Linked Life Data

12417013

Source:http://linkedlifedata.com/resource/pubmed/id/12417013

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-11-5
pubmed:abstractText
The biological function of protein kinase C (PKC) depends on its catalytic activity and spatial localization. Its catalytic competence and localization in the resting state are regulated by serine/threonine phosphorylations, i.e., "maturation." Upon stimulation of various receptors, PKC is catalytically activated by several activators including diacylglycerol. In addition, PKC often translocates to particular subcellular compartments including the plasma membrane and Golgi complex, and such translation is here referred to as "targeting." In short, the physiological function of PKC is controlled by the three events: maturation, catalytic activation, and targeting. Catalytic activation and targeting contribute to temporal, spatial, and isotype-specific regulation of PKC. This review summarizes the evidence for the role of these three events in the isotype-specific activation of PKC, with particular emphasis on catalytic activation and targeting by lipid mediators.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
663-8
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Activation mechanisms of protein kinase C: maturation, catalytic activation, and targeting.
pubmed:affiliation
Laboratory of Molecular Pharmacology, Biosignal Research Center, Kobe University, Kobe 657-8501.
pubmed:publicationType
Journal Article, Review