Rutter Jared, Probst Brandon L, McKnight Steven L
Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.
Cell. 2002 Oct 4;111(1):17-28. doi: 10.1016/s0092-8674(02)00974-1.
PAS kinase is a serine/threonine kinase regulated in cis by a PAS domain. A genetic study of the two PAS kinase genes in budding yeast gave evidence of the involvement of these enzymes in the control of sugar metabolism and translation. Using a biochemical screen for PAS kinase substrates, three translation factors were identified as direct phosphorylation targets. PAS kinase was also found to phosphorylate UDP-glucose pyrophosphorylase and glycogen synthase, the enzymes catalyzing the two final steps in the glycogen biosynthetic pathway. Genetic, biochemical, and physiological data provide evidence that both of these enzymes are inhibited by PAS kinase-dependent phosphorylation, thereby downregulating carbohydrate storage. These studies provide evidence of a cell-autonomous signaling system that both controls and connects the balance of fuel consumption/storage to protein synthesis.
PAS激酶是一种由PAS结构域顺式调控的丝氨酸/苏氨酸激酶。对芽殖酵母中两个PAS激酶基因的遗传学研究表明,这些酶参与了糖代谢和翻译的调控。通过对PAS激酶底物进行生化筛选,鉴定出三种翻译因子为直接磷酸化靶点。还发现PAS激酶可磷酸化UDP-葡萄糖焦磷酸化酶和糖原合酶,这两种酶催化糖原生物合成途径的最后两个步骤。遗传学、生化和生理学数据表明,这两种酶均受PAS激酶依赖性磷酸化的抑制,从而下调碳水化合物的储存。这些研究证明了一种细胞自主信号系统,该系统既能控制燃料消耗/储存的平衡,又能将其与蛋白质合成联系起来。