Literature DB >> 35945363

The role of the glycerol transporter channel Fps1p in cellular proteostasis during enhanced proteotoxic stress.

Kuljit Singh1,2, Ratnika Sethi2, Eshita Das2, Ipsita Roy3.   

Abstract

In response to osmotic shock, the components of high-osmolarity glycerol (HOG) pathway regulate the level of intracellular glycerol in yeast and ensure cell survival. Glycerol is a compatible solute and a stabiliser of proteins. Its role in maintaining proteostasis is less explored. We show that mild stress in the form of dietary restriction leads to increased glycerol level which increases cell viability. However, dietary restriction coupled with protein aggregation decreases intracellular glycerol level and attenuates cell viability. The transcript level of FPS1, the glycerol transporter channel, remains unchanged. However, its activity is altered under enhanced proteotoxic stress. Our results provide evidence for a probable role of the Fps1p channel in the cellular proteostasis network. KEY POINTS: • Dietary restriction led to increased accumulation of glycerol in Fps1-deleted yeast cells. • This led to lower protein aggregation in these cells. • Increased production of glycerol under dietary restriction was not linked to increased level of Fps1.
© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.

Entities:  

Keywords:  Compatible osmolyte; Glycerol; HOG pathway; Osmoregulation; Proteostasis network

Mesh:

Substances:

Year:  2022        PMID: 35945363     DOI: 10.1007/s00253-022-12118-3

Source DB:  PubMed          Journal:  Appl Microbiol Biotechnol        ISSN: 0175-7598            Impact factor:   5.560


  63 in total

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Journal:  Hum Mol Genet       Date:  2000-11-22       Impact factor: 6.150

2.  Detection and quantification of tau aggregation using a membrane filter assay.

Authors:  Edward Chang; Jeff Kuret
Journal:  Anal Biochem       Date:  2007-09-19       Impact factor: 3.365

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Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

4.  The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation.

Authors:  R Ansell; K Granath; S Hohmann; J M Thevelein; L Adler
Journal:  EMBO J       Date:  1997-05-01       Impact factor: 11.598

5.  Stabilization of beta-lactoglobulin by polyols and sugars against temperature-induced denaturation involves diverse and specific structural regions of the protein.

Authors:  Alberto Barbiroli; Mauro Marengo; Dimitrios Fessas; Enzio Ragg; Stefano Renzetti; Francesco Bonomi; Stefania Iametti
Journal:  Food Chem       Date:  2017-04-21       Impact factor: 7.514

6.  Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.

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Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-15       Impact factor: 11.205

7.  GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway.

Authors:  J Albertyn; S Hohmann; J M Thevelein; B A Prior
Journal:  Mol Cell Biol       Date:  1994-06       Impact factor: 4.272

8.  The yeast osmostress response is carbon source dependent.

Authors:  Roja Babazadeh; Petri-Jaan Lahtvee; Caroline B Adiels; Mattias Goksör; Jens B Nielsen; Stefan Hohmann
Journal:  Sci Rep       Date:  2017-04-20       Impact factor: 4.379

9.  Protein aggregation activates erratic stress response in dietary restricted yeast cells.

Authors:  Ankan Kumar Bhadra; Eshita Das; Ipsita Roy
Journal:  Sci Rep       Date:  2016-09-16       Impact factor: 4.379

10.  Rewiring yeast osmostress signalling through the MAPK network reveals essential and non-essential roles of Hog1 in osmoadaptation.

Authors:  Roja Babazadeh; Takako Furukawa; Stefan Hohmann; Kentaro Furukawa
Journal:  Sci Rep       Date:  2014-04-15       Impact factor: 4.379

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