@article{Tobys2021-01Inhib-52302,
  year={2021},
  doi={10.1111/tra.12770},
  title={Inhibition of clathrin-mediated endocytosis by knockdown of AP-2 leads to alterations in the plasma membrane proteome},
  number={1-2},
  volume={22},
  issn={1398-9219},
  journal={Traffic},
  pages={6--22},
  author={Tobys, David and Kowalski, Lisa Maria and Cziudaj, Eva and Müller, Stefan and Zentis, Peter and Pach, Elke and Zigrino, Paola and Bläske, Tobias and Höning, Stefan}
}

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    <dc:creator>Tobys, David</dc:creator>
    <dc:contributor>Zigrino, Paola</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivatives 4.0 International</dc:rights>
    <dc:contributor>Bläske, Tobias</dc:contributor>
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    <dc:creator>Pach, Elke</dc:creator>
    <dc:creator>Kowalski, Lisa Maria</dc:creator>
    <dc:contributor>Höning, Stefan</dc:contributor>
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    <dc:contributor>Pach, Elke</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-01-07T10:26:19Z</dc:date>
    <dc:language>eng</dc:language>
    <dc:creator>Müller, Stefan</dc:creator>
    <dc:contributor>Müller, Stefan</dc:contributor>
    <dc:creator>Zentis, Peter</dc:creator>
    <dc:creator>Zigrino, Paola</dc:creator>
    <dcterms:issued>2021-01</dcterms:issued>
    <dcterms:abstract xml:lang="eng">In eukaryotic cells, clathrin-mediated endocytosis (CME) is a central pathway for the internalization of proteins from the cell surface, thereby contributing to the maintenance of the plasma membrane protein composition. A key component for the formation of endocytic clathrin-coated vesicles (CCVs) is AP-2, as it sequesters cargo membrane proteins, recruits a multitude of other endocytic factors and initiates clathrin polymerization. Here, we inhibited CME by depletion of AP-2 and explored the consequences for the plasma membrane proteome. Quantitative analysis revealed accumulation of major constituents of the endosomal-lysosomal system reflecting a block in retrieval by compensatory CME. The noticeable enrichment of integrins and blockage of their turnover resulted in severely impaired cell migration. Rare proteins such as the anti-cancer drug target CA9 and tumor markers (CD73, CD164, CD302) were significantly enriched. The AP-2 knockdown attenuated the global endocytic capacity, but clathrin-independent entry pathways were still operating, as indicated by persistent internalization of specific membrane-spanning and GPI-anchored receptors (PVR, IGF1R, CD55, TNAP). We hypothesize that blocking AP-2 function and thus inhibiting CME may be a novel approach to identify new druggable targets, or to increase their residence time at the plasma membrane, thereby increasing the probability for efficient therapeutic intervention.</dcterms:abstract>
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    <dc:creator>Cziudaj, Eva</dc:creator>
    <dc:contributor>Kowalski, Lisa Maria</dc:contributor>
    <dc:contributor>Cziudaj, Eva</dc:contributor>
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    <dc:creator>Höning, Stefan</dc:creator>
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