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ARFGAP1 promotes AP-2-dependent endocytosis
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
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2011 (English)In: Nature Cell Biology, ISSN 1465-7392, E-ISSN 1476-4679, Vol. 13, no 5, 559-U144 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2011. Vol. 13, no 5, 559-U144 p.
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Biological Sciences
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URN: urn:nbn:se:su:diva-68140DOI: 10.1038/ncb2221ISI: 000290148700015OAI: oai:DiVA.org:su-68140DiVA: diva2:471915
Note
authorCount :14Available from: 2012-01-03 Created: 2012-01-03 Last updated: 2017-12-08Bibliographically approved

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