Document Detail


Changes in Bni4 localization induced by cell stress in Saccharomyces cerevisiae.
MedLine Citation:
PMID:  20197406     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Septin complexes at the bud neck in Saccharomyces cerevisiae serve as a scaffold for proteins involved in signaling, cell cycle control, and cell wall synthesis. Many of these bind asymmetrically, associating with either the mother- or daughter-side of the neck. Septin structures are inherently apolar so the basis for the asymmetric binding remains unknown. Bni4, a regulatory subunit of yeast protein phosphatase type 1, Glc7, binds to the outside of the septin ring prior to bud formation and remains restricted to the mother-side of the bud neck after bud emergence. Bni4 is responsible for targeting Glc7 to the mother-side of the bud neck for proper deposition of the chitin ring. We show here that Bni4 localizes symmetrically, as two distinct rings on both sides of the bud neck following energy depletion or activation of cell cycle checkpoints. Our data indicate that loss of Bni4 asymmetry can occur via at least two different mechanisms. Furthermore, we show that Bni4 has a Swe1-dependent role in regulating the cell morphogenesis checkpoint in response to hydroxyurea, which suggests that the change in localization of Bni4 following checkpoint activation may help stabilize the cell cycle regulator Swe1 during cell cycle arrest.
Authors:
Jennifer R Larson; Lukasz Kozubowski; Kelly Tatchell
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-03-02
Journal Detail:
Title:  Journal of cell science     Volume:  123     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2010 Apr 
Date Detail:
Created Date:  2010-03-24     Completed Date:  2010-09-07     Revised Date:  2011-07-27    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1050-9     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Cycle / drug effects
Cell Cycle Proteins / biosynthesis*,  genetics,  metabolism*
Cell Line
Energy Metabolism
Hydroxyurea / pharmacology
Protein Binding
Protein Engineering
Protein Stability
Protein Transport / drug effects*
Protein-Serine-Threonine Kinases / metabolism*
Protein-Tyrosine Kinases / metabolism*
Recombinant Fusion Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins / biosynthesis*,  genetics,  metabolism*
Stress, Physiological*
Grant Support
ID/Acronym/Agency:
GM-47789/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bni4p protein, S cerevisiae; 0/Cell Cycle Proteins; 0/Recombinant Fusion Proteins; 0/Saccharomyces cerevisiae Proteins; 127-07-1/Hydroxyurea; EC 2.7.1.-/SWE1 protein, S cerevisiae; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.11.1/HSL1 protein, S cerevisiae; EC 2.7.11.1/Protein-Serine-Threonine Kinases
Comments/Corrections

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