4.3 Article

Specificity of amyloid precursor-like protein 2 interactions with MHC class I molecules

期刊

IMMUNOGENETICS
卷 60, 期 6, 页码 303-313

出版社

SPRINGER
DOI: 10.1007/s00251-008-0296-0

关键词

amyloid precursor-like protein 2; antigen presentation; beta 2-microglobulin; major histocompatibility complex class I; mouse

资金

  1. NCRR NIH HHS [P20 RR018759] Funding Source: Medline
  2. NIGMS NIH HHS [R01 GM074876-03, GM74876, R01 GM057428, R01 GM057428-09, GM57428, R01 GM074876] Funding Source: Medline
  3. NATIONAL CENTER FOR RESEARCH RESOURCES [P20RR018759] Funding Source: NIH RePORTER
  4. NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM057428, R01GM074876] Funding Source: NIH RePORTER

向作者/读者索取更多资源

The ubiquitously expressed amyloid precursor-like protein 2 (APLP2) has been previously found to regulate cell surface expression of the major histocompatibility complex (MHC) class I molecule K-d and bind strongly to Kd. In the study reported here, we demonstrated that APLP2 binds, in varied degrees, to several other mouse MHC class I allotypes and that the ability of APLP2 to affect cell surface expression of an MHC class I molecule is not limited to K-d. L-d, like K-d, was found associated with APLP2 in the Golgi, but Kd was also associated with APLP2 within intracellular vesicular structures. We also investigated the effect of beta(2)m on APLP2/MHC interaction and found that human beta(2)m transfection increased the association of APLP2 with mouse MHC class I molecules, likely by affecting H2 class I heavy chain conformation. APLP2 was demonstrated to bind specifically to the conformation of Ld having folded outer domains, consistent with our previous results with Kd and indicating APLP2 interacts with the alpha 1 alpha 2 region on each of these H2 class I molecules. Furthermore, we observed that binding to APLP2 involved the MHC alpha 3/transmembrane/cytoplasmic region, suggesting that conserved as well as polymorphic regions of the H2 class I molecule may participate in interaction with APLP2. In summary, we demonstrated that APLP2's binding, co-localization pattern, and functional impact vary among H2 class I molecules and that APLP2/MHC association is influenced by multiple domains of the MHC class I heavy chain and by beta(2)m's effects on the conformation of the heavy chain.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.3
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据