PMID- 10207085
OWN - NLM
STAT- MEDLINE
DCOM- 19990518
LR  - 20190508
IS  - 0270-7306 (Print)
IS  - 0270-7306 (Linking)
VI  - 19
IP  - 5
DP  - 1999 May
TI  - The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger
      transcription factor.
PG  - 3614-23
AB  - 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 a 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.
FAU - Daniel, J M
AU  - Daniel JM
AD  - Department of Cell Biology, Vanderbilt University, Nashville, Tennessee
      37232-2175, USA.
FAU - Reynolds, A B
AU  - Reynolds AB
LA  - eng
SI  - GENBANK/AF097416
GR  - P30 CA068485/CA/NCI NIH HHS/United States
GR  - R01 CA055724/CA/NCI NIH HHS/United States
GR  - CA 55724/CA/NCI NIH HHS/United States
GR  - CA 68485/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (Catenins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Phosphoproteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Transcription Factors)
RN  - 0 (ZNF-kaiso protein, human)
RN  - 0 (delta catenin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Catenins
MH  - Cell Adhesion Molecules/*metabolism
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Fluorescent Antibody Technique
MH  - Humans
MH  - Molecular Sequence Data
MH  - Mutation
MH  - Nuclear Proteins/analysis
MH  - Phosphoproteins/*metabolism
MH  - Precipitin Tests
MH  - RNA, Messenger/metabolism
MH  - Sequence Alignment
MH  - Transcription Factors/*genetics/metabolism
MH  - *Zinc Fingers
PMC - PMC84161
EDAT- 1999/04/17 00:00
MHDA- 1999/04/17 00:01
CRDT- 1999/04/17 00:00
PHST- 1999/04/17 00:00 [pubmed]
PHST- 1999/04/17 00:01 [medline]
PHST- 1999/04/17 00:00 [entrez]
AID - 10.1128/mcb.19.5.3614 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1999 May;19(5):3614-23. doi: 10.1128/mcb.19.5.3614.