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Temporal Ordering in Endocytic Clathrin-Coated Vesicle Formation via AP2 Phosphorylation
AG. Wrobel, Z. Kadlecova, J. Kamenicky, JC. Yang, T. Herrmann, BT. Kelly, AJ. McCoy, PR. Evans, S. Martin, S. Müller, S. Salomon, F. Sroubek, D. Neuhaus, S. Höning, DJ. Owen,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
Grant support
Wellcome Trust - United Kingdom
MC_U105178845
Medical Research Council - United Kingdom
MC_U105178934
Medical Research Council - United Kingdom
090909/Z/09/Z
Wellcome Trust - United Kingdom
097040/Z/11/Z
Wellcome Trust - United Kingdom
NLK
Cell Press Free Archives
from 2001-07-01 to 1 year ago
Free Medical Journals
from 2001 to 1 year ago
Elsevier Open Access Journals
from 2001-07-01 to 2023-06-19
Elsevier Open Archive Journals
from 2001-07-01 to 1 year ago
- MeSH
- Adaptor Protein Complex alpha Subunits genetics MeSH
- Adaptor Protein Complex 2 genetics metabolism MeSH
- Endocytosis genetics MeSH
- Phosphorylation genetics MeSH
- Clathrin genetics metabolism MeSH
- Clathrin-Coated Vesicles genetics metabolism MeSH
- Humans MeSH
- Coated Pits, Cell-Membrane genetics metabolism MeSH
- Sorting Nexins genetics MeSH
- Protein Binding genetics MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Clathrin-mediated endocytosis (CME) is key to maintaining the transmembrane protein composition of cells' limiting membranes. During mammalian CME, a reversible phosphorylation event occurs on Thr156 of the μ2 subunit of the main endocytic clathrin adaptor, AP2. We show that this phosphorylation event starts during clathrin-coated pit (CCP) initiation and increases throughout CCP lifetime. μ2Thr156 phosphorylation favors a new, cargo-bound conformation of AP2 and simultaneously creates a binding platform for the endocytic NECAP proteins but without significantly altering AP2's cargo affinity in vitro. We describe the structural bases of both. NECAP arrival at CCPs parallels that of clathrin and increases with μ2Thr156 phosphorylation. In turn, NECAP recruits drivers of late stages of CCP formation, including SNX9, via a site distinct from where NECAP binds AP2. Disruption of the different modules of this phosphorylation-based temporal regulatory system results in CCP maturation being delayed and/or stalled, hence impairing global rates of CME.
Center for Molecular Medicine University of Cologne Robert Koch Straße 21 50931 Cologne Germany
CIMR WT MRC Building Hills Road Cambridge CB2 0QQ UK
The Francis Crick Institute 1 Midland Road London NW1 1ST UK
University of Grenoble Alpes CNRS CEA IBS 38000 Grenoble France
References provided by Crossref.org
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