Yip1A structures the mammalian endoplasmic reticulum.
Yip1A structures the mammalian endoplasmic reticulum.
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DOI：
10.1091/mbc.e09-12-1002
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发表时间：
2010-05-01
影响因子：
3.3
通讯作者：
Lee TH
中科院分区：
文献类型：
--
作者：
Dykstra KM;Pokusa JE;Suhan J;Lee TH
Yip 1A耗竭导致ER重组为堆叠和同心螺旋膜以及货物出口减缓。Yip 1A的网络扩散功能依赖于一个保守的残基。因此，一个保守的Yip 1A介导的ER网络分散机制可能调节细胞器的蛋白质输出功能。内质网（ER）的结构在特化细胞类型中经历高度调节的变化。一种经常观察到的变化类型是其重组为堆叠和同心螺纹膜，但其潜在的机制和货物出口的功能相关性尚不清楚。在这里，我们确定Yip 1A，一个保守的膜蛋白，ER和早期高尔基体之间的循环，作为ER组织的关键介质。Yip 1A的耗尽导致网络重组为多个微米级的同心螺旋。膜堆叠和螺纹形成正好与外壳蛋白（COP）II介导的蛋白质出口显着放缓。此外，由在COPII功能中没有作用的ER蛋白的外源表达驱动的螺旋形成也延迟了货物输出。因此，由Yip 1A缺失诱导的蛋白质输出的减缓可能归因于Yip 1A在调节ER网络分散中的近端作用。Yip 1A的内质网扩散功能被阻断的一个单一的保守氨基酸（E95 K）在其N-末端胞质结构域的改变。这些结果揭示了一个保守的Yip 1A介导的机制，ER膜组织，可能有助于调节货物出口的细胞器。
Yip1A depletion leads to reorganization of the ER into stacked and concentrically whorled membranes as well as a slowing of cargo export. The network dispersal function of Yip1A depends on a conserved residue. Thus, a conserved Yip1A-mediated ER network dispersal mechanism may regulate the protein export function of the organelle. The structure of the endoplasmic reticulum (ER) undergoes highly regulated changes in specialized cell types. One frequently observed type of change is its reorganization into stacked and concentrically whorled membranes, but the underlying mechanisms and functional relevance for cargo export are unknown. Here, we identify Yip1A, a conserved membrane protein that cycles between the ER and early Golgi, as a key mediator of ER organization. Yip1A depletion led to restructuring of the network into multiple, micrometer-sized concentric whorls. Membrane stacking and whorl formation coincided with a marked slowing of coat protein (COP)II-mediated protein export. Furthermore, whorl formation driven by exogenous expression of an ER protein with no role in COPII function also delayed cargo export. Thus, the slowing of protein export induced by Yip1A depletion may be attributed to a proximal role for Yip1A in regulating ER network dispersal. The ER network dispersal function of Yip1A was blocked by alteration of a single conserved amino acid (E95K) in its N-terminal cytoplasmic domain. These results reveal a conserved Yip1A-mediated mechanism for ER membrane organization that may serve to regulate cargo exit from the organelle.
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影响因子：
--
作者：
CARR, I;CARR, J
通讯作者：
CARR, J
影响因子：
3.3
作者：
Heidtman, M;Chen, CZ;Barlowe, C
通讯作者：
Barlowe, C
影响因子：
4
作者：
Kano, Fumi;Yamauchi, Shinobu;Murata, Masayuki
通讯作者：
Murata, Masayuki
影响因子：
11.4
作者：
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通讯作者：
Gallwitz, D
影响因子：
7.8
作者：
HWANG, KM;YANG, LC;SARTORELLI, AC
通讯作者：
SARTORELLI, AC