Schu P V, Takegawa K, Fry M J, Stack J H, Waterfield M D, Emr S D
Division of Cellular and Molecular Medicine, University of California, San Diego, School of Medicine.
Science. 1993 Apr 2;260(5104):88-91. doi: 10.1126/science.8385367.
The VPS34 gene product (Vps34p) is required for protein sorting to the lysosome-like vacuole of the yeast Saccharomyces cerevisiae. Vps34p shares significant sequence similarity with the catalytic subunit of bovine phosphatidylinositol (PI) 3-kinase [the 110-kilodalton (p110) subunit of PI 3-kinase], which is known to interact with activated cell surface receptor tyrosine kinases. Yeast strains deleted for the VPS34 gene or carrying vps34 point mutations lacked detectable PI 3-kinase activity and exhibited severe defects in vacuolar protein sorting. Overexpression of Vps34p resulted in an increase in PI 3-kinase activity, and this activity was specifically precipitated with antisera to Vps34p. VPS34 encodes a yeast PI 3-kinase, and this enzyme appears to regulate intracellular protein trafficking decisions.
VPS34基因产物(Vps34p)对于蛋白质分选至酿酒酵母的类溶酶体液泡是必需的。Vps34p与牛磷脂酰肌醇(PI)3激酶的催化亚基[PI 3激酶的110千道尔顿(p110)亚基]具有显著的序列相似性,已知该亚基与活化的细胞表面受体酪氨酸激酶相互作用。缺失VPS34基因或携带vps34点突变的酵母菌株缺乏可检测到的PI 3激酶活性,并在液泡蛋白分选方面表现出严重缺陷。Vps34p的过表达导致PI 3激酶活性增加,并且这种活性可被抗Vps34p抗血清特异性沉淀。VPS34编码一种酵母PI 3激酶,并且这种酶似乎调节细胞内蛋白质运输决策。