Suppr超能文献

一种蛋白质和脂质激酶复合物在分泌蛋白分选过程中的重要作用。

An essential role for a protein and lipid kinase complex in secretory protein sorting.

作者信息

Herman P K, Stack J H, Emr S D

机构信息

Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

出版信息

Trends Cell Biol. 1992 Dec;2(12):363-8. doi: 10.1016/0962-8924(92)90048-r.

Abstract

Yeast genetics has identified more than 40 genes involved in the biogenesis and maintenance of the yeast lysosome-like vacuole. Recent data on two of these genes, VPS15 and VPS34, are beginning to provide some fundamental insights into the mechanisms governing protein sorting within the eukaryotic secretory pathway. VPS15 and VPS34 encode a novel protein kinase and a phosphatidylinositol 3-kinase, respectively, that function together as components of a membrane-associated signal transduction complex. These studies of the VPS15-VPS34 complex indicate that intracellular protein trafficking decisions may be regulated by protein phosphorylation and phosphatidylinositol signalling events.

摘要

酵母遗传学已鉴定出40多个参与酵母溶酶体样液泡生物合成与维持的基因。最近有关其中两个基因VPS15和VPS34的数据,开始为真核生物分泌途径中蛋白质分选调控机制提供一些基本见解。VPS15和VPS34分别编码一种新型蛋白激酶和一种磷脂酰肌醇3激酶,它们作为膜相关信号转导复合物的组成部分共同发挥作用。对VPS15 - VPS34复合物的这些研究表明,细胞内蛋白质运输决策可能受蛋白质磷酸化和磷脂酰肌醇信号事件调控。

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验