title: The protein tyrosine phosphatase PTP-Basophil/Basophil-like. Interacting proteins and molecular functions.
abstract: The protein tyrosine phosphatase PTP-Basophil (PTP-Bas) and its mouse homologue, PTP-Basophil-like (PTP-BL), are high molecular mass protein phosphatases consisting of a number of diverse protein-protein interaction modules. Several splicing variants of these phosphatases are known to exist thus demonstrating the complexity of these molecules. PTP-Bas/BL serves as a central scaffolding protein facilitating the assembly of a multiplicity of different proteins mainly via five different PDZ domains. Many of these interacting proteins are implicated in the regulation of the actin cytoskeleton. However, some proteins demonstrate a nuclear function of this protein tyrosine phosphatase. PTP-Bas is involved in the regulation of cell surface expression of the cell death receptor, Fas. Moreover, it is a negative regulator of ephrinB phosphorylation, a receptor playing an important role during development. The phosphorylation status of other proteins such as RIL, IkappaBalpha and beta-catenin can also be regulated by this phosphatase. Finally, PTP-BL has been shown to be involved in the regulation of cytokinesis, the last step in cell division. Although the precise molecular function of PTP-Bas/BL is still elusive, current data suggest clearly that PTP-Bas/BL belongs to the family of PDZ domain containing proteins involved in the regulation of the cytoskeleton and of intracellular vesicular transport processes.
authors.affiliation: Department of Molecular Neurobiochemistry, Ruhr-University Bochum, Germany. kai.erdmann@yale.edu
authors.forename: Kai S
authors.initials: KS
authors.lastname: Erdmann
mesh_terms: D000818:Animals; D017209:Apoptosis; D002455:Cell Division; D003599:Cytoskeleton / Q000378:metabolism; D036387:Ephrin-B1 / Q000737:chemistry; D006801:Humans; D017403:In Situ Hybridization; D008954:Models, Biological; D008957:Models, Genetic; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry / Q000502:physiology*; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D015398:Signal Transduction; D019014:fas Receptor / Q000737:chemistry
chemical_list: D036387:Ephrin-B1; D019014:fas Receptor; D012313:RNA; C516742:PTPN13 protein, human; D054595:Protein Tyrosine Phosphatase, Non-Receptor Type 13; D017027:Protein Tyrosine Phosphatases; C516743:Ptpn13 protein, mouse