Linked Life Data

18239272

Source:http://linkedlifedata.com/resource/pubmed/id/18239272

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2008-2-1
pubmed:abstractText
A novel phosphorylation motif for casein kinase 1 (CK1) in response to two sulfated lipids [sulfatide and cholesterol-3-sulfate (SCS)] was determined, using three functional proteins [myelin basic protein (MBP), tau protein (TP) and RhoA (a small GTPase)] and five synthetic MBP peptides as phosphate acceptors for the kinase in vitro. It was found that (i) MBP, p8 (positions 38-118) cleaved from MBP, and a synthetic peptide M103 were effectively phosphorylated by CK1delta in the presence of SCS; (ii) sulfatide in comparison with CH-3S highly enhanced autophosphorylation of CK1delta; (iii) SCS had a high binding affinity with MBP and peptide M103, but not other MBP peptides lacking K-G-R; and (iv) a novel consensus phosphorylation motif (K/R-X-K/R-X-X-S/T) for CK1 was identified among several SCS-binding proteins (SCS-BPs) and three CK1 isoforms (delta, epsilon and gamma). The binding of SCS to two basic brain proteins (MBP and TP) resulted in the high stimulation of their phosphorylation by three CK1 isoforms (alpha, delta and epsilon), but not CK1gamma. In contrast, an acidic protein (RhoA) was effectively phosphorylated by CK1delta in the presence of SCS, and also highly phosphorylated by CK1gamma in the presence of sulfatide. Our results presented here suggest that (i) sulfatide may function as an effective stimulator for autophosphorylation of CK1; and (ii) cellular SCS-binding proteins, containing novel phosphorylation motifs for CK1, may be preferentially phosphorylated by CK1 with isoform specificity at the highly accumulated level of SCS in the brain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
31
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
193-200
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
A novel consensus phosphorylation motif in sulfatide- and cholesterol-3-sulfate-binding protein substrates for CK1 in vitro.
pubmed:affiliation
Laboratory of Signal Biology, Graduate School of Medical Sciences, Kitasato University, Sagamihara, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't