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primary topic: The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae

The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae
type: Article
abstract: Stress-induced protein aggregation represents a major threat for cell survival and is also associated with various human disorders and cellular aging. The primary cellular response to aberrant protein conformations is the refolding of misfolded proteins by molecular chaperones or their elimination by AAA+ proteases. Once this first line of defense has been overrun, aggregated proteins are directed to specific compartments, thus protecting the cellular environment from potentially deleterious protein conformations. Organizing protein aggregates might also facilitate the recruitment of protein quality control components, thereby increasing the efficiency of aggregate removal in a subsequent phase. In Saccharomyces cerevisiae application of mild stress (37°C) results, upon inhibiting proteasomal degradation, in partitioning of misfolded proteins between two distinct compartments (Kaganovich, 2008). More mobile misfolded proteins, which are ubiquitylated and likely represent substrates for proteasomal degradation, are sequestered at the JUNQ (juxtanuclear quality control) compartment. Terminally aggregated, insoluble proteins are sorted to the peripheral IPOD (insoluble protein deposit) compartment that also harbors amyloidogenic proteins. To gain further insight into the spatio-temporal organization of misfolded proteins in Saccharomyces cerevisiae, I analyzed the localization of stress-induced protein aggregates by employing various fluorescent reporter proteins that either misfold upon stress application or bind to aggregated proteins. Since little is known about cellular factors involved in the sorting of misfolded proteins, I performed a candidate approach and focused on the Saccharomyces cerevisiae small heat shock proteins (sHsps), namely Hsp26 and Hsp42. I identified Hsp42 as an essential factor in the formation of IPOD-like inclusions. In hsp42 cells misfolded proteins do not accumulate in peripheral inclusions, but seem to be re-directed to the JUNQ. As Hsp42…
date: 2010
status: published
author list: authors
type: EPrint
type: DoctoralThesisEPrint
is part of: repository
has document: The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (PDF)
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subject: 570 Biowissenschaften, Biologie

The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (PDF)
type: Document
has file: 100607_Dissertation_Sebastian_Specht.pdf
has part: 100607_Dissertation_Sebastian_Specht.pdf

Sebastian Specht
type: Person
given name: Sebastian
family name: Specht

The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (Other)
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is version of: The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (PDF)
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The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (Other)
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The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (Other)
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The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (Other)
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The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae (Other)
type: Document
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primary topic: The Small Heat Shock Protein Hsp42 Controls the Spatio-Temporal Organization of Aggregated Proteins in Saccharomyces Cerevisiae

570 Biowissenschaften, Biologie
type: Concept
preferred label: 570 Life sciences @en