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 Google Scholar
Google Scholar
Right arrow Articles by Bi, X.
Right arrow Articles by Mortin, M. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bi, X.
Right arrow Articles by Mortin, M. A.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, February 2003, p. 1014-1024, Vol. 23, No. 3
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.3.1014-1024.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Carboxy Terminus of Prospero Regulates Its Subcellular Localization

Xiaolin Bi,1 Andrey V. Kajava,2 Tamara Jones,1 Zoya N. Demidenko,1,{dagger} and Mark A. Mortin1*

Laboratory of Biochemistry, National Cancer Institute,1 Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Bethesda, Maryland 208922

Received 9 July 2002/ Returned for modification 29 August 2002/ Accepted 30 October 2002

Subcellular localization of the transcription factor Prospero is dynamic. For example, the protein is cytoplasmic in neuroblasts, nuclear in sheath cells, and degraded in newly formed neurons. The carboxy terminus of Prospero, including the homeodomain and Prospero domain, plays roles in regulating these changes. The homeodomain has two distinct subdomains, which exclude proteins from the nucleus, while the intact homeo/Prospero domain masks this effect. One subdomain is an Exportin-dependent nuclear export signal requiring three conserved hydrophobic residues, which models onto helix 1. Another, including helices 2 and 3, requires proteasome activity to degrade nuclear protein. Finally, the Prospero domain is missing in prosI13 embryos, thus unmasking nuclear exclusion, resulting in constitutively cytoplasmic protein. Multiple processes direct Prospero regulation of cell fate in embryonic nervous system development.


* Corresponding author. Mailing address: Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bldg. 37, Rm. 6134, 37 Convent Dr., Bethesda, MD 20892. Phone: (301) 435-2033. Fax: (301) 402-3095. E-mail: mortinm{at}mail.nih.gov.

{dagger} Present address: George Washington University Medical Center, Institute of Biomedical Sciences, Washington, DC 20037.


Molecular and Cellular Biology, February 2003, p. 1014-1024, Vol. 23, No. 3
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.3.1014-1024.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.







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 © 2003 by the American Society for Microbiology. All rights reserved.