拉布
GTP酶
抗原呈递
细胞生物学
交叉展示
内体
MHC I级
抗原处理
抗原
生物
小泡
细胞内
化学
主要组织相容性复合体
生物化学
膜
免疫系统
T细胞
免疫学
作者
Liyun Zou,Jingran Zhou,Yukui Zhang,Jing Wang,Na Liu,Linlin Chai,Na Li,Ting Liu,Liqi Li,Zhunyi Xie,Hongli Liu,Ying Wan,Yuzhang Wu
标识
DOI:10.1073/pnas.0905684106
摘要
Antigen cross-presentation in dendritic cells is a complex intracellular membrane transport process, but the underlying molecular mechanisms remain to be thoroughly investigated. In this study, we examined the effect of siRNA-mediated knockdown of 57 Rab GTPases, the key regulators of membrane trafficking, on antigen cross-presentation. Twelve Rab GTPases were identified to be associated with antigen cross-presentation, and Rab3b/3c was indicated to be colocalized with MHC class I molecules at perinuclear tubular structure. Tracing with fluorescence protein-tagged beta(2)-microglobulin demonstrated that the MHC class I molecules were internalized from the plasma membrane to Rab3b/3c-positive compartments, which were also colocalized with the internalized transferrin. Moreover, depletion of Rab3b/3c strongly reduced the fast phase recycling rate of transferrin receptors. Furthermore, the Rab3b/3c-positive compartments were colocalized with a fraction of Rab27a at a juxtaposition of phagosomes. Together, these data demonstrate that Rab3b/3c-positive recycling vesicles are involved in and may constitute one of the recycling compartments in exogenous antigen cross-presentation.
科研通智能强力驱动
Strongly Powered by AbleSci AI