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