PMID- 10187801
OWN - NLM
STAT- MEDLINE
DCOM- 19990503
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 15
DP  - 1999 Apr 9
TI  - Phosphorylation and free pool of beta-catenin are regulated by tyrosine kinases 
      and tyrosine phosphatases during epithelial cell migration.
PG  - 10173-83
AB  - Cell migration requires precise control, which is altered or lost when tumor 
      cells become invasive and metastatic. Although the integrity of cell-cell 
      contacts, such as adherens junctions, is essential for the maintenance of 
      functional epithelia, they need to be rapidly disassembled during migration. The 
      transmembrane cell adhesion protein E-cadherin and the cytoplasmic catenins are 
      molecular elements of these structures. Here we demonstrate that epithelial cell 
      migration is accompanied by tyrosine phosphorylation of beta-catenin and an 
      increase of its free cytoplasmic pool. We show further that the protein-tyrosine 
      phosphatase LAR (leukocyte common antigen related) colocalizes with the 
      cadherin-catenin complex in epithelial cells and associates with beta-catenin and 
      plakoglobin. Interestingly, ectopic expression of protein-tyrosine phosphatase 
      (PTP) LAR inhibits epithelial cell migration by preventing phosphorylation and 
      the increase in the free pool of beta-catenin; moreover, it inhibits tumor 
      formation in nude mice. These data support a function for PTP LAR in the 
      regulation of epithelial cell-cell contacts at adherens junctions as well as in 
      the control of beta-catenin signaling functions. Thus PTP-LAR appears to play an 
      important role in the maintenance of epithelial integrity, and a loss of its 
      regulatory function may contribute to malignant progression and metastasis.
FAU - Muller, T
AU  - Muller T
AD  - Department of Molecular Biology, Max Planck Institute for Biochemistry, Am 
      Klopferspitz 18a, 82152 Martinsried, Federal Republic of Germany. 
      Mueller@ariad.com
FAU - Choidas, A
AU  - Choidas A
FAU - Reichmann, E
AU  - Reichmann E
FAU - Ullrich, A
AU  - Ullrich A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (CTNNB1 protein, human)
RN  - 0 (CTNNB1 protein, mouse)
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Ctnnb1 protein, rat)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Desmoplakins)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Trans-Activators)
RN  - 0 (beta Catenin)
RN  - 0 (gamma Catenin)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 3.1.3.48 (PTPRA protein, human)
RN  - EC 3.1.3.48 (PTPRF protein, human)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
RN  - EC 3.1.3.48 (Ptpra protein, mouse)
RN  - EC 3.1.3.48 (Ptpra protein, rat)
RN  - EC 3.1.3.48 (Ptprf protein, mouse)
RN  - EC 3.1.3.48 (Ptprf protein, rat)
RN  - EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 2)
RN  - EC 3.1.3.48 (Receptor-Like Protein Tyrosine Phosphatases, Class 4)
SB  - IM
MH  - Animals
MH  - Cadherins/metabolism
MH  - Cell Adhesion Molecules/metabolism
MH  - Cell Communication
MH  - Cell Movement
MH  - Cell Transformation, Neoplastic
MH  - Cytoskeletal Proteins/*metabolism
MH  - Desmoplakins
MH  - Desmosomes/metabolism
MH  - Epithelial Cells/cytology/*physiology
MH  - Humans
MH  - Mice
MH  - Mice, Nude
MH  - Neoplasm Invasiveness
MH  - Neoplasm Metastasis
MH  - *Nerve Tissue Proteins
MH  - Phosphorylation
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - Rats
MH  - Receptor-Like Protein Tyrosine Phosphatases, Class 2
MH  - Receptor-Like Protein Tyrosine Phosphatases, Class 4
MH  - Receptors, Cell Surface/*metabolism
MH  - *Trans-Activators
MH  - Tumor Cells, Cultured
MH  - beta Catenin
MH  - gamma Catenin
EDAT- 1999/04/03 00:00
MHDA- 1999/04/03 00:01
CRDT- 1999/04/03 00:00
PHST- 1999/04/03 00:00 [pubmed]
PHST- 1999/04/03 00:01 [medline]
PHST- 1999/04/03 00:00 [entrez]
AID - S0021-9258(19)73699-0 [pii]
AID - 10.1074/jbc.274.15.10173 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Apr 9;274(15):10173-83. doi: 10.1074/jbc.274.15.10173.