Heidemann, J, Kölbel, K, Konijnenberg, A et al. (5 more authors) (2020) Further insights from structural mass spectrometry into endocytosis adaptor protein assemblies. International Journal of Mass Spectrometry, 447. 116240. ISSN 1387-3806
Abstract
As a fundament in many biologically relevant processes, endocytosis in its different guises has been arousing interest for decades and still does so. This is true for the actual transport and its initiation alike. In clathrin-mediated endocytosis, a comparatively well understood endocytic pathway, a set of adaptor proteins bind specific lipids in the plasma membrane, subsequently assemble and thus form a crucial bridge from clathrin to actin for the ongoing process. These adaptor proteins are highly interesting themselves and the subject of this manuscript. Using many of the instruments that are available now in the mass spectrometry toolbox, we added some facets to the picture of how these minimal assemblies may look, how they form, and what influences the structure. Especially, lipids in the adaptor protein complexes result in reduced charging of a normal sized complex due to their specific binding position. The results further support our structural model of a double ring structure with interfacial lipids.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2019 The Authors. Published by Elsevier B.V. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
Keywords: | ANTH/Sla2; Epsin; ENTH; Native mass spectrometry; Ion mobility; Surface induced dissociation |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 14 Nov 2019 10:28 |
Last Modified: | 14 Nov 2019 10:28 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.ijms.2019.116240 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:153403 |