191 results found
    1. Cell Biology

    The membrane-associated proteins FCHo and SGIP are allosteric activators of the AP2 clathrin adaptor complex

    Gunther Hollopeter et al.
    Endocytosis is triggered by membrane-associated proteins that transform the clathrin adaptor into an active complex.
    1. Cell Biology

    NECAPs are negative regulators of the AP2 clathrin adaptor complex

    Gwendolyn M Beacham et al.
    Endocytosis is regulated by a protein family that recycles the AP2 clathrin adaptor by restoring the inactive form of complex.
    1. Structural Biology and Molecular Biophysics
    2. Microbiology and Infectious Disease

    Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1

    Xiaofei Jia et al.
    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.
    1. Structural Biology and Molecular Biophysics
    2. Cell Biology

    9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments

    Svetlana O Dodonova et al.
    A molecular model of the assembled COPI coat, determined by cryo-electron tomography of an in vitro reconstituted budding reaction, reveals details of interactions mediating coat assembly and shows the binding site of ArfGAP2.
    1. Cell Biology
    2. Neuroscience

    AP2 hemicomplexes contribute independently to synaptic vesicle endocytosis

    Mingyu Gu et al.
    A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.
    1. Cell Biology

    The AP-2 complex has a specialized clathrin-independent role in apical endocytosis and polar growth in fungi

    Olga Martzoukou et al.
    In filamentous fungi the AP-2 complex, which in mammals is an adaptor of clathrin-mediated endocytosis, is recruited to specific clathrin-independent apical endocytosis necessary for proper lipid maintenance and polar growth.
    1. Cell Biology
    2. Structural Biology and Molecular Biophysics

    A structural mechanism for phosphorylation-dependent inactivation of the AP2 complex

    Edward A Partlow et al.
    Cryo-EM reveals how a protein called NECAP inactivates the AP2 clathrin adaptor complex through concerted engagement of two domains which confer specificity for membrane-activated and phosphorylated AP2.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing

    Perunthottathu K Umasankar et al.
    The muniscin protein FCHO1 interacts with, and activates, the adapter protein-2 complex (AP-2) to promote the assembly of clathrin-coated vesicles.
    1. Biochemistry and Chemical Biology
    2. Cell Biology

    A novel GTP-binding protein–adaptor protein complex responsible for export of Vangl2 from the trans Golgi network

    Yusong Guo et al.
    The ability of epithelial cells to distinguish between domains on opposing cell surfaces within a tissue, a property known as planar cell polarity, relies on proteins and protein complexes directing the traffic of signaling proteins to specific locations on the cell surface membrane.
    1. Structural Biology and Molecular Biophysics

    How HIV-1 Nef hijacks the AP-2 clathrin adaptor to downregulate CD4

    Xuefeng Ren et al.
    The structure of the Nef:AP-2 complex has been determined and used as the basis of a model that explains how HIV-1 Nef downregulates the CD4 receptor from the surface of the infected cells.

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