TY  - JOUR
A1  - Dejonghe, Wim
A1  - Kuenen, Sabine
A1  - Mylle, Evelien
A1  - Vasileva, Mina
A1  - Keech, Olivier
A1  - Viotti, Corrado
A1  - Swerts, Jef
A1  - Fendrych, Matyas
A1  - Ortiz-Morea, Fausto Andres
A1  - Mishev, Kiril
A1  - Delang, Simon
A1  - Scholl, Stefan
A1  - Zarza, Xavier
A1  - Heilmann, Mareike
A1  - Kourelis, Jiorgos
A1  - Kasprowicz, Jaroslaw
A1  - Nguyen, Le Son Long
A1  - Drozdzecki, Andrzej
A1  - Van Houtte, Isabelle
A1  - Szatmari, Anna-Maria
A1  - Majda, Mateusz
A1  - Baisa, Gary
A1  - Bednarek, Sebastian York
A1  - Robert, Stephanie
A1  - Audenaert, Dominique
A1  - Testerink, Christa
A1  - Munnik, Teun
A1  - Van Damme, Daniel
A1  - Heilmann, Ingo
A1  - Schumacher, Karin
A1  - Winne, Johan
A1  - Friml, Jiri
A1  - Verstreken, Patrik
A1  - Russinova, Eugenia
T1  - Mitochondrial uncouplers inhibit clathrin-mediated endocytosis largely through cytoplasmic acidification
JF  - Nature Communications
N2  - ATP production requires the establishment of an electrochemical proton gradient across the inner mitochondrial membrane. Mitochondrial uncouplers dissipate this proton gradient and disrupt numerous cellular processes, including vesicular trafficking, mainly through energy depletion. Here we show that Endosidin9 (ES9), a novel mitochondrial uncoupler, is a potent inhibitor of clathrin-mediated endocytosis (CME) in different systems and that ES9 induces inhibition of CME not because of its effect on cellular ATP, but rather due to its protonophore activity that leads to cytoplasm acidification. We show that the known tyrosine kinase inhibitor tyrphostinA23, which is routinely used to block CME, displays similar properties, thus questioning its use as a specific inhibitor of cargo recognition by the AP-2 adaptor complex via tyrosine motif-based endocytosis signals. Furthermore, we show that cytoplasm acidification dramatically affects the dynamics and recruitment of clathrin and associated adaptors, and leads to reduction of phosphatidylinositol 4,5-biphosphate from the plasma membrane.
Y1  - 2016
U6  - https://doi.org/10.1038/ncomms11710
SN  - 2041-1723
VL  - 7
SP  - 1959
EP  - 1968
PB  - Nature Publ. Group
CY  - London
ER  - 
TY  - JOUR
A1  - Frescatada-Rosa, Marcia
A1  - Stanislas, Thomas
A1  - Backues, Steven K.
A1  - Reichardt, Ilka
A1  - Men, Shuzhen
A1  - Boutte, Yohann
A1  - Juergens, Gerd
A1  - Moritz, Thomas
A1  - Bednarek, Sebastian York
A1  - Grebe, Markus
T1  - High lipid order of Arabidopsis cell-plate membranes mediated by sterol and Dynamin-Related Protein 1A function
JF  - The plant journal
N2  - Membranes of eukaryotic cells contain high lipid-order sterol-rich domains that are thought to mediate temporal and spatial organization of cellular processes. Sterols are crucial for execution of cytokinesis, the last stage of cell division, in diverse eukaryotes. The cell plate of higher-plant cells is the membrane structure that separates daughter cells during somatic cytokinesis. Cell-plate formation in Arabidopsis relies on sterol- and DYNAMIN-RELATED PROTEIN1A (DRP1A)-dependent endocytosis. However, functional relationships between lipid membrane order or lipid packing and endocytic machinery components during eukaryotic cytokinesis have not been elucidated. Using ratiometric live imaging of lipid order-sensitive fluorescent probes, we show that the cell plate of Arabidopsis thaliana represents a dynamic, high lipid-order membrane domain. The cell-plate lipid order was found to be sensitive to pharmacological and genetic alterations of sterol composition. Sterols co-localize with DRP1A at the cell plate, and DRP1A accumulates in detergent-resistant membrane fractions. Modifications of sterol concentration or composition reduce cell-plate membrane order and affect DRP1A localization. Strikingly, DRP1A function itself is essential for high lipid order at the cell plate. Our findings provide evidence that the cell plate represents a high lipid-order domain, and pave the way to explore potential feedback between lipid order and function of dynamin-related proteins during cytokinesis.
KW  - membrane order
KW  - sterol
KW  - cytokinesis
KW  - DRP1A
KW  - Arabidopsis
Y1  - 2014
U6  - https://doi.org/10.1111/tpj.12674
SN  - 0960-7412
SN  - 1365-313X
VL  - 80
IS  - 5
SP  - 745
EP  - 757
PB  - Wiley-Blackwell
CY  - Hoboken
ER  -