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The effect of the sn‐2 acyl chain of diacylglycerol on its interaction with C1 domains and its signaling role
Author(s) -
Kurilova Svetlana,
Yoon Youngdae,
Lee Park Joo,
Bhardwaj Nitin,
Lu Hui,
Cho Wonhwa
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.690.3
Subject(s) - diacylglycerol kinase , membrane , chemistry , fluorescence correlation spectroscopy , biophysics , subcellular localization , biochemistry , signal transduction , intracellular , microbiology and biotechnology , biology , cytoplasm , protein kinase c , molecule , organic chemistry
Diacylglycerol (DAG) is a signaling lipid that interacts with the C1 domain in various target proteins, including protein kinases C, and Ras guanyl nucleotide‐releasing proteins, thereby recruiting them to the plasma membrane. Although these proteins can all bind DAG, some are known to target other intracellular membranes. To understand the basis of this differential membrane targeting, we explored the possibility that a difference in the acyl chain composition of DAG in the plasma membrane and other membranes may affect the C1‐DAG interaction. To test this notion, we measured the binding of the various C1 domains to DAGs with different sn ‐2 acyl groups by fluorescence correlation spectroscopy (FCS). The C1 domains were expressed as an enhanced green fluorescence protein‐fusion protein to enhance protein stability and allow FCS measurements. FCS measurements as well as the molecular dynamics simulation show that the sn ‐2 acyl group of DAG has significant and differential effects on the membrane binding properties of C1 domains, which is consistent with the differential subcellular localization of the C1 domains. Supported by NIH GM76581