The adenomatous polyposis coli (APC) tumor suppressor

Biochim Biophys Acta. 1997 Jun 7;1332(3):F127-47. doi: 10.1016/s0304-419x(97)00008-5.

Abstract

Defects in the APC gene are inarguably linked to the progression of colon cancers that arise both sporadically and through the transmission of germline mutations. Genetic evidence from humans and mouse models suggest that APC is a classic tumor suppressor in that both alleles likely require inactivation for tumor growth to ensue. Nearly all of the mutations, germline and somatic, result in premature termination of the single polypeptide chain, normally consisting of 2843 amino acids. Several definable motifs have now been mapped to the linear amino acid sequence of the APC polypeptide. These include an oligomerization domain, armadillo repeats, binding sites for beta-catenin, the human discs large protein, microtubules, and other proteins of unknown function. Inactivation of APC in cancer is likely due to loss of function(s) normally associated with the deleted protein structure.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenomatous Polyposis Coli / genetics*
  • Adenomatous Polyposis Coli / pathology
  • Adenomatous Polyposis Coli Protein
  • Amino Acid Sequence
  • Animals
  • Cell Division
  • Cytoskeletal Proteins / chemistry
  • Cytoskeletal Proteins / genetics*
  • Cytoskeletal Proteins / metabolism
  • Disease Models, Animal
  • Genes, APC*
  • Humans
  • Molecular Sequence Data
  • Molecular Structure
  • Mutation
  • Trans-Activators*
  • beta Catenin

Substances

  • Adenomatous Polyposis Coli Protein
  • CTNNB1 protein, human
  • Cytoskeletal Proteins
  • Trans-Activators
  • beta Catenin