Methods for Assessing the Regulation of a Kinase by the Rab GTPase Ypt1.
Methods for Assessing the Regulation of a Kinase by the Rab GTPase Ypt1.
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评估 Rab GTPase Ypt1 对激酶调节的方法。
DOI：
10.1007/978-1-0716-1346-7_14
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Ferro-Novick S
中科院分区：
文献类型：
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作者：
Wang J;Wang S;Ferro-Novick S
从内质网 (ER) 出芽的 COPII 包被囊泡通常会运输到高尔基体。然而，在饥饿期间，COPII 囊泡被重定向到巨自噬途径，成为自噬体的膜源。酪蛋白激酶 1 (CK1) Hrr25 对外壳的磷酸化是囊泡脱壳和膜融合的先决条件。 CK1 家族成员最初被认为是组成型活性激酶，通过其亚细胞定位进行调节。然而，最近的研究表明，Rab GTPase Ypt1 结合并激活 Hrr25（哺乳动物中的 CK1δ）以空间调节其激酶活性。与 Hrr25 在巨自噬中的直接作用一致，hrr25 和 dypt1 突变体在自噬体生物发生中存在缺陷。这些研究为 COPII 囊泡的行程如何在两种不同的运输途径上协调提供了见解。
COPII coated vesicles that bud from the endoplasmic reticulum (ER) normally traffic to the Golgi. However, during starvation, COPII vesicles are redirected to the macroautophagy pathway where they become a membrane source for autophagosomes. Phosphorylation of the coat by the casein kinase 1 (CK1), Hrr25, is a prerequisite for vesicle uncoating and membrane fusion. CK1 family members were initially thought to be constitutively active kinases that are regulated through their subcellular localization. Recent studies, however, have shown that the Rab GTPase Ypt1 binds to and activates Hrr25 (CK1δ in mammals) to spatially regulate its kinase activity. Consistent with a direct role for Hrr25 in macroautophagy,hrr25andypt1mutants are defective in autophagosome biogenesis. These studies have provided insights into how the itinerary of COPII vesicles is coordinated on two different trafficking pathways.