MCB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Catez, F.
Right arrow Articles by Diaz, J.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Catez, F.
Right arrow Articles by Diaz, J.-J.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2002, p. 1126-1139, Vol. 22, No. 4
0270-7306/01/$04.00+0     DOI: 10.1128/MCB.22.4.1126-1139.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Unique Motif for Nucleolar Retention and Nuclear Export Regulated by Phosphorylation

Frédéric Catez,1,{dagger} Monique Erard,2 Nathalie Schaerer-Uthurralt,1 Karine Kindbeiter,1 Jean-Jacques Madjar,1,{ddagger} and Jean-Jacques Diaz1*

INSERM U369, Faculté de Médecine Lyon-René Théophile Hyacinthe Laennec, 69372 Lyon Cedex 08,1 Institut de Pharmacologie et de Biologie Structurale, 31077 Toulouse Cedex 4, France2

Received 26 July 2001/ Returned for modification 7 September 2001/ Accepted 8 November 2001

By microinjecting purified glutathione S-transferase linked to all or parts of herpes simplex virus type 1 US11 protein into either the nucleus or the cytoplasm, we have demonstrated that this nucleolar protein exhibits a new type of localization signal controlling both retention in nucleoli and export to the cytoplasm. Saturated mutagenesis combined with computer modeling allowed us to draw the fine-structure map of this domain, revealing a new proline-rich motif harboring both activities, which are temperature dependent and regulated by phosphorylation. Finally, crossing the nuclear pore complex from the cytoplasm to the nucleus is an energy-dependent process for US11 protein, while getting to nucleoli through the nucleoplasm is energy independent.


* Corresponding author. Mailing address: INSERM U369, Faculté de Médecine Lyon-R.T.H. Laennec, 7, Rue Guillaume Paradin, 69372 Lyon Cedex 08, France. Phone: 33-(0)4-78-77-87-17. Fax: 33-(0)4-78-77-87-36. E-mail: diaz{at}laennec.univ-lyon1.fr.

{dagger} Present address: Protein Section, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892.

{ddagger} Present address: DIAMB, Université Claude Bernard Lyon-1, 69622 Villeurbanne Cedex, France.


Molecular and Cellular Biology, February 2002, p. 1126-1139, Vol. 22, No. 4
0022-538X/01/$04.00+0     DOI: 10.1128/MCB.22.4.1126-1139.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2002 by the American Society for Microbiology. All rights reserved.