Some protein tyrosine phosphatases target in part to lipid rafts and interact with caveolin-1.
A profile-based search of the SWISS-PROT database reveals that most protein tyrosine phosphatases (PTPs) contain at least one caveolin-1-binding motif. To ascertain if the presence of caveolin-binding motif(s) in PTPs corresponds to their actual localization in caveolin-1-enriched membrane fractions, we performed subcellular fractionating experiments. We found that all tested PTPs ... (PTP1B, PTP1C, SHPTP2, PTEN, and LAR) are actually localized in caveolin-enriched membrane fractions, despite their distribution in other subcellular sites, too. More than 1/2 of LAR and about 1/4 of SHPTP2 and PTP-1C are localized in caveolin-enriched membrane fractions whereas, in these fractions, PTP-1B and PTEN are poorly concentrated. Co-immunoprecipitation experiments with antibodies specific for each tested PTP demonstrated that all five phosphatases form molecular complexes with caveolin-1 in vivo. Collectively, our findings propose that particular PTPs could perform some of their cellular actions or are regulated by recruitment into caveolin-enriched membrane fractions.
Mesh Terms:
Amino Acid Motifs, Binding Sites, Caveolin 1, Caveolins, Cell Line, Humans, Macromolecular Substances, Membrane Microdomains, Precipitin Tests, Protein Transport, Protein Tyrosine Phosphatases
Amino Acid Motifs, Binding Sites, Caveolin 1, Caveolins, Cell Line, Humans, Macromolecular Substances, Membrane Microdomains, Precipitin Tests, Protein Transport, Protein Tyrosine Phosphatases
Biochem. Biophys. Res. Commun.
Date: Aug. 23, 2002
PubMed ID: 12176037
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