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衔接蛋白3依赖的微管介导的裂解颗粒向免疫突触的移动。

Adaptor protein 3-dependent microtubule-mediated movement of lytic granules to the immunological synapse.

作者信息

Clark Richard H, Stinchcombe Jane C, Day Anna, Blott Emma, Booth Sarah, Bossi Giovanna, Hamblin Terry, Davies E Graham, Griffiths Gillian M

机构信息

Sir William Dunn School of Pathology, South Parks Road, Oxford, OX1 3RE, UK.

出版信息

Nat Immunol. 2003 Nov;4(11):1111-20. doi: 10.1038/ni1000. Epub 2003 Oct 19.

Abstract

Hermansky-Pudlak syndrome (HPS) is a rare autosomal recessive disease characterized by platelet defects and oculocutaneous albinism. Individuals with HPS type 2 (HPS2) lack the cytosolic adaptor protein 3 (AP-3) involved in lysosomal sorting, and are also immunodeficient. Here we characterize an HPS2 mutation and demonstrate that AP-3 deficiency leads to a loss of cytotoxic T lymphocyte (CTL)-mediated cytotoxicity. Although the lysosomal protein CD63 was mislocalized to the plasma membrane, perforin and granzymes were correctly localized to the lytic granules in AP-3-deficient CTLs. However, the lytic granules of AP-3-deficient CTLs were enlarged and were unable to move along microtubules and dock within the secretory domain of the immunological synapse. These data show that AP-3 is essential for polarized secretion from CTLs.

摘要

赫尔曼斯基-普德拉克综合征(HPS)是一种罕见的常染色体隐性疾病,其特征为血小板缺陷和眼皮肤白化病。2型HPS(HPS2)患者缺乏参与溶酶体分选的胞质衔接蛋白3(AP-3),并且存在免疫缺陷。在此,我们对一种HPS2突变进行了表征,并证明AP-3缺陷导致细胞毒性T淋巴细胞(CTL)介导的细胞毒性丧失。尽管溶酶体蛋白CD63定位错误至质膜,但穿孔素和颗粒酶在AP-3缺陷的CTL中正确定位于溶细胞颗粒。然而,AP-3缺陷的CTL的溶细胞颗粒增大,并且无法沿微管移动并停靠在免疫突触的分泌区域内。这些数据表明,AP-3对于CTL的极化分泌至关重要。

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