Analysis of protein-lipid interactions using purified C2 domains

Perez-Sancho, Jessica, Schapire, Arnaldo L., Botella, Miguel A. and Rosado, Abel (2016). Analysis of protein-lipid interactions using purified C2 domains. In Jose R. Botella and Miguel A. Botella (Ed.), Plant signal transduction (pp. 175-187) New York, NY, United States: Humana Press. doi:10.1007/978-1-4939-3115-6_14

Author Perez-Sancho, Jessica
Schapire, Arnaldo L.
Botella, Miguel A.
Rosado, Abel
Title of chapter Analysis of protein-lipid interactions using purified C2 domains
Title of book Plant signal transduction
Place of Publication New York, NY, United States
Publisher Humana Press
Publication Year 2016
Sub-type Research book chapter (original research)
DOI 10.1007/978-1-4939-3115-6_14
Open Access Status Not yet assessed
ISBN 9781493931149
ISSN 1064-3745
Editor Jose R. Botella
Miguel A. Botella
Volume number 1363
Chapter number 14
Start page 175
End page 187
Total pages 13
Total chapters 19
Collection year 2017
Language eng
Formatted Abstract/Summary
C2 domains (C2s) are regulatory protein modules identified in eukaryotic proteins targeted to cell membranes. C2s were initially characterized as independently folded Ca2+-dependent phospholipids binding domains; however, later studies have shown that C2s have evolutionarily diverged into Ca2+-dependent and Ca2+-independent forms. These forms interact and regulate their affinity to diverse lipid species using different binding mechanisms. In this protocol we describe a biochemical approach to produce, purify, and solubilize functional C2 domains bound to GST for the identification of their putative Ca2+-dependent and Ca2+-independent lipid-binding partners.
Keyword C2 domain
Ca2+-dependent lipid binding
Multilamellar vesicles
Protein-lipid overlay assay
Q-Index Code B1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Book Chapter
Collection: Scopus Import
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