Mutations in the APC gene and their implications for protein structure and function.
An enormous number of germline and somatic mutations have been identified in the APC tumor suppressor gene. Nearly all of these mutations result in premature polypeptide chain termination, but the consequences to APC protein function are unknown. Recent advances, including the identification of an oligomerization domain, the localization of several beta-catenin binding sites, some of which down-regulate beta-catenin in vivo, and the identification of a microtubule-binding domain in the carboxy-terminal region of APC, are beginning to provide some clues.
Polakis
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Onyx Pharmaceuticals, Richmond, California 94806, USA.
D025601:Adenomatous Polyposis Coli Protein; D000818:Animals; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D017491:Genes, APC; D006801:Humans; D009154:Mutation; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D025601:Adenomatous Polyposis Coli Protein; D003598:Cytoskeletal Proteins