Purification and cloning of PZR, a binding protein and putative physiological substrate of tyrosine phosphatase SHP-2.
Overexpression of a catalytically inactive mutant of tyrosine phosphatase SHP-2 in 293 cells resulted in hyperphosphorylation of a glycoprotein specifically associated with the enzyme. The protein has been purified to near homogeneity. Based on the amino acid sequences of peptides obtained from the protein, a full-length cDNA was isolated. The ... cDNA encodes a protein with a single transmembrane segment and a signal sequence. The extracellular portion of the protein contains a single immunoglobulin-like domain displaying 46% sequence identity to that of myelin P0, a major structural protein of peripheral myelin. The intracellular segment of the protein shows no significant sequence identity to any known protein except for two immunoreceptor tyrosine-based inhibitory motifs. We name the protein PZR for protein zero related. Transfection of the PZR cDNA in Jurkat cells gave rise to a protein of expected molecular size. Stimulation of cells with pervanadate resulted in tyrosine phosphorylation of PZR and a near-stoichiometric association of PZR with SHP-2. Northern blotting analyses revealed that PZR is widely expressed in human tissues and is particularly abundant in heart, placenta, kidney, and pancreas. As a binding protein and a putative substrate of SHP-2, PZR protein may have an important role in cell signaling.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Blotting, Northern, Carrier Proteins, Cell Line, Chromatography, High Pressure Liquid, Cloning, Molecular, DNA, Complementary, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Phosphoproteins, Precipitin Tests, Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, Sequence Homology, Amino Acid, Substrate Specificity
Amino Acid Sequence, Base Sequence, Blotting, Northern, Carrier Proteins, Cell Line, Chromatography, High Pressure Liquid, Cloning, Molecular, DNA, Complementary, Humans, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Phosphoproteins, Precipitin Tests, Protein Tyrosine Phosphatase, Non-Receptor Type 11, Protein Tyrosine Phosphatase, Non-Receptor Type 6, Protein Tyrosine Phosphatases, Sequence Homology, Amino Acid, Substrate Specificity
J. Biol. Chem.
Date: Nov. 06, 1998
PubMed ID: 9792637
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