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Molecular interactions between vinculin and phospholipids
Author(s) -
Goldmann Wolfgang H.
Publication year - 2018
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.10978
Subject(s) - vinculin , membrane , chemistry , biophysics , protonation , domain (mathematical analysis) , lipid bilayer , biochemistry , focal adhesion , biology , organic chemistry , signal transduction , mathematics , ion , mathematical analysis
Abstract The focal adhesion protein vinculin has been implicated in associating with soluble and membranous phospholipids. Detailed investigations over the past ten years describe the intermolecular interactions of the vinculin tail domain with soluble and membrane phospholipids. Previous studies have implied that the tail's unstructured C‐terminal region affects the mechanical behavior of cells and that the same region, at the molecular level, has bi‐stable behavior sensitive to different protonation states. The aim of this short communication is to discuss whether the C‐terminal vinculin tail (Vt) domain interacts favorably with membrane‐embedded phospholipids such as PIP 2 and that the region is also an anchor for lipid membranes.