Eukaryotic Cell
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF 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 Lu, J. M.-Y.
Right arrow Articles by Fassler, J. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lu, J. M.-Y.
Right arrow Articles by Fassler, J. S.

 Previous Article  |  Next Article 

Eukaryotic Cell, December 2003, p. 1304-1314, Vol. 2, No. 6
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.6.1304-1314.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Saccharomyces cerevisiae Histidine Phosphotransferase Ypd1p Shuttles between the Nucleus and Cytoplasm for SLN1-Dependent Phosphorylation of Ssk1p and Skn7p

Jade Mei-Yeh Lu, Robert J. Deschenes, and Jan S. Fassler*

Departments of Biological Sciences and Biochemistry, University of Iowa, Iowa City, Iowa 52242

Received 23 June 2003/ Accepted 10 September 2003

Sln1p is a plasma membrane-localized two-component histidine kinase that functions as an osmotic stress sensor in Saccharomyces cerevisiae. Changes in osmotic pressure modulate Sln1p kinase activity, which, together with Ypd1p, a phosphorelay intermediate, changes the phosphorylation status of two response regulators, Ssk1p and Skn7p. Ssk1p controls the activity of the HOG1 mitogen-activated protein kinase pathway. Skn7p is a nuclearly localized transcription factor that regulates genes involved in cell wall integrity and other processes. Subcellular compartmentalization may therefore play an important role in eukaryotic two-component pathway regulation. We have studied the subcellular localization of SLN1 pathway components and find that Ypd1p is a dynamic protein with a role in shuttling the osmotic stress signal from Sln1p to Ssk1p in the cytosol and to Skn7p in the nucleus. The need to translocate the signal into different intracellular compartments contributes a spatial dimension to eukaryotic two-component pathways compared to the prototypical two-component pathways of prokaryotes.


* Corresponding author. Mailing address: Department of Biological Sciences, University of Iowa, Iowa City, IA 52242. Phone: (319) 335-1542. Fax: (319) 335-1069. E-mail: jan-fassler{at}uiowa.edu.


Eukaryotic Cell, December 2003, p. 1304-1314, Vol. 2, No. 6
1535-9778/03/$08.00+0     DOI: 10.1128/EC.2.6.1304-1314.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Appl. Environ. Microbiol. Infect. Immun. J. Bacteriol.
Mol. Cell Biol. Microbiol. Mol. Biol. Rev. ALL ASM JOURNALS
Copyright © 2003 by the American Society for Microbiology.