Accessory proteins that control the assembly of MHC molecules with peptides
Accessory proteins that control the assembly of MHC molecules with peptides
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DOI：
10.1385/ir:23:2-3:205
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发表时间：
2001-01-01
影响因子：
4.4
通讯作者：
Van Kaer, L
中科院分区：
文献类型：
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作者：
Van Kaer, L
主要组织相容性复合体(MHC)分子与多肽的稳定组装受多种辅因子的控制，包括具有一般内务功能的蛋白质和MHC组装中具有特定功能的蛋白质。我实验室最近的工作主要集中在两个伴侣蛋白，TPN和DM，它们分别在将多肽装载到MHC I类和MHC II类分子中发挥关键作用。Tapasin是一种跨膜蛋白，它将内质网中的I类空分子连接到与抗原处理相关的转运蛋白上。DM是一种肽交换因子，它与内体和溶酶体隔室中的空的和载肽的II类分子结合。尽管已经提出了Tapasin和DM的许多不同的功能，但越来越多的证据表明，这两种伴侣蛋白都保留了不稳定的MHC分子，直到它们与高亲和力的多肽结合。因此，这些辅因子促进了长寿命MHC-肽复合体的表面表达。
The stable assembly of Major Histocompatibility Complex (MHC) molecules with peptides is controlled by a number of cofactors, including proteins with general housekeeping functions and proteins with dedicated functions in MHC assembly. Recent work in my laboratory has focused on two chaperones, tapasin (tpn) and DM, that play critical roles in the loading of peptides onto MHC class I and MHC class II molecules, respectively. Tapasin is a transmembrane protein that tethers empty class I molecules in the endoplasmic reticulum to the transporter associated with antigen processing. DM is a peptide exchange factor that binds with empty and peptide-loaded class II molecules in endosomal and lysosomal compartments. Although a number of different functions for tapasin and DM have been proposed, emerging evidence suggests that both of these chaperones retain unstable MHC molecules in peptide-loading compartments: until they bind with high-affinity peptides. These cofactors therefore promote the surface expression of long-lived MHC-peptide complexes.