Wirth, Volker F. and List, Felix and Diez, Gerold and Goldmann, Wolfgang H. (2010) Vinculin's C-terminal region facilitates phospholipid membrane insertion. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 398 (3). pp. 433-437. ISSN 0006-291X, 1090-2104
Full text not available from this repository. (Request a copy)Abstract
The focal adhesion protein vinculin has been implicated in associating with soluble and membranous phospholipids. Here, we investigated the intermolecular interactions of two vinculin tail domains with membrane phospholipids. Previous studies have shown that the tail's unstructured C-terminus affects the mechanical behavior of cells, but not the H3 region. The aim of this work was to establish whether the C-terminal or the H3 region either associate favorably with or anchor in lipid membranes. This work characterizes the energetics and dynamics of phospholipid interactions using differential scanning calorimetry (DSC) as well as circular dichroism (CD) spectroscopy. Biochemical data from tryptophan quenching and SDS-PAGE experiments support calorimetric and CD spectroscopic findings insofar that only vinculin's C-terminus inserts into lipid membranes. These in vitro results provide further insight into the mechanical behavior of vinculin tail regions in cells and contribute to the understanding of their structure and function. (C) 2010 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TAIL DOMAIN; LIPID-MEMBRANES; CELL MECHANICS; ADHESION; ACTIVATION; SITE; TURNOVER; BEHAVIOR; PROTEIN; SHAPE; Vinculin; Vinculin tail: H3 and C-terminus; Lipid-membrane binding; Focal adhesions; Differential scanning calorimetry; Circular dichroism spectroscopy; Tryptophan quenching; Gel electrophoresis |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 22 Jul 2020 06:13 |
| Last Modified: | 22 Jul 2020 06:13 |
| URI: | https://pred.uni-regensburg.de/id/eprint/24443 |
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