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从边缘回归:从末端隔室中回收膜蛋白:从液泡和内溶酶体中回收膜蛋白的意外途径。

Back From the Brink: Retrieval of Membrane Proteins From Terminal Compartments: Unexpected Pathways for Membrane Protein Retrieval From Vacuoles and Endolysosomes.

机构信息

University of Cambridge, Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Addenbrookes Hospital, CB2 0XY, UK.

出版信息

Bioessays. 2019 Mar;41(3):e1800146. doi: 10.1002/bies.201800146. Epub 2019 Feb 1.

Abstract

It has long been believed that membrane proteins present in degradative compartments such as endolysosomes or vacuoles would be destined for destruction. Now however, it appears that mechanisms and machinery exist in simple eukaryotes such as yeast and more complex organisms such as mammals that can rescue potentially "doomed" membrane proteins by retrieving them from these "late" compartments and recycling them back to the Golgi complex. In yeast, a sorting nexin dimer containing Snx4p can recognize and retrieve the Atg27p membrane protein while in mammals, the AP5 complex (with SPG11 and SPG15) directs the recycling of Golgi-localized proteins along with the cation-independent mannose 6-phosphate receptor (CIMPR). Although the respective machinery is different, there is much commonality between yeast and mammals regarding the mechanisms of retrieval and the physiological importance of these late recycling pathways.

摘要

长期以来,人们一直认为存在于降解隔间(如内溶酶体或液泡)中的膜蛋白注定要被破坏。然而,现在似乎在简单的真核生物(如酵母)和更复杂的生物体(如哺乳动物)中存在着一些机制和机器,它们可以从这些“晚期”隔间中回收潜在的“注定要失败”的膜蛋白,并将其重新循环到高尔基体复合物中。在酵母中,含有 Snx4p 的分选连接蛋白二聚体可以识别和回收 Atg27p 膜蛋白,而在哺乳动物中,AP5 复合物(与 SPG11 和 SPG15 一起)指导沿着阳离子非依赖性甘露糖 6-磷酸受体(CIMPR)对高尔基体定位蛋白进行回收。尽管各自的机制不同,但在酵母和哺乳动物之间,关于回收的机制以及这些晚期回收途径的生理重要性方面,存在着许多共同之处。

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