Journal
SCIENCE
Volume 367, Issue 6481, Pages 1039-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aay5359
Keywords
-
Categories
Funding
- NIH [DP2AI117923-01, R01GM043987, R01GM118396, R01GM123089, F31GM116441]
- NSF-Simons Center for Mathematical and Statistical Analysis of Biology at Harvard [1764269]
- Harvard Quantitative Biology Initiative
- Wellcome Grant [203276/Z/16/Z]
- Volkswagen Foundation
- Royal Society University Research Fellowship
- Wellcome Trust [203276/Z/16/Z] Funding Source: Wellcome Trust
Ask authors/readers for more resources
The actin fold is found in cytoskeletal polymers, chaperones, and various metabolic enzymes. Many actin-fold proteins, such as the carbohydrate kinases, do not polymerize. We found that Glk1, a Saccharomyces cerevisiae glucokinase, forms two-stranded filaments with ultrastructure that is distinct from that of cytoskeletal polymers. In cells, Glk1 polymerized upon sugar addition and depolymerized upon sugar withdrawal. Polymerization inhibits enzymatic activity; the Glk1 monomer-polymer equilibrium sets a maximum rate of glucose phosphorylation regardless of Glk1 concentration. A mutation that eliminated Glk1 polymerization alleviated concentration-dependent enzyme inhibition. Yeast containing nonpolymerizing Glk1 were less fit when growing on sugars and more likely to die when refed glucose. Glk1 polymerization arose independently from other actin-related filaments and may allow yeast to rapidly modulate glucokinase activity as nutrient availability changes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available