Title : Kinetic analysis of the interaction of the C1 domain of protein kinase C with lipid membranes by stopped-flow spectroscopy.

Pub. Date : 2008 Mar 21

PMID : 18187412






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The diacylglycerol (DG)/phorbol ester-dependent translocation of conventional protein kinase C (PKC) isozymes is mediated by the C1 domain, a membrane-targeting module that also selectively binds phosphatidylserine (PS). Phorbol Esters protein kinase C beta Homo sapiens
2 The decreased effectiveness of DG compared with phorbol esters in retaining the C1 domain on membranes contributes to the molecular dichotomy of the rapid, transient nature of DG-dependent PKC signaling versus the chronic hyperactivity of phorbol ester-activated PKC. Phorbol Esters protein kinase C beta Homo sapiens
3 The decreased effectiveness of DG compared with phorbol esters in retaining the C1 domain on membranes contributes to the molecular dichotomy of the rapid, transient nature of DG-dependent PKC signaling versus the chronic hyperactivity of phorbol ester-activated PKC. Phorbol Esters protein kinase C beta Homo sapiens