Wirth, Volker F. ; List, Felix ; Diez, Gerold ; Goldmann, Wolfgang H.
Alternative Links zum Volltext:DOIVerlag
| Dokumentenart: | Artikel |
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| Titel eines Journals oder einer Zeitschrift: | Biochemical and Biophysical Research Communications |
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| Verlag: | ACADEMIC PRESS INC ELSEVIER SCIENCE |
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| Ort der Veröffentlichung: | SAN DIEGO |
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| Band: | 398 |
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| Nummer des Zeitschriftenheftes oder des Kapitels: | 3 |
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| Seitenbereich: | S. 433-437 |
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| Datum: | 2010 |
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| Institutionen: | Biologie und Vorklinische Medizin > Institut für Biophysik und physikalische Biochemie |
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| Identifikationsnummer: | | Wert | Typ |
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| 10.1016/j.bbrc.2010.06.094 | DOI |
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| Stichwörter / 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 |
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| Dewey-Dezimal-Klassifikation: | 500 Naturwissenschaften und Mathematik > 570 Biowissenschaften, Biologie |
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| Status: | Veröffentlicht |
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| Begutachtet: | Ja, diese Version wurde begutachtet |
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| An der Universität Regensburg entstanden: | Ja |
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| Dokumenten-ID: | 65940 |
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Web of Science
Zusammenfassung
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 ...
Zusammenfassung
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.
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