Linked Life Data

19200342

Source:http://linkedlifedata.com/resource/pubmed/id/19200342

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-4-1
pubmed:abstractText
In order to examine the possible involvements of Ca(2+)/calmodulin-dependent protein kinases (CaM kinases) in the regulation of ribosomal functions, we tested the phosphorylation of rat ribosomal protein S19 (RPS19) by various CaM kinases in vitro. We found that CaM kinase Ialpha, but not CaM kinase Ibeta1, Ibeta2, II, or IV, robustly phosphorylated RPS19. From the consensus phosphorylation site sequence, Ser59, Ser90, and Thr124 were likely to be phosphorylated; therefore, we mutated each amino acid to alanine and found that the mutation of Ser59 to alanine strongly attenuated phosphorylation by CaM kinase Ialpha, suggesting that Ser59 was a major phosphorylation site. Furthermore, we produced a specific antibody against RPS19 phosphorylated at Ser59, and found that Ser59 was phosphorylated both in GT1-7 cells and rat brain. Phosphorylation of RPS19 in GT1-7 cells was inhibited by KN93, an inhibitor of CaM kinases. Immunoblot analysis after subcellular fractionation of rat brain demonstrated that phosphorylated RPS19 was present in 80S ribosomes. Phosphorylation of RPS19 by CaM kinase Ialpha augmented the interaction of RPS19 with the previously identified S19 binding protein. These results suggest that CaM kinase Ialpha regulates the functions of RPS19 through phosphorylation of Ser59.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1471-4159
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
393-402
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Phosphorylation of ribosomal protein S19 at Ser59 by CaM kinase I alpha.
pubmed:affiliation
Department of Biochemistry, University of the Ryukyus, Okinawa, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't