Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.

Distinct N-terminal regions of the exomer secretory vesicle cargo Chs3 regulate its trafficking itinerary.
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DOI:
10.3389/fcell.2014.00047
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发表时间:
2014
影响因子:
5.5
通讯作者:
Fromme JC
Fromme JC
中科院分区:
生物学2区
文献类型:
--
作者:
Weiskoff AM;Fromme JC

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细胞通过将细胞器分选成小泡来运输细胞器之间的完整膜蛋白。货物适配器的作用是识别跨膜货物中的分拣信号,并与有助于囊泡生物发生的被膜复合体相互作用。目前还没有鉴定出产生从反式高尔基体网络(TGN)到质膜的分泌囊泡的外壳蛋白,但外聚体复合体被鉴定为一种货物适配器复合体,在这一途径中介导了几种蛋白质的运输。Chs3是研究最充分的外源物质,它与细胞周期同步地在TGN和质膜之间循环,为研究响应信号循环的蛋白质的调控提供了机会。在这里,我们证明了Chs3N末端的不同片段介导了不同的转运步骤。残基10-27是已知的介导滞留的物质,似乎也在内化过程中发挥作用。残基28-52参与运输到质膜和内小体的循环,以防止液泡中的降解。我们还给出了与外聚体复合体结合的残基10-27的晶体结构,表明不同的货物适配器可以竞争结合这一片段,为调节提供了一种潜在的机制。
Cells transport integral membrane proteins between organelles by sorting them into vesicles. Cargo adaptors act to recognize sorting signals in transmembrane cargos and to interact with coat complexes that aid in vesicle biogenesis. No coat proteins have yet been identified that generate secretory vesicles from the trans-Golgi network (TGN) to the plasma membrane, but the exomer complex has been identified as a cargo adaptor complex that mediates transport of several proteins in this pathway. Chs3, the most well-studied exomer cargo, cycles between the TGN and the plasma membrane in synchrony with the cell cycle, providing an opportunity to study regulation of proteins that cycle in response to signaling. Here we show that different segments of the Chs3 N-terminus mediate distinct trafficking steps. Residues 10–27, known to mediate retention, also appear to play a role in internalization. Residues 28–52 are involved in transport to the plasma membrane and recycling out of endosomes to prevent degradation in the vacuole. We also present the crystal structure of residues 10–27 bound to the exomer complex, suggesting different cargo adaptors could compete for binding to this segment, providing a potential mechanism for regulation.
CHS7P是一种新蛋白,参与控制蛋白质从内质网的输出,该蛋白质专门从事酿酒酵母中几丁质合成的调节。
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