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Hsp70-nucleotide exchange factor (NEF) Fes1 has non-NEF roles in degradation of gluconeogenic enzymes and cell wall integrity.
- Source :
-
PLoS genetics [PLoS Genet] 2019 Jun 26; Vol. 15 (6), pp. e1008219. Date of Electronic Publication: 2019 Jun 26 (Print Publication: 2019). - Publication Year :
- 2019
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Abstract
- Fes1 is a conserved armadillo repeat-containing Hsp70 nucleotide exchange factor important for growth at high temperature, proteasomal protein degradation and prion propagation. Depleting or mutating Fes1 induces a stress response and causes defects in these processes that are ascribed solely to disruption of Fes1 regulation of Hsp70. Here, we find Fes1 was essential for degradation of gluconeogenic enzymes by the vacuole import and degradation (Vid) pathway and for cell wall integrity (CWI), which is crucial for growth at high temperature. Unexpectedly, Fes1 mutants defective in physical or functional interaction with Hsp70 retained activities that support Vid and CWI. Fes1 and the Fes1 mutants bound to the Vid substrate Fbp1 in vitro and captured Slt2, a signaling kinase that regulates CWI, from cell lysates. Our data show that the armadillo domain of Fes1 binds proteins other than Hsp70, that Fes1 has important Hsp70-independent roles in the cell, and that major growth defects caused by depleting Fes1 are due to loss of these functions rather than to loss of Hsp70 regulation. We uncovered diverse functions of Fes1 beyond its defined role in regulating Hsp70, which points to possible multi-functionality among its conserved counterparts in other organisms or organelles.<br />Competing Interests: The authors have declared that no competing interests exist.
- Subjects :
- Cytosol metabolism
Gluconeogenesis genetics
Glucose genetics
Glucose metabolism
HSP70 Heat-Shock Proteins genetics
Molecular Chaperones genetics
Saccharomyces cerevisiae genetics
Vacuoles genetics
Cell Wall genetics
Guanine Nucleotide Exchange Factors genetics
Intracellular Signaling Peptides and Proteins genetics
Mitogen-Activated Protein Kinases genetics
Saccharomyces cerevisiae Proteins genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1553-7404
- Volume :
- 15
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- PLoS genetics
- Publication Type :
- Academic Journal
- Accession number :
- 31242183
- Full Text :
- https://doi.org/10.1371/journal.pgen.1008219