The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor

Mol Cell Biol. 1999 May;19(5):3614-23. doi: 10.1128/MCB.19.5.3614.

Abstract

p120(ctn) is an Armadillo repeat domain protein with structural similarity to the cell adhesion cofactors beta-catenin and plakoglobin. All three proteins interact directly with the cytoplasmic domain of the transmembrane cell adhesion molecule E-cadherin; beta-catenin and plakoglobin bind a carboxy-terminal region in a mutually exclusive manner, while p120 binds the juxtamembrane region. Unlike beta-catenin and plakoglobin, p120 does not interact with alpha-catenin, the tumor suppressor adenomatous polyposis coli (APC), or the transcription factor Lef-1, suggesting that it has unique binding partners and plays a distinct role in the cadherin-catenin complex. Using p120 as bait, we conducted a yeast two-hybrid screen and identified a novel transcription factor which we named Kaiso. Kaiso's deduced amino acid sequence revealed an amino-terminal BTB/POZ protein-protein interaction domain and three carboxy-terminal zinc fingers of the C2H2 DNA-binding type. Kaiso thus belongs to a rapidly growing family of POZ-ZF transcription factors that include the Drosophila developmental regulators Tramtrak and Bric à brac, and the human oncoproteins BCL-6 and PLZF, which are causally linked to non-Hodgkins' lymphoma and acute promyelocytic leukemia, respectively. Monoclonal antibodies to Kaiso were generated and used to immunolocalize the protein and confirm the specificity of the p120-Kaiso interaction in mammalian cells. Kaiso specifically coprecipitated with a variety of p120-specific monoclonal antibodies but not with antibodies to alpha- or beta-catenin, E-cadherin, or APC. Like other POZ-ZF proteins, Kaiso localized to the nucleus and was associated with specific nuclear dots. Yeast two-hybrid interaction assays mapped the binding domains to Arm repeats 1 to 7 of p120 and the carboxy-terminal 200 amino acids of Kaiso. In addition, Kaiso homodimerized via its POZ domain but it did not heterodimerize with BCL-6, which heterodimerizes with PLZF. The involvement of POZ-ZF proteins in development and cancer makes Kaiso an interesting candidate for a downstream effector of cadherin and/or p120 signaling.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Catenins
  • Cell Adhesion Molecules / metabolism*
  • Cell Line
  • Cloning, Molecular
  • Delta Catenin
  • Fluorescent Antibody Technique
  • Humans
  • Molecular Sequence Data
  • Mutation
  • Nuclear Proteins / analysis
  • Phosphoproteins / metabolism*
  • Precipitin Tests
  • RNA, Messenger / metabolism
  • Sequence Alignment
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Zinc Fingers*

Substances

  • Catenins
  • Cell Adhesion Molecules
  • Nuclear Proteins
  • Phosphoproteins
  • RNA, Messenger
  • Transcription Factors
  • ZBTB33 protein, human
  • Delta Catenin
  • CTNND1 protein, human

Associated data

  • GENBANK/AF097416