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Anitei, M.* ; Stange, C.* ; Czupalla, C.* ; Niehage, C.* ; Schuhmann, K.* ; Sala, P. ; Czogalla, A. ; Pursche, T.* ; Coskun, Ü. ; Shevchenko, A.* ; Hoflack, B.*

Spatiotemporal control of lipid conversion, actin-based mechanical forces, and curvature sensors during clathrin/AP-1-coated vesicle biogenesis.

Cell Rep. 20, 2087-2099 (2017)
Verlagsversion Forschungsdaten DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
Clathrin/adaptor protein-1-coated carriers connect the secretory and the endocytic pathways. Carrier biogenesis relies on distinct protein networks changing membrane shape at the trans-Golgi network, each regulating coat assembly, F-actin-based mechanical forces, or the biophysical properties of lipid bilayers. How these different hubs are spatiotemporally coordinated remains largely unknown. Using in vitro reconstitution systems, quantitative proteomics, and lipidomics, as well as in vivo cell-based assays, we characterize the protein networks controlling membrane lipid composition, membrane shape, and carrier scission. These include PIP5K1A and phospholipase C-beta 3 controlling the conversion of PI[4]P into diacylglycerol. PIP5K1A binding to RAC1 provides a link to F-actin-based mechanical forces needed to tubulate membranes. Tubular membranes then recruit the BAR-domain-containing arfaptin-1/2 guiding carrier scission. These findings provide a framework for synchronizing the chemical/biophysical properties of lipid bilayers, F-actin-based mechanical forces, and the activity of proteins sensing membrane shape during clathrin/adaptor protein-1-coated carrier biogenesis.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Ap-1 ; Pi[4,5]p2 ; Arfaptin ; Clathrin ; Diacylglycerol ; Mannose-6-phosphate Receptor ; Trans-golgi Network ; Transport Carrier; Trans-golgi Network; Mannose 6-phosphate Receptor; Adp-ribosylation Factor; Protein-kinase-c; Plasma-membrane; Phospholipase-d; Living Cells; Arfaptin 1; Trafficking; Scission
ISSN (print) / ISBN 2211-1247
e-ISSN 2211-1247
Zeitschrift Cell Reports
Quellenangaben Band: 20, Heft: 9, Seiten: 2087-2099 Artikelnummer: , Supplement: ,
Verlag Cell Press
Verlagsort Cambridge
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Pancreatic Islet Research (IPI)