Structural insights into the aPKC regulatory switch mechanism of the human cell polarity protein lethal giant larvae 2 [electronic resource]

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Tác giả:

Ngôn ngữ: eng

Ký hiệu phân loại: 570.1 Philosophy and theory

Thông tin xuất bản: Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy, 2019

Mô tả vật lý: Size: p. 10804-10812 : , digital, PDF file.

Bộ sưu tập: Metadata

ID: 260017

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 Metazoan cell polarity is controlled by a set of highly conserved proteins. Lethal giant larvae (Lgl) functions in apical-basal polarity through phosphorylation-dependent interactions with several other proteins as well as the plasma membrane. Phosphorylation of Lgl by atypical protein kinase C (aPKC), a component of the partitioning-defective (Par) complex in epithelial cells, excludes Lgl from the apical membrane, a crucial step in the establishment of epithelial cell polarity. We present the crystal structures of human Lgl2 in both its unphosphorylated and aPKC-phosphorylated states. Lgl2 adopts a double ?-propeller structure that is unchanged by aPKC phosphorylation of an unstructured loop in its second ?-propeller, ruling out models of phosphorylation-dependent conformational change. Here, we demonstrate that phosphorylation controls the direct binding of purified Lgl2 to negative phospholipids in vitro. We also show that a coil?helix transition of this region that is promoted by phosphatidylinositol 4,5-bisphosphate (PIP<
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