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Published on: May 26, 2011
Molecular cloning of a mouse epithelial protein-tyrosine phosphatase with similarities to submembranous proteins
W Hendriks1, J Schepens, D Bächner
1Department of Cell Biology and Histology, University of Nijmegen, The Netherlands.
Abstract:
Protein-tyrosine phosphatases (PTPases) form an important class of cell regulatory proteins. We have isolated overlapping cDNA clones that together comprise an 8 kb transcript encoding a novel murine PTPase which is expressed in various organs. Sequence analysis revealed an open reading frame of 2,460 amino acid residues. The predicted protein, PTP-BL, is a large non-transmembrane PTPase that exhibits 80% homology with PTP-BAS, a recently described human PTPase. PTP-BL shares some intriguing sequence homologies with submembranous proteins. It contains a band 4.1-like motif also present in the tumor suppressors neurofibromatosis 2 and expanded, five 80 amino acid repeats also present in the discs-large tumor suppressor, and a single catalytic phosphatase domain. No obvious homologies to other proteins were found for the N-terminal region of the protein other than human PTP-BAS. RNA in situ hybridization experiments show that the PTP-BL gene is expressed in epithelial cells, predominantly in kidney, lung, and skin. These data suggest a cell cortical localization for PTP-BL in epithelial cells and a possible role in the morphology and motility of epithelial tissues.
Insights
Researchers discovered a new protein-tyrosine phosphatase (PTPase) in mice, named PTP-BL. This large enzyme, found in epithelial cells, may play a role in tissue structure and movement.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Protein-tyrosine phosphatases (PTPases) are crucial regulators of cellular processes.
- Understanding novel PTPases is key to deciphering complex cell signaling pathways.
Purpose of the Study:
- To identify and characterize a novel murine protein-tyrosine phosphatase.
- To investigate the structural features and expression patterns of the newly discovered PTPase.
Main Methods:
- Isolation and sequencing of cDNA clones encoding the novel PTPase.
- Sequence analysis to predict protein structure and homology.
- RNA in situ hybridization to determine gene expression patterns.
Main Results:
- An 8 kb transcript encoding a large, non-transmembrane PTPase, PTP-BL, was identified.
- PTP-BL shares homology with human PTP-BAS and contains domains found in submembranous proteins.
- PTP-BL gene expression is prominent in epithelial cells of the kidney, lung, and skin.
Conclusions:
- PTP-BL is a novel murine PTPase with structural similarities to known regulatory proteins.
- Its expression in epithelial tissues suggests a role in cell morphology and motility.
- Further research into PTP-BL could reveal new insights into epithelial tissue regulation.
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