Linked Life Data

14529276

Source:http://linkedlifedata.com/resource/pubmed/id/14529276

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2003-10-7
pubmed:abstractText
PKCepsilon is a member of the group of novel PKCs that contain a C2 domain located in their N-terminal region. On the basis of recent structural studies, a series of mutants were prepared to increase our knowledge of the mechanism of the phospholipid binding site of this domain. The results revealed that this domain preferentially binds to phosphatidic acid- and phosphatidylserine-containing vesicles. Although the increase in affinity was linear in the case of phosphatidic acid, it became exponential when the vesicles contained increasing concentrations of phosphatidylserine. Site-directed mutagenesis studies showed that residues W23, R26, and R32 located in loop 1 and I89 and Y91 located in loop 3 are of critical importance when the binding is performed with phosphatidic acid-containing vesicles. Furthermore, when the same mutants were assayed with phosphatidylserine-containing vesicles, no binding was observed in any case, reflecting the smaller affinity of the C2 domain for phosphatidylserine-containing vesicles. A study of the ionic nature of the membrane interaction suggested that it is mainly driven by electrostatic interactions that are disrupted by very low salt concentrations. Differential scanning calorimetry experiments performed to ascertain whether this interaction affected the transition phase of the phosphatidic acid demonstrated that increasing concentrations of the protein lead to changes in the transition, with more than one peak appearing at lower temperatures, which suggests a weak interaction focused on the polar headgroup of the phospholids. In conclusion, a different membrane-binding mode from those previously described in other C2 domains has been found and is seemingly based on electrostatic, interfacial, and hydrophobic interactions without the participation of Ca(2+) ions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
42
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11661-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Characterization of the membrane binding mode of the C2 domain of PKC epsilon.
pubmed:affiliation
Department de Bioquímica y Biología Molecular (A), Facultad de Veterinaria, Universidad de Murcia, Apdo. 4021, E-30100 Murcia, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't