Document Detail


The polarisome is required for segregation and retrograde transport of protein aggregates.
MedLine Citation:
PMID:  20141839     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The paradigm sirtuin, Sir2p, of budding yeast is required for establishing cellular age asymmetry, which includes the retention of damaged and aggregated proteins in mother cells. By establishing the global genetic interaction network of SIR2 we identified the polarisome, the formin Bni1p, and myosin motor protein Myo2p as essential components of the machinery segregating protein aggregates during mitotic cytokinesis. Moreover, we found that daughter cells can clear themselves of damage by a polarisome- and tropomyosin-dependent polarized flow of aggregates into the mother cell compartment. The role of Sir2p in cytoskeletal functions and polarity is linked to the CCT chaperonin in sir2Delta cells being compromised in folding actin. We discuss the findings in view of recent models hypothesizing that polarity may have evolved to avoid clonal senescence by establishing an aging (soma-like) and rejuvenated (germ-like) lineage.
Authors:
Beidong Liu; Lisa Larsson; Antonio Caballero; Xinxin Hao; David Oling; Julie Grantham; Thomas Nystr?m
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell     Volume:  140     ISSN:  1097-4172     ISO Abbreviation:  Cell     Publication Date:  2010 Jan 
Date Detail:
Created Date:  2010-02-09     Completed Date:  2010-02-25     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0413066     Medline TA:  Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  257-67     Citation Subset:  IM    
Copyright Information:
Copyright 2010 Elsevier Inc. All rights reserved.
Affiliation:
Department of Cell and Molecular Biology, University of Gothenburg, Medicinaregatan 9C, 413 90 G?teborg, Sweden.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism
Chaperonins / metabolism
Heat-Shock Proteins / metabolism
Microfilament Proteins / metabolism
Mitosis
Organelles / metabolism
Protein Transport
Saccharomyces cerevisiae / cytology*,  metabolism*
Saccharomyces cerevisiae Proteins / metabolism
Silent Information Regulator Proteins, Saccharomyces cerevisiae / metabolism
Sirtuin 2 / metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Bni1 protein, S cerevisiae; 0/Heat-Shock Proteins; 0/Microfilament Proteins; 0/Saccharomyces cerevisiae Proteins; 0/Silent Information Regulator Proteins, Saccharomyces cerevisiae; 143012-44-6/HsP104 protein, S cerevisiae; EC 3.5.1.-/SIR2 protein, S cerevisiae; EC 3.5.1.-/Sirtuin 2; EC 3.6.1.-/Chaperonins
Comments/Corrections
Comment In:
Cell. 2010 Jan 22;140(2):176-8   [PMID:  20141830 ]

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