Preparing your results

Our searching services are busy right now. Your search will reload in five seconds.

X
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Functional interaction of an axin homolog, conductin, with beta-catenin, APC, and GSK3beta.

Science (New York, N.Y.) | Apr 24, 1998

http://www.ncbi.nlm.nih.gov/pubmed/9554852

Control of stability of beta-catenin is central in the wnt signaling pathway. Here, the protein conductin was found to form a complex with both beta-catenin and the tumor suppressor gene product adenomatous polyposis coli (APC). Conductin induced beta-catenin degradation, whereas mutants of conductin that were deficient in complex formation stabilized beta-catenin. Fragments of APC that contained a conductin-binding domain also blocked beta-catenin degradation. Thus, conductin is a component of the multiprotein complex that directs beta-catenin to degradation and is located downstream of APC. In Xenopus embryos, conductin interfered with wnt-induced axis formation.

Pubmed ID: 9554852 RIS Download

Mesh terms: Adenomatous Polyposis Coli Protein | Amino Acid Sequence | Animals | Axin Protein | Binding Sites | Body Patterning | Calcium-Calmodulin-Dependent Protein Kinases | Cytoskeletal Proteins | Glycogen Synthase Kinase 3 | Humans | Mice | Molecular Sequence Data | Mutation | Phosphorylation | Proteins | Proto-Oncogene Proteins | Repressor Proteins | Signal Transduction | Trans-Activators | Tumor Cells, Cultured | Xenopus | Xenopus Proteins | beta Catenin

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

None

BioGRID (Data, Interactions)

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.