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Published online before print July 18, 2005, 10.1101/gad.1327405
GENES & DEVELOPMENT 19:1767-1772, 2005
©2005 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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RESEARCH COMMUNICATION

Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response

Haiyun Song1,4, Minghua Nie1,2, Feng Qiao1,2,3, James U. Bowie1,2,3 and Albert J. Courey1,2,5

1 Department of Chemistry and Biochemistry, 2 Molecular Biology Institute, 3 UCLA-DOE Institute of Genomics and Proteomics, University of California, Los Angeles, Los Angeles, California 90095, USA

Phosphorylation of Yan, a major target of Ras signaling, leads to Crm1-dependent Yan nuclear export, a response that is regulated by Yan polymerization. Yan SAM (sterile {alpha} motif) domain mutations preventing polymerization result in Ras-independent, but Crm1-dependent Yan nuclear export, suggesting that polymerization prevents Yan export. Mae, which depolymerizes Yan, competes with Crm1 for binding to Yan. Phosphorylation of Yan favors Crm1 in this competition and counteracts inhibition of nuclear export by Mae. These findings suggest that, prior to Ras activation, the Mae/Yan interaction blocks premature nuclear export of Yan monomers. After activation, transcriptional up-regulation of Mae apparently leads to complete depolymerization and export of Yan.

[Keywords: Yan; Mae; Crm1; SAM domain; Ras; nuclear export]

Received April 26, 2005; revised version accepted June 3, 2005.

Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1327405.

4 Present address: Institute of Molecular Biology, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.

5 Corresponding author.
E-MAIL courey{at}chem.ucla.edu; FAX (310) 206-4038.


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