BIOMAT Database Logo BIOMAT Database Logo

CD45 protein-tyrosine phosphatase associates with the WW domain-containing protein, CD45AP, through the transmembrane region. 1995

E D Cahir McFarland, and M L Thomas
Howard Hughes Medical Institute, Department of Pathology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.

CD45 is a transmembrane protein-tyrosine phosphatase required for antigen receptor signaling in lymphocytes. CD45 activates the Src family protein-tyrosine kinases, p56lck and p59fyn, by dephosphorylating a negative regulatory tyrosine in the carboxyl terminus. Immunoprecipitation of CD45 precipitates p56lck and CD45AP. Although the function of CD45AP is unknown, it has been proposed to be an adapter between p56lck and CD45. To assess the ability of CD45AP to function as an adapter, we determined the regions required for the interaction with CD45 by expressing chimeric proteins in HeLa cells. CD45AP has a region similar to a potential protein-protein interaction domain, the WW domain. Surprisingly, this domain was not necessary for the association with CD45. Rather, a 40-amino acid sequence encompassing the putative transmembrane domain of CD45AP was sufficient to mediate binding to CD45. Similarly, a 39-amino acid sequence encompassing the CD45 transmembrane region was sufficient to direct the interaction with CD45AP. Expression of p56lck with CD45AP resulted in an interaction that could only be detected by in vitro kinase reaction, suggesting that the association of p56lck and CD45AP is weak. These data support a model in which CD45AP links CD45 with other proteins but not necessarily p56lck.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010750 Phosphoproteins Phosphoprotein
D011518 Proto-Oncogene Proteins Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity. Cellular Proto-Oncogene Proteins,c-onc Proteins,Proto Oncogene Proteins, Cellular,Proto-Oncogene Products, Cellular,Cellular Proto Oncogene Proteins,Cellular Proto-Oncogene Products,Proto Oncogene Products, Cellular,Proto Oncogene Proteins,Proto-Oncogene Proteins, Cellular,c onc Proteins
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

Related Publications

E D Cahir McFarland, and M L Thomas
New insights into the transmembrane protein tyrosine phosphatase CD45.
November 2001, The international journal of biochemistry & cell biology,
E D Cahir McFarland, and M L Thomas
The transmembrane protein-tyrosine phosphatase CD45 is associated with decreased insulin receptor signaling.
January 1996, The Journal of biological chemistry,
E D Cahir McFarland, and M L Thomas
CD45: a transmembrane protein tyrosine phosphatase involved in the transduction of antigenic signals.
February 1992, Biochemical Society transactions,
E D Cahir McFarland, and M L Thomas
CD45 protein-tyrosine phosphatase inhibitor development.
January 2003, Current topics in medicinal chemistry,
E D Cahir McFarland, and M L Thomas
Regulation of integrin-mediated T cell adhesion by the transmembrane protein tyrosine phosphatase CD45.
June 1999, Journal of immunology (Baltimore, Md. : 1950),
E D Cahir McFarland, and M L Thomas
The regulation of B- and T-lymphocyte activation by the transmembrane protein tyrosine phosphatase CD45.
April 1994, Current opinion in cell biology,
E D Cahir McFarland, and M L Thomas
Integrin CD11a cytoplasmic tail interacts with the CD45 membrane-proximal protein tyrosine phosphatase domain 1.
July 2005, Immunology,
E D Cahir McFarland, and M L Thomas
CD45. A prototype for transmembrane protein tyrosine phosphatases.
December 1991, The Journal of biological chemistry,
E D Cahir McFarland, and M L Thomas
Isoforms of the transmembrane tyrosine phosphatase CD45 differentially affect T cell recognition.
May 1994, Immunity,
E D Cahir McFarland, and M L Thomas
Point mutation in the second phosphatase domain of CD45 abrogates tyrosine phosphatase activity.
January 1995, Biochemical and biophysical research communications,
Copied contents to your clipboard!