BIOMAT Database Logo BIOMAT Database Logo

ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. 1999

K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
Pharmaceutical Biotechnology Sector, Biotechnology Research Institute, Montreal, Quebec H4P 2R2, Canada.

Protein-protein interactions play an important role in the specificity of cellular signaling cascades. By using the yeast two-hybrid system, a specific interaction was identified between the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E and a novel protein, which was termed ZRP-1 to indicate its sequence similarity to the Zyxin protein family. The mRNA encoding this protein is distributed widely in human tissues and contains an open reading frame of 1428 base pairs, predicting a polypeptide of 476 amino acid residues. The deduced protein displays a proline-rich amino-terminal region and three double zinc finger LIM domains at its carboxyl terminus. The specific interaction of this novel protein with the second PDZ domain of hPTP1E was demonstrated both in vitro, using bacterially expressed proteins, and in vivo, by co-immunoprecipitation studies. Deletion analysis indicated that an intact carboxyl terminus is required for its interaction with the second PDZ domain of hPTP1E in the yeast two-hybrid system and suggested that other sequences, including the LIM domains, also participate in the interaction. The genomic organization of the ZRP-1 coding sequence is identical to that of the lipoma preferred partner gene, another Zyxin-related protein, suggesting that the two genes have evolved from a recent gene duplication event.

UI MeSH Term Description Entries
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
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000074183 ATPases Associated with Diverse Cellular Activities A large highly conserved family of ATPases with diverse functions in cells that are characterized by the presence of a P-LOOP and a ring shape. They couple the energy generated by ATP hydrolysis to remodeling or mechanical translocation of their target molecules. AAA ATPase,AAA Protease,AAA+ ATPase,AAA+ Protease,AAA ATPases,AAA Proteases,AAA+ ATPases,AAA+ Proteases,ATPase, AAA,ATPase, AAA+,ATPases, AAA+,Protease, AAA,Protease, AAA+,Proteases, AAA,Proteases, AAA+
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
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014157 Transcription Factors Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process. Transcription Factor,Factor, Transcription,Factors, Transcription
D017027 Protein Tyrosine Phosphatases An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis. Phosphotyrosine Phosphatase,Protein-Tyrosine-Phosphatase,Tyrosyl Phosphoprotein Phosphatase,PTPase,Phosphotyrosyl Protein Phosphatase,Protein-Tyrosine Phosphatase,Phosphatase, Phosphotyrosine,Phosphatase, Phosphotyrosyl Protein,Phosphatase, Protein-Tyrosine,Phosphatase, Tyrosyl Phosphoprotein,Phosphatases, Protein Tyrosine,Phosphoprotein Phosphatase, Tyrosyl,Protein Phosphatase, Phosphotyrosyl,Protein Tyrosine Phosphatase,Tyrosine Phosphatases, Protein

Related Publications

K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL.
April 2000, European journal of cell biology,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1.
September 1997, The Journal of biological chemistry,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.
May 2001, FEBS letters,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein.
January 1998, Current biology : CB,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
Energetics of peptide recognition by the second PDZ domain of human protein tyrosine phosphatase 1E.
January 2007, Biochemistry,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
Rat protein tyrosine phosphatase eta physically interacts with the PDZ domains of syntenin.
June 2001, FEBS letters,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
Solution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions.
July 2002, Journal of molecular biology,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain.
August 2000, Oncogene,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
Histidine domain-protein tyrosine phosphatase interacts with Grb2 and GrpL.
December 2010, PloS one,
K K Murthy, and K Clark, and Y Fortin, and S H Shen, and D Banville
PDZ domain protein GIPC interacts with the cytoplasmic tail of melanosomal membrane protein gp75 (tyrosinase-related protein-1).
September 2001, The Journal of biological chemistry,
Copied contents to your clipboard!