Transport and quality control of MHC class I molecules in the early secretory pathway.
Transport and quality control of MHC class I molecules in the early secretory pathway.
复制标题
DOI：
10.1016/j.coi.2015.02.009
复制
发表时间：
2015-06
影响因子：
7
通讯作者：
S. Springer
中科院分区：
文献类型：
--
作者：
S. Springer
突出显示MHC I类分子的细胞表面转运是由它们的折叠，肽结合，缺乏肽或β 2 m的I类分子可以到达ER后区室，通常被识别并返回ER。细胞质量控制可能检测部分组装的I类分子的部分解折叠和/或构象柔性。没有证据表明肽或β 2 m的优选ER输出。主要组织相容性复合体（MHC）I类分子的折叠和肽结合已经被彻底研究，但是这些生化事件与I类通过早期分泌途径的进展之间的机械联系还不太清楚。这篇综述集中在如何部分组装形式的I类（缺乏高亲和力肽和/或轻链β-2微球蛋白）保留在细胞内的问题。这些研究为研究人员提供了令人兴奋的机会，以了解I类结构，构象动力学，肽结合动力学和热力学，细胞内运输和抗原呈递之间的联系。
HighlightsCell surface transport of MHC class I molecules is determined by their folding, peptide binding, and interaction with chaperones.Class I molecules that lack peptide or β 2 m can reach post-ER compartments and are often recognized and returned to the ER.Cellular quality control probably detects the partial unfolding and/or conformational flexibility of partially assembled class I molecules.There is no evidence for preferred ER export of peptide-bound class I.Folding and peptide binding of major histocompatibility complex (MHC) class I molecules have been thoroughly researched, but the mechanistic connection between these biochemical events and the progress of class I through the early secretory pathway is much less well understood. This review focuses on the question how the partially assembled forms of class I (which lack high-affinity peptide and/or the light chain beta-2 microglobulin) are retained inside the cell. Such investigations offer researchers exciting chances to understand the connections between class I structure, conformational dynamics, peptide binding kinetics and thermodynamics, intracellular transport, and antigen presentation.