在衣被蛋白复合体γ亚基内存在一个用于双赖氨酸回收基序和p23的单一结合位点。
A single binding site for dilysine retrieval motifs and p23 within the gamma subunit of coatomer.
作者信息
Harter C, Wieland F T
机构信息
Biochemie-Zentrum Heidelberg, Ruprecht-Karls-Universität, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
出版信息
Proc Natl Acad Sci U S A. 1998 Sep 29;95(20):11649-54. doi: 10.1073/pnas.95.20.11649.
Abstract
Coatomer, the major component of the coat of COPI transport vesicles, binds both to the dilysine motif of resident membrane proteins of the endoplasmic reticulum and to the cytoplasmic domain of p23, a major type I membrane protein of COPI vesicles. Using a photocrosslinking approach, we find that under native conditions a peptide analogous to the cytoplasmic domain of p23 interacts with coatomer exclusively through its gamma subunit and shares its binding site with a KKXX retrieval motif. However, upon dissociation of coatomer, interaction with various subunits, including an alpha-, beta'-, epsilon-COP subcomplex, of the photoreactive peptide is observed. We suggest that, under physiological conditions, interaction of coatomer with both endoplasmic reticulum retrieval motifs and the cytoplasmic domain of p23 is mediated by gamma-COP.
摘要
外套蛋白是 COPI 转运囊泡衣被的主要成分，它既能与内质网驻留膜蛋白的双赖氨酸基序结合，也能与 COPI 囊泡的主要 I 型膜蛋白 p23 的胞质结构域结合。通过光交联方法，我们发现在天然条件下，一个类似于 p23 胞质结构域的肽仅通过其γ亚基与外套蛋白相互作用，并与 KKXX 回收基序共享其结合位点。然而，在外套蛋白解离后，可观察到光反应性肽与包括α-、β'-、ε-COP 亚复合体在内的各种亚基相互作用。我们认为，在生理条件下，外套蛋白与内质网回收基序和 p23 胞质结构域的相互作用是由γ-COP 介导的。
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