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 PIP2 and that the region is also an anchor for lipid membranes.
journal_name
Cell Biol Intjournal_title
Cell biology internationalauthors
Goldmann WHdoi
10.1002/cbin.10978subject
Has Abstractpub_date
2018-08-01 00:00:00pages
1076-1078issue
8eissn
1065-6995issn
1095-8355journal_volume
42pub_type
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