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A piggybacking mechanism enables peroxisomal localization of the glyoxylate cycle enzyme Mdh2 in yeast
Journal of Cell Science ( IF 3.3 ) Pub Date : 2020-12-17 , DOI: 10.1242/jcs.244376
Shiran Gabay-Maskit 1 , Luis Daniel Cruz-Zaragoza 2 , Nadav Shai 1 , Miriam Eisenstein 1 , Chen Bibi 1 , Nir Cohen 1 , Tobias Hansen 2 , Eden Yifrach 1 , Nofar Harpaz 1 , Ruth Belostotsky 3 , Wolfgang Schliebs 2 , Maya Schuldiner 4 , Ralf Erdmann 5 , Einat Zalckvar 4
Affiliation  

Shiran Gabay-Maskit, Luis Daniel Cruz-Zaragoza, Nadav Shai, Miriam Eisenstein, Chen Bibi, Nir Cohen, Tobias Hansen, Eden Yifrach, Nofar Harpaz, Ruth Belostotsky, Wolfgang Schliebs, Maya Schuldiner, Ralf Erdmann, and Einat Zalckvar

Eukaryotic cells have evolved organelles that allow the compartmentalization and regulation of metabolic processes. Knowledge of molecular mechanisms that allow temporal and spatial organization of enzymes within organelles is therefore crucial for understanding eukaryotic metabolism. Here, we show that the yeast malate dehydrogenase 2 (Mdh2) is dually localized to the cytosol and to peroxisomes and is targeted to peroxisomes via association with Mdh3 and a Pex5-dependent piggybacking mechanism. This dual localization of Mdh2 contributes to our understanding of the glyoxylate cycle and provides a new perspective on compartmentalization of cellular metabolism, which is critical for the perception of metabolic disorders and aging.



中文翻译:

搭载机制使乙醛酸循环酶 Mdh2 在酵母中定位于过氧化物酶体

Shiran Gabay-Maskit、Luis Daniel Cruz-Zaragoza、Nadav Shai、Miriam Eisenstein、Chen Bibi、Nir Cohen、Tobias Hansen、Eden Yifrach、Nofar Harpaz、Ruth Belostotsky、Wolfgang Schliebs、Maya Schuldiner、Ralf Erdmann 和 Einat Zalckvar

真核细胞已经进化出能够划分和调节代谢过程的细胞器。因此,了解细胞器内酶的时间和空间组织的分子机制对于理解真核代谢至关重要。在这里,我们表明酵母苹果酸脱氢酶 2 (Mdh2) 双重定位于胞质溶胶和过氧化物酶体,并通过与 Mdh3 关联和 Pex5 依赖的捎带机制靶向过氧化物酶体。Mdh2 的这种双重定位有助于我们对乙醛酸循环的理解,并为细胞代谢的区室化提供了新的视角,这对于代谢紊乱和衰老的感知至关重要。

更新日期:2021-01-04
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