Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae
Lap3 is a selective target of autophagy in yeast, Saccharomyces cerevisiae
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DOI：
10.1016/j.bbrc.2008.11.084
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发表时间：
2009-01-16
影响因子：
3.1
通讯作者：
Ohsumi, Yoshinori
中科院分区：
文献类型：
--
作者：
Kageyama, Takuya;Suzuki, Kuninori;Ohsumi, Yoshinori
自噬是饥饿时溶酶体/空泡中细胞质成分的主要非选择性降解系统。在酵母中，自噬也参与了液泡水解酶Ape 1的选择性转运，作为生物合成途径。Ald 6是一种可溶性细胞质酶，通过自噬优先从细胞质中消除。然而，关于Ald 6靶向自噬体的机制知之甚少。在这里，我们表明，Lap 3，可溶性胞质半胱氨酸蛋白酶，空间与Ape 1和选择性运输到液泡在氮饥饿。Lap 3的转运速率远高于Ald 6，与Ape 1相似。此外，ATG 11和ATG 19，Ape 1运输的必要因素，是重要的Lap 3运输。大多数Lap 3是在几个小时内降解的液泡中，相反，Ape 1，因此，我们得出结论，Ape 1生物合成所需的机器用于选择性降解Lap 3。(C)2008年爱思唯尔公司All rights reserved.
Autophagy is a primarily non-selective degradation system of cytoplasmic constituents in lysosomes/vacuoles during starvation. In yeast, autophagy is also involved in the selective transport of Ape1, a vacuolar hydrolase, as a biosynthetic route. Ald6, a soluble cytoplasmic enzyme, is preferentially eliminated from cytoplasm via autophagy. However, little is known about the mechanisms of Ald6 targeting to autophagosomes. Here, we show that Lap3, a soluble cytosolic cysteine protease, is spatially associated with Ape1 and selectively transported to the vacuole during nitrogen Starvation. The rate of Lap3 transport is much higher than that of Ald6 and is similar to that of Ape1. Moreover, ATG11 and ATG19, essential factors for Ape1 transport, are important for Lap3 transport. Most Lap3 is degraded within a couple of hours in the vacuole in contrast to Ape1; therefore, we conclude that the machinery required for Ape1 biosynthesis is used for selective degradation of Lap3. (C) 2008 Elsevier Inc. All rights reserved.