Rechsteiner M, Realini C, Ustrell V
Department of Biochemistry, University of Utah School of Medicine, 50 North Medical Drive, Salt Lake City, UT 84132, USA.
Biochem J. 2000 Jan 1;345 Pt 1(Pt 1):1-15.
There are two immune responses in vertebrates: humoral immunity is mediated by circulating antibodies, whereas cytotoxic T lymphocytes (CTL) confer cellular immunity. CTL lyse infected cells upon recognition of cell-surface MHC Class I molecules complexed with foreign peptides. The displayed peptides are produced in the cytosol by degradation of host proteins or proteins from intracellular pathogens that might be present. Proteasomes are cylindrical multisubunit proteases that generate many of the peptides eventually transferred to the cell surface for immune surveillance. In mammalian proteasomes, six active sites face a central chamber. As this chamber is sealed off from the enzyme's surface, there must be mechanisms to promote entry of substrates. Two protein complexes have been found to bind the ends of the proteasome and activate it. One of the activators is the 19 S regulatory complex of the 26 S proteasome; the other activator is '11 S REG' [Dubiel, Pratt, Ferrell and Rechsteiner (1992) J. Biol. Chem. 267, 22369-22377] or 'PA28' [Ma, Slaughter and DeMartino (1992) J. Biol. Chem. 267, 10515-10523]. During the past 7 years, our understanding of the structure of REG molecules has increased significantly, but much less is known about their biological functions. There are three REG subunits, namely alpha, beta and gamma. Recombinant REGalpha forms a ring-shaped heptamer of known crystal structure. 11 S REG is a heteroheptamer of alpha and beta subunits. REGgamma is also presumably a heptameric ring, and it is found in the nuclei of the nematode work Caenorhabditis elegans and higher organisms, where it may couple proteasomes to other nuclear components. REGalpha and REGbeta, which are abundant in vertebrate immune tissues, are located mostly in the cytoplasm. Synthesis of REG alpha and beta subunits is induced by interferon-gamma, and this has led to the prevalent hypothesis that REG alpha/beta hetero-oligomers play an important role in Class I antigen presentation. In the present review we focus on the structural properties of REG molecules and on the evidence that REGalpha/beta functions in the Class I immune response.
体液免疫由循环抗体介导,而细胞毒性T淋巴细胞(CTL)赋予细胞免疫。CTL在识别与外来肽复合的细胞表面I类主要组织相容性复合体(MHC)分子后裂解被感染的细胞。所展示的肽是通过宿主蛋白或可能存在的细胞内病原体的蛋白在细胞质中降解产生的。蛋白酶体是圆柱形的多亚基蛋白酶,可产生许多最终转移到细胞表面进行免疫监视的肽。在哺乳动物蛋白酶体中,六个活性位点面向中央腔室。由于该腔室与酶的表面隔绝,因此必须有促进底物进入的机制。已发现两种蛋白质复合物结合蛋白酶体的末端并激活它。其中一种激活剂是26S蛋白酶体的19S调节复合物;另一种激活剂是“11S REG”[杜比埃尔、普拉特、费雷尔和雷施泰纳(1992年)《生物化学杂志》267,22369 - 22377]或“PA28”[马、斯劳特和德马蒂诺(1992年)《生物化学杂志》267,10515 - 10523]。在过去的7年里,我们对REG分子结构的理解有了显著增加,但对其生物学功能的了解却少得多。有三个REG亚基,即α、β和γ。重组REGα形成具有已知晶体结构的环形七聚体。11S REG是α和β亚基的异源七聚体。REGγ大概也是一个七聚体环,它存在于线虫秀丽隐杆线虫和高等生物的细胞核中,在那里它可能将蛋白酶体与其他核成分偶联起来。REGα和REGβ在脊椎动物免疫组织中含量丰富,主要位于细胞质中。REGα和β亚基的合成由γ干扰素诱导,这导致了一个普遍的假设,即REGα/β异源寡聚体在I类抗原呈递中起重要作用。在本综述中,我们重点关注REG分子的结构特性以及REGα/β在I类免疫反应中发挥作用的证据。