Further insights from structural mass spectrometry into endocytosis adaptor protein assemblies.
ANTH/Sla2
ENTH
Epsin
Ion mobility
Native mass spectrometry
Surface induced dissociation
Journal
International journal of mass spectrometry
ISSN: 1387-3806
Titre abrégé: Int J Mass Spectrom
Pays: Netherlands
ID NLM: 101137096
Informations de publication
Date de publication:
Jan 2020
Jan 2020
Historique:
entrez:
27
11
2020
pubmed:
28
11
2020
medline:
28
11
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 33244295
doi: 10.1016/j.ijms.2019.116240
pmc: PMC7116418
mid: EMS103420
doi:
Types de publication
Journal Article
Langues
eng
Pagination
116240Subventions
Organisme : European Research Council
ID : 759661
Pays : International
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