| The polarisome is required for segregation and retrograde transport of protein aggregates. | |
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MedLine Citation:
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PMID: 20141839 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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Beidong Liu; Lisa Larsson; Antonio Caballero; Xinxin Hao; David Oling; Julie Grantham; Thomas Nystr?m |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Cell Volume: 140 ISSN: 1097-4172 ISO Abbreviation: Cell Publication Date: 2010 Jan |
Date Detail:
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Created Date: 2010-02-09 Completed Date: 2010-02-25 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0413066 Medline TA: Cell Country: United States |
Other Details:
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Languages: eng Pagination: 257-67 Citation Subset: IM |
Copyright Information:
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Copyright 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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Department of Cell and Molecular Biology, University of Gothenburg, Medicinaregatan 9C, 413 90 G?teborg, Sweden. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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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:
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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:
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Cell. 2010 Jan 22;140(2):176-8
[PMID:
20141830
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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