Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
Cytoplasm-to-vacuole targeting and autophagy employ the same machinery to deliver proteins to the yeast vacuole
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DOI：
10.1073/pnas.93.22.12304
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发表时间：
1996-10-29
影响因子：
11.1
通讯作者：
Klionsky, DJ
中科院分区：
文献类型：
--
作者：
Scott, SV;HefnerGravink, A;Klionsky, DJ
空泡蛋白氨肽酶I（API）使用一种新的细胞质-空泡靶向（Cvt）途径。互补分析缺陷的酵母突变体的细胞质到液泡蛋白质靶向（cvt）和自噬（apg）揭示了这两组突变体之间的7个重叠互补组。此外，所有14个apg互补组在向液泡递送API方面都有缺陷。类似地，大多数非重叠的cvt互补组似乎在自噬中至少有部分缺陷。蛋白质递送速率的动力学分析表明，自噬蛋白的摄取是由氮饥饿诱导的，而CVT是一个组成性的生物合成途径。然而，控制Cvt的机制受到氮饥饿的影响，因为由API过表达引起的靶向缺陷可以通过诱导自噬来挽救。
The vacuolar protein aminopeptidase I (API) uses a novel cytoplasm-to-vacuole targeting (Cvt) pathway. Complementation analysis of yeast mutants defective for cytoplasm-to-vacuole protein targeting (cvt) and autophagy (apg) revealed seven overlapping complementation groups between these two sets of mutants. In addition, all 14 apg complementation groups are defective in the delivery of API to the vacuole. Similarly, the majority of nonoverlapping cvt complementation groups appear to he at least partially defective in autophagy. Kinetic analyses of protein delivery rates indicate that autophagic protein uptake is induced by nitrogen starvation, whereas Cvt is a constitutive biosynthetic pathway. However, the machinery governing Cvt is affected by nitrogen starvation as targeting defects resulting from API overexpression can be rescued by induction of autophagy.