The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.
Protein tyrosine phosphatase-basophil like (PTP-BL) is a large non-transmembrane protein tyrosine phosphatase implicated in the modulation of the cytoskeleton. Here we describe a novel interaction of PTP-BL with the protein kinase C-related kinase 2 (PRK2), a serine/threonine kinase regulated by the G-protein rho. This interaction is mediated by the PSD-95, ... Drosophila discs large, zonula occludens (PDZ)3 domain of PTP-BL and the extreme C-terminus of PRK2 as shown by yeast two-hybrid assays and coimmunoprecipitation experiments from transfected HeLa cells. In particular, we demonstrate that a conserved C-terminal cysteine of PRK2 is indispensable for the interaction with PTP-BL. In HeLa cells we demonstrate colocalization of both proteins in lamellipodia like structures. Interaction of PTP-BL with the rho effector kinase PRK2 gives further evidence for a possible function of PTP-BL in the regulation of the actin cytoskeleton.
Mesh Terms:
Actins, Amino Acid Motifs, Animals, Basophils, Conserved Sequence, Cysteine, Cytoskeleton, DNA, Complementary, Gene Library, Hela Cells, Humans, Plasmids, Precipitin Tests, Protein Binding, Protein Kinase C, Protein Structure, Tertiary, Protein Tyrosine Phosphatase, Non-Receptor Type 13, Protein Tyrosine Phosphatases, Rats, Transfection, Two-Hybrid System Techniques
Actins, Amino Acid Motifs, Animals, Basophils, Conserved Sequence, Cysteine, Cytoskeleton, DNA, Complementary, Gene Library, Hela Cells, Humans, Plasmids, Precipitin Tests, Protein Binding, Protein Kinase C, Protein Structure, Tertiary, Protein Tyrosine Phosphatase, Non-Receptor Type 13, Protein Tyrosine Phosphatases, Rats, Transfection, Two-Hybrid System Techniques
FEBS Lett.
Date: May. 11, 2001
PubMed ID: 11356191
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