ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation.
ESCRT, not intralumenal fragments, sorts ubiquitinated vacuole membrane proteins for degradation.
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DOI:
10.1083/jcb.202012104
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发表时间:
2021-08-02
期刊:
影响因子:
--
通讯作者:
Li M
中科院分区:
文献类型:
--
作者:
Yang X;Reist L;Chomchai DA;Chen L;Arines FM;Li M
Yang et al. applied a microfluidics-based imaging method to resolve a controversy regarding how ubiquitinated lysosome membrane proteins are sorted into the lumen for degradation. ESCRTs, but not intralumenal fragments, are responsible for the sorting. The lysosome (or vacuole in fungi and plants) is an essential organelle for nutrient sensing and cellular homeostasis. In response to environmental stresses such as starvation, the yeast vacuole can adjust its membrane composition by selectively internalizing membrane proteins into the lumen for degradation. Regarding the selective internalization mechanism, two competing models have been proposed. One model suggests that the ESCRT machinery is responsible for the sorting. In contrast, the ESCRT-independent intralumenal fragment (ILF) pathway proposes that the fragment generated by homotypic vacuole fusion is responsible for the sorting. Here, we applied a microfluidics-based imaging method to capture the complete degradation process in vivo. Combining live-cell imaging with a synchronized ubiquitination system, we demonstrated that ILF cargoes are not degraded through intralumenal fragments. Instead, ESCRTs function on the vacuole membrane to sort them into the lumen for degradation. We further discussed challenges in reconstituting vacuole membrane protein degradation.
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DOI:
10.1083/jcb.201611029
发表时间:
2017-10-02
期刊:
The Journal of cell biology
影响因子:
--
作者:
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通讯作者:
Sakai Y
影响因子:
5.3
作者:
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通讯作者:
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影响因子:
16.6
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影响因子:
11.8
作者:
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通讯作者:
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影响因子:
7.7
作者:
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通讯作者:
Teis, David