Linked Life Data

11377816

Source:http://linkedlifedata.com/resource/pubmed/id/11377816

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2001-5-29
pubmed:abstractText
The biosynthesis of gangliosides is known to be under strict metabolic control. One level of control is through post-translational modification of the glycosyltransferases responsible for their biosynthesis. Thus, the activities of several sialyltransferases have been demonstrated to be downregulated by the action of protein kinase C (PKC) in cell-free and intact cell systems. This modulatory effect can be reversed at least in part by the action of membrane-bound phosphatases. In contrast, the activity of N-acetylgalactosaminyltransferase can be upregulated by the action of protein kinase A (PKA) in cultured cells. In addition, studies from several laboratories have demonstrated that phosphorylation of certain glycosyltransferases can affect their intracellular processing and translocation. Thus, modulation of glycosyltransferases by phosphorylation and dephosphorylation should represent an important regulatory mechanism for ganglioside biosynthesis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
177
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Regulation of glycosyltransferases in ganglioside biosynthesis by phosphorylation and dephosphorylation.
pubmed:affiliation
Institute of Molecular Medicine and Genetics, Medical College of Georgia, 1120 15th Street, Augusta, GA 30912, USA. ryu@mail.mcg.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review