Division of Rheumatology, Immunology and Allergy, Brigham and Women's Hospital, and Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.
Nat Cell Biol. 2011 May;13(5):559-67. doi: 10.1038/ncb2221. Epub 2011 Apr 17.
COPI (coat protein I) and the clathrin-AP-2 (adaptor protein 2) complex are well-characterized coat proteins, but a component that is common to these two coats has not been identified. The GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), ARFGAP1, is a known component of the COPI complex. Here, we show that distinct regions of ARFGAP1 interact with AP-2 and coatomer (components of the COPI complex). Selectively disrupting the interaction of ARFGAP1 with either of these two coat proteins leads to selective inhibition in the corresponding transport pathway. The role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport.
COPI（衣被蛋白 I）和网格蛋白-衔接蛋白 2（衔接蛋白 2）复合物是两种特征明确的衣被蛋白，但尚未鉴定出这两种衣被蛋白共有的成分。ADP-核糖基化因子 1（ARF1）的 GTP 酶激活蛋白（GAP）ARFGAP1 是 COPI 复合物的一个已知组成部分。在这里，我们表明 ARFGAP1 的不同区域与 AP-2 和衣被（COPI 复合物的组成部分）相互作用。选择性破坏 ARFGAP1 与这两种衣被蛋白之一的相互作用会导致相应的运输途径被选择性抑制。ARFGAP1 在 AP-2 调节的内吞作用中的作用与其在 COPI 运输中的作用具有机制上的相似性，因为其 GAP 活性和衣被功能都有助于促进 AP-2 运输。
