Receptor-mediated cellular entry of nuclear localizing anti-DNA antibodies via myosin 1
Receptor-mediated cellular entry of nuclear localizing anti-DNA antibodies via myosin 1
复制标题
DOI：
10.1172/jci119517
复制
发表时间：
1997-07-01
影响因子：
15.9
通讯作者：
Madaio, MP
中科院分区：
文献类型：
--
作者：
Yanase, K;Smith, RM;Madaio, MP
一个独特的子集的抗DNA抗体进入活细胞，与DNA酶1相互作用，并抑制核酸内切酶的活性，在他们的核定位和随后的衰减凋亡，我们现在报告，这些免疫球蛋白的内吞作用介导的细胞表面结合刷状缘肌球蛋白（肌球蛋白1）。通过这种独特的受体进入细胞和内化提供了进入和分选这些免疫球蛋白的初始接触，以易位到核孔并进入细胞核，与细胞质内的DNA酶1相互作用，或再循环回到细胞表面。这种内化途径为大蛋白质跨细胞膜的易位和细胞内抗体对细胞病理学的功能作用提供了线索。这是第一次证明刷状缘肌球蛋白作为一种特异性细胞表面受体，用于大蛋白质的内化。
A unique subset of anti-DNA antibodies enters living cells, interacts with DNase 1, and inhibits endonuclease activity, before their nuclear localization and subsequent attenuation of apoptosis, We now report that endocytosis of these immunoglobulins is mediated by cell surface binding to brush border myosin (myosin 1). Cellular entry and internalization via this unique receptor provides initial contact for entry and sorting these immunoglobulins to translocate to the nuclear pore and enter the nucleus, interact with DNase 1 within the cytoplasm, or recycle back to the cell surface. This internalization pathway provides clues to the translocation of large proteins across cell membranes and the functional effects of intracellular antibodies on cytopathology. This is the first demonstration that brush border myosin functions as a specific cell surface receptor for internalization of large proteins.