Linked Life Data

12628243

Source:http://linkedlifedata.com/resource/pubmed/id/12628243

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-3-11
pubmed:abstractText
The tumour suppressor protein adenomatous polyposis coli (APC) regulates the level and the intracellular localisation of the proto-oncoprotein beta-catenin. There are indications that a region comprising seven homologous 20-amino acid residue repeats within the APC protein is responsible for the interaction with beta-catenin and that the phosphorylation of conserved serine residues within these repeats increases the affinity for beta-catenin. We used biophysical methods to analyse the beta-catenin binding of single repeats or repeat combinations as non-phosphorylated or phosphorylated recombinant proteins. The non-phosphorylated repeats showed similar affinities, no matter whether they were tested as single recombinant repeats or in combination with neighbouring repeats. This result makes a cooperative influence between the repetitive motifs unlikely. The phosphorylation of the APC protein was mimicked by specific serine/aspartate mutations, which align to serine residues in the cytoplasmic beta-catenin binding domain of E-cadherin. Remarkably, the mimicked phosphorylation of a serine, which is not involved in beta-catenin interaction in the E-cadherin/beta-catenin complex, led to a significant increase in the APC affinity for beta-catenin. These results indicate structural differences between the E-cadherin/beta-catenin and the APC/beta-catenin complexes and provide quantitative evidence for the importance of the APC phosphorylation for its interaction with beta-catenin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
327
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
359-67
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12628243-Adenomatous Polyposis Coli, pubmed-meshheading:12628243-Adenomatous Polyposis Coli Protein, pubmed-meshheading:12628243-Aspartic Acid, pubmed-meshheading:12628243-Cadherins, pubmed-meshheading:12628243-Calorimetry, pubmed-meshheading:12628243-Cytoplasm, pubmed-meshheading:12628243-Cytoskeletal Proteins, pubmed-meshheading:12628243-Glutathione Transferase, pubmed-meshheading:12628243-Humans, pubmed-meshheading:12628243-Molecular Mimicry, pubmed-meshheading:12628243-Molecular Weight, pubmed-meshheading:12628243-Mutagenesis, Site-Directed, pubmed-meshheading:12628243-Peptide Fragments, pubmed-meshheading:12628243-Phosphorylation, pubmed-meshheading:12628243-Protein Binding, pubmed-meshheading:12628243-Recombinant Fusion Proteins, pubmed-meshheading:12628243-Serine, pubmed-meshheading:12628243-Thermodynamics, pubmed-meshheading:12628243-Trans-Activators, pubmed-meshheading:12628243-beta Catenin
pubmed:year
2003
pubmed:articleTitle
Differences between the interaction of beta-catenin with non-phosphorylated and single-mimicked phosphorylated 20-amino acid residue repeats of the APC protein.
pubmed:affiliation
Max-Planck-Institut für molekulare Physiologie, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't