2014年4月29日 · We report the crystal structure of a protein complex containing Vpu and BST2 cytoplasmic domains and the core of the clathrin adaptor protein complex 1 (AP1). This, together with our biochemical and functional validations, reveals how Vpu hijacks the AP1-dependent membrane trafficking pathways to mistraffick BST2.

2019年7月17日 · Heterotetrameric clathrin adaptor protein complexes (APs) orchestrate the formation of coated vesicles for transport among organelles of the cell periphery. AP1 binds membranes enriched for phosphatidylinositol 4-phosphate, such as the trans Golgi network, while AP2 associates with phosphatidylinositol 4,5-bisphosphate of the plasma membrane.

2014年4月29日 · HIV-1 viral protein u (Vpu) can stimulate novel versions of canonical interactions with the clathrin adaptor AP1 to counteract the host antiviral protein BST2.

2015年4月1日 · HIV-1 Vpu hijacks clathrin AP1 for the mistrafficking of BST2/tetherin. Antiviral restriction factors are an integral part of the host innate immune system that protects cells from viral pathogens, such as human immunodeficiency virus (HIV).

We report the crystal structure of a protein complex containing Vpu and BST2 cytoplasmic domains and the core of the clathrin adaptor protein complex 1 (AP1). This, together with our biochemical and functional validations, reveals how Vpu hijacks the AP1-dependent membrane trafficking pathways to mistraffick BST2.

2014年3月25日 · We report the crystal structure of a protein complex containing Vpu and BST2 cytoplasmic domains and the core of the clathrin adaptor protein complex 1 (AP1). This, together with our biochemical and functional validations, reveals how Vpu hijacks the AP1-dependent membrane trafficking pathways to mistraffick BST2.

2008年6月12日 · Here, we review how the Vif and Vpu (and probably Vpr) proteins each suppress the antiviral activity of specific restriction factors, whereas the multifunctional Nef protein contributes, inter alia, to partial evasion from adaptive, cell-mediated immunity.

We report the crystal structure of a protein complex containing Vpu and BST2 cytoplasmic domains and the core of the clathrin adaptor protein complex 1 (AP1). This, together with our biochemical and functional validations, reveals how Vpu hijacks the AP1-dependent membrane trafficking pathways to mistraffick BST2.

Heterotetrameric clathrin Adaptor Protein complexes (APs) orchestrate the formation of coated vesicles for transport among organelles of the cell periphery. AP1 binds membranes enriched for PI4P, such as the TGN, while AP2 associates with PIP2 of ...

2021年7月30日 · 80 et. Al., 2015, suggested that Vpu interacts with AP1/AP2 Catherin adapters to facilitate the 81 endosomal degradation of BST-2/Tetherin in a manner that is also dependent on the S52/56 82 phosphoserines. 83 In addition to its well characterized role in targeting cellular proteins, Vpu has been