小鼠TAP1/TAP2转运体的肽段长度和序列特异性
Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator.
作者信息
Schumacher T N, Kantesaria D V, Heemels M T, Ashton-Rickardt P G, Shepherd J C, Fruh K, Yang Y, Peterson P A, Tonegawa S, Ploegh H L
机构信息
Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.
出版信息
J Exp Med. 1994 Feb 1;179(2):533-40. doi: 10.1084/jem.179.2.533.
Abstract
The transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticulum in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. We show that the mouse TAP translocator (H-2b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino acid. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably well with the specificity of the TAP translocator. In addition to transport in the lumenal direction, efflux of peptide in the cytosolic direction is observed in an ATP- and temperature-dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this efflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides.
摘要
抗原加工相关转运体（TAP）以三磷酸腺苷（ATP）依赖的方式将肽转运至内质网腔，以供主要组织相容性复合体I类分子呈递。我们发现，小鼠TAP转运体（H-2b单倍型）基于至少九个残基的最小长度以及COOH末端疏水氨基酸的存在来选择肽。因此，能够与小鼠I类分子结合的肽中COOH末端疏水氨基酸占优势，这与TAP转运体的特异性非常契合。除了向腔室方向转运外，还观察到肽以ATP和温度依赖的方式向胞质方向流出。通过在I类组装位点维持低肽浓度，这种流出机制可确保I类分子优先加载高亲和力肽。
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