Abstract
Molecular chaperones are an essential group of proteins required to maintain proper protein homeostasis in the cell and include Hsp40, Hsp60, Hsp70, Hsp90, and Hsp100 among others. Hsp110 proteins form a subfamily of the Hsp70 family and seem to primarily function as nucleotide exchange factors for the Hsp70s. Data to date suggest that Hsp110 together with Hsp70 are required to ensure proper spindle assembly and nuclear distribution during cell division. More specifically, we propose that an Hsp110-Hsp70 complex modulates the activity and directionality of the kinesin-5 motor, Cin8, which is required for spindle elongation. The modulation of spindle length by molecular chaperones might be a mechanism by which cell division can be controlled especially under proteostatic stress.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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HSP110 Heat-Shock Proteins / chemistry
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HSP110 Heat-Shock Proteins / genetics
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HSP110 Heat-Shock Proteins / metabolism*
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HSP70 Heat-Shock Proteins / chemistry
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HSP70 Heat-Shock Proteins / genetics
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HSP70 Heat-Shock Proteins / metabolism*
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Kinetochores / metabolism
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Microtubules / metabolism
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Models, Biological
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Models, Molecular
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Molecular Chaperones / chemistry
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Mutation
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Protein Binding
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Spindle Apparatus / metabolism*
Substances
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HSP110 Heat-Shock Proteins
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HSP70 Heat-Shock Proteins
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Molecular Chaperones
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SSE1 protein, S cerevisiae
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SSE2 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins