Journal
GENES & DEVELOPMENT
Volume 19, Issue 15, Pages 1767-1772Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1327405
Keywords
Yan; Mae; Crm1; SAM domain; Ras; nuclear export
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Funding
- NCI NIH HHS [R01 CA081000] Funding Source: Medline
- NIGMS NIH HHS [R01 GM63596, R01 GM063596, R01 GM44522, R01 GM044522] Funding Source: Medline
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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 a 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.
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