The permeability of the cell-to-cell membrane channel and its regulation in mammalian cell junctions

In Vitro ◽  
1980 ◽  
Vol 16 (12) ◽  
pp. 1043-1048 ◽  
Author(s):  
Jean L. Flagg-Newton
Keyword(s):  
Cell Membrane ◽  
Mammalian Cell ◽  
Cell Junctions ◽  
Membrane Channel

Affordable Membrane Permeability Calculations: Permeation of Short-Chain Alcohols through Pure-Lipid Bilayers and a Mammalian Cell Membrane

2019 ◽  
Vol 15 (5) ◽  
pp. 2913-2924 ◽  
Author(s):  
Chi Hang Tse ◽  
Jeffrey Comer ◽  
Simon Kit Sang Chu ◽  
Yi Wang ◽  
Christophe Chipot
Keyword(s):  
Cell Membrane ◽  
Membrane Permeability ◽  
Lipid Bilayers ◽  
Mammalian Cell ◽  
Short Chain

scholarly journals Control by Calcium of mammalian cell membrane electropermeabilization

2009 ◽  
Vol 96 (3) ◽  
pp. 361a
Author(s):  
Muriel Golzio ◽  
Florin Ciobanu ◽  
Eugenia Kovacs ◽  
Justin Teissie
Keyword(s):  
Cell Membrane ◽  
Mammalian Cell

Pathogenesis of Shigella Diarrhea: XVII. A Mammalian Cell Membrane Glycolipid, Gb3, Is Required but Not Sufficient to Confer Sensitivity to Shiga Toxin

1994 ◽  
Vol 169 (3) ◽  
pp. 538-546 ◽  
Author(s):  
M. S. Jacewicz ◽  
M. Mobassaleh ◽  
S. K. Gross ◽  
K. A. Balasubramanian ◽  
P. F. Daniel ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Mammalian Cell ◽  
Shiga Toxin

scholarly journals α-catenin switches between a slip and a cooperative catch bond with F-actin to regulate cell junction fluidity

2020 ◽  
Author(s):  
C. Arbore ◽  
M Sergides ◽  
L. Gardini ◽  
F.S. Pavone ◽  
M. Capitanio
Keyword(s):  
Cell Membrane ◽  
Actin Cytoskeleton ◽  
Protein Unfolding ◽  
Solid Phase ◽  
Cell Junctions ◽  
Cell Junction ◽  
Laser Tweezers ◽  
Catch Bond ◽  
Membrane Cytoskeleton ◽  
Solid Phase Transition

α-catenin is a crucial protein at cell junctions that provides connection between the actin cytoskeleton and the cell membrane. At adherens junctions (AJs), α-catenin forms heterodimers with β-catenin that are believed to resist force on F-actin. Outside AJs, α-catenin forms homodimers that directly connect the cell membrane to the actin cytoskeleton, but their mechanosensitive properties are inherently unknown. Surprisingly, by using ultra-fast laser tweezers we found that a single α-β-catenin heterodimer does not resist force but instead slips along F-actin in the direction of force. Conversely, the action of 5 to 10 α-β-catenin heterodimers together with unidirectional force applied to F-actin engaged a molecular switch in α-catenin, which unfolded and strongly bound F-actin as a cooperative catch bond. Similarly, an α-catenin homodimer formed an asymmetric catch bond with F-actin triggered by protein unfolding under force. Our data reveal that α-catenin clustering together with intracellular tension engage a fluid-to-solid phase transition at the membrane-cytoskeleton interface.

Engineering of mammalian cell membrane proteins

2012 ◽  
Vol 1 (4) ◽  
pp. 411-417 ◽  
Author(s):  
Masahiro Kawahara ◽  
Teruyuki Nagamune
Keyword(s):  
Membrane Proteins ◽  
Cell Membrane ◽  
Mammalian Cell ◽  
Cell Membrane Proteins
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