美国哈佛大学Ethan C. Garner、Andrew W. Murray等研究人员合作发现，肌动蛋白ATP酶家族的聚合调节酵母己糖激酶活性。2020年2月28日，《科学》发表了这一成果。

Title: Polymerization in the actin ATPase clan regulates hexokinase activity in yeast

Author: Patrick R. Stoddard, Eric M. Lynch, Daniel P. Farrell, Annie M. Dosey, Frank DiMaio, Tom A. Williams, Justin M. Kollman, Andrew W. Murray, Ethan C. Garner

Issue&Volume: 2020/02/28

Abstract: AbstractThe 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.

DOI: 10.1126/science.aay5359

Source: https://science.sciencemag.org/content/367/6481/1039