Carpentier J L, Paccaud J P, Gorden P, Rutter W J, Orci L
Department of Morphology, University of Geneva Medical Center, Switzerland.
Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):162-6. doi: 10.1073/pnas.89.1.162.
The role of insulin-induced receptor autophosphorylation in its internalization was analyzed by comparing 125I-labeled insulin (125I-insulin) internalization in Chinese hamster ovary (CHO) cell lines transfected with normal (CHO.T) or mutated insulin receptors. In four cell lines with a defect of insulin-induced autophosphorylation, 125I-insulin internalization was impaired. By contrast, in CHO.T cells and in two other CHO cell lines with amino acid deletions or insertions that do not perturb autophosphorylation, 125I-insulin internalization was not affected. A morphological analysis showed that the inhibition is linked to the ligand-specific surface redistribution in which the insulin-receptor complexes leave microvilli and concentrate on nonvillous segments of the membrane where endocytosis occurs.
通过比较用正常（CHO.T）或突变胰岛素受体转染的中国仓鼠卵巢（CHO）细胞系中125I标记胰岛素（125I-胰岛素）的内化情况，分析了胰岛素诱导的受体内磷酸化在其内化过程中的作用。在四个存在胰岛素诱导的自磷酸化缺陷的细胞系中，125I-胰岛素的内化受损。相比之下，在CHO.T细胞以及另外两个具有不干扰自磷酸化的氨基酸缺失或插入的CHO细胞系中，125I-胰岛素的内化未受影响。形态学分析表明，这种抑制与配体特异性的表面重新分布有关，其中胰岛素-受体复合物离开微绒毛并聚集在内吞作用发生的膜的非绒毛部分。
