Linked Life Data

9668093

Source:http://linkedlifedata.com/resource/pubmed/id/9668093

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
30
pubmed:dateCreated
1998-8-20
pubmed:abstractText
C2 domains have been identified in a wide range of intracellular proteins, including lipid modifying enzymes, protein kinases, GTPases, and proteins involved in membrane trafficking. Many C2 domains bind membranes in a calcium-dependent manner. The first C2 domain from synaptotagmin I (SytIC2A) and the C2 domain from cytosolic phospholipase A2 (cPLA2C2) are among the best characterized C2 domains in terms of their structures and calcium binding. Here we demonstrate that the protein-lipid interaction is dramatically different for these two domains. Photolabeling with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine ([125I]TID) in the presence of phospholipid vesicles indicates that cPLA2C2 penetrates into the hydrophobic region of the membrane. Hydrophobic surfaces on cPLA2C2 are exposed even in the absence of calcium, but only in its presence does the domain penetrate into the nonpolar core of the membrane. The interaction of SytIC2A with phospholipid membranes is primarily electrostatic with binding being abolished in 500 mM NaCl. Because soluble phospholipid head group analogues do not compete with binding of either SytIC2A or cPLA2C2 to vesicles, it is likely that membrane binding by these domains involves multiple interactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19093-6
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Calcium-dependent membrane penetration is a hallmark of the C2 domain of cytosolic phospholipase A2 whereas the C2A domain of synaptotagmin binds membranes electrostatically.
pubmed:affiliation
Medical Research Council, Laboratory of Molecular Biology, MRC Centre, Hills Road, Cambridge CB22QH, United Kingdom. baz@mrc-lmb.cam.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't