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Vol. 10, Issue 5, 1395-1407, May 1999
Departments of Molecular Biology and Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
Transcriptional induction of many stress-response genes is
dependent on stress-induced nuclear accumulation of stress-activated protein kinases (SAPKs). In the fission yeast
Schizosaccharomyces pombe, nuclear accumulation of the
SAPK Spc1 (also known as StyI) requires activating phosphorylation
catalyzed by the SAPK kinase Wis1; however, it is unknown whether the
localization of Spc1 is regulated by nuclear transport factors. Herein
are reported studies that show that Spc1 localization is regulated by
active transport mechanisms during osmotic stress. Nuclear import of Spc1 requires Pim1, a homologue of the guanine nucleotide exchange factor RCC1 that is essential for nucleocytoplasmic shuttling of
proteins. Nuclear export of Spc1 is regulated by the export factor
Crm1. An Spc1-Crm1 complex forms as Spc1 is exported from the nucleus.
Wis1 and the tyrosine phosphatases Pyp1 and Pyp2 that inactivate Spc1
are excluded from the nucleus by a Crm1-independent mechanism; hence
the nuclear import of Spc1 leads to transient isolation from its
regulatory proteins. Thus, active nucleocytoplasmic shuttling is
required for both the function and regulation of Spc1 during the
osmotic shock response.
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