The regulation of Saccharomyces cerevisiae Snf1 protein kinase on glucose utilization is in a glucose-dependent manner.


Journal

Current genetics
ISSN: 1432-0983
Titre abrégé: Curr Genet
Pays: United States
ID NLM: 8004904

Informations de publication

Date de publication:
Apr 2021
Historique:
received: 06 08 2020
accepted: 21 11 2020
revised: 19 11 2020
pubmed: 2 1 2021
medline: 4 8 2021
entrez: 1 1 2021
Statut: ppublish

Résumé

Protein phosphorylation catalyzed by protein kinases is the major regulatory mechanism that controls many cellular processes. The regulatory mechanism of one protein kinase in different signals is distinguished, probably inducing multiple phenotypes. The Saccharomyces cerevisiae Snf1 protein kinase, a member of the AMP‑activated protein kinase family, plays important roles in the response to nutrition and environmental stresses. Glucose is an important nutrient for life activities of cells, but glucose repression and osmotic pressure could be produced at certain concentrations. To deeply understand the role of Snf1 in the regulation of nutrient metabolism and stress response of S. cerevisiae cells, the role and the regulatory mechanism of Snf1 in glucose metabolism are discussed in different level of glucose: below 1% (glucose derepression status), in 2% (glucose repression status), and in 30% glucose (1.66 M, an osmotic equivalent to 0.83 M NaCl). In summary, Snf1 regulates glucose metabolism in a glucose-dependent manner, which is associated with the different regulation on activation, localization, and signal pathways of Snf1 by varied glucose. Exploring the regulatory mechanism of Snf1 in glucose metabolism in different concentrations of glucose can provide insights into the study of the global regulatory mechanism of Snf1 in yeast and can help to better understand the complexity of physiological response of cells to stresses.

Identifiants

pubmed: 33385241
doi: 10.1007/s00294-020-01137-0
pii: 10.1007/s00294-020-01137-0
doi:

Substances chimiques

Protein Kinases EC 2.7.-
SNF1-related protein kinases EC 2.7.1.-
Protein Serine-Threonine Kinases EC 2.7.11.1
Glucose IY9XDZ35W2

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

245-248

Subventions

Organisme : the Scientific Research Foundation of Hainan University
ID : KYQD1660

Références

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Auteurs

Xue Lin (X)

College of Food Science and Engineering, Hainan University, Haikou, 570228, People's Republic of China. linxiaoxuelx@163.com.

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