however, the presence of a functional Rev-like nuclear export sequence in hRPF1/Nedd4 ensures a predominant cytoplasmic localization. Cumulatively, these findings highlight a nuclear role for the ubiquitin ligase hRPF1/Nedd4 and underscore cytoplasmic/nuclear localization as an important regulatory component of hRPF1/Nedd4-substrate recognition.

* This work was supported by a United States Army Research and Material Command Predoctoral Fellowship DAMD17-98-1-8072 (to M. H. H.) and by National Institutes of Health Grant DK50494 (to D. P. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Duke University Medical Center, Dept. of Pharmacology and Cancer Biology, Box 3813, Durham, NC 27710. Tel.: 919-684-6035; Fax: 919-681-7139; E-mail: mcdon016@acpub.duke.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 Mol. Cell. Biol.Home page
J.-E. Kim, I. Ryu, W. J. Kim, O.-K. Song, J. Ryu, M. Y. Kwon, J. H. Kim, and S. K. Jang
Proline-Rich Transcript in Brain Protein Induces Stress Granule Formation
Mol. Cell. Biol., January 15, 2008; 28(2): 803 - 813.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
S.-Y. Li, P. J. Davidson, N. Y. Lin, R. J. Patterson, J. L. Wang, and E. J. Arnoys
Transport of galectin-3 between the nucleus and cytoplasm. II. Identification of the signal for nuclear export
Glycobiology, July 1, 2006; 16(7): 612 - 622.
[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 Biol.Home page
S. M. Plafker, K. S. Plafker, A. M. Weissman, and I. G. Macara
Ubiquitin charging of human class III ubiquitin-conjugating enzymes triggers their nuclear import
J. Cell Biol., November 22, 2004; 167(4): 649 - 659.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. L. Stone, E. M. Anderson, R. T. Mullen, and D. R. Goring
ARC1 Is an E3 Ubiquitin Ligase and Promotes the Ubiquitination of Proteins during the Rejection of Self-Incompatible Brassica Pollen
PLANT CELL, April 1, 2003; 15(4): 885 - 898.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. R. Glodowski, J. M. Petersen, and J. E. Dahlberg
Complex Nuclear Localization Signals in the Matrix Protein of Vesicular Stomatitis Virus
J. Biol. Chem., November 27, 2002; 277(49): 46864 - 46870.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. F. Harvey, L. M. Shearwin-Whyatt, A. Fotia, R. G. Parton, and S. Kumar
N4WBP5, a Potential Target for Ubiquitination by the Nedd4 Family of Proteins, Is a Novel Golgi-associated Protein
J. Biol. Chem., March 8, 2002; 277(11): 9307 - 9317.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Sci.Home page
N. Shcherbik, S. Kumar, and D. S. Haines
Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1
J. Cell Sci., January 3, 2002; 115(5): 1041 - 1048.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Murillas, K. S. Simms, S. Hatakeyama, A. M. Weissman, and M. R. Kuehn
Identification of Developmentally Expressed Proteins That Functionally Interact with Nedd4 Ubiquitin Ligase
J. Biol. Chem., January 18, 2002; 277(4): 2897 - 2907.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.