PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL
| العنوان: | PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL |
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| المؤلفون: | Bé Wieringa, Wiljan Hendriks, Edwin Cuppen, Herlinde Gerrits, Barry Pepers |
| المساهمون: | Hubrecht Institute for Developmental Biology and Stem Cell Research |
| المصدر: | Molecular Biology of the Cell, 9, pp. 671-683 ResearcherID Scopus-Elsevier Molecular Biology of the Cell, 9(3), 671-683. American Society for Cell Biology Molecular Biology of the Cell, 9, 671-683 |
| سنة النشر: | 1998 |
| مصطلحات موضوعية: | animal structures, Molecular Sequence Data, PDZ domain, chemical and pharmacologic phenomena, Protein tyrosine phosphatase, Plasma protein binding, Biology, Epithelium, Article, Substrate Specificity, Mice, chemistry.chemical_compound, Animals, Humans, Amino Acid Sequence, Phosphorylation, Tyrosine, Molecular Biology, Peptide sequence, LIM domain, Binding Sites, Sequence Homology, Amino Acid, Phage exposition technology as a novel tool to identify partner proteins in signal transduction networks, Microfilament Proteins, Tyrosine phosphorylation, Cell Biology, LIM Domain Proteins, Faag expositie technologie als nieuw middel om partner-eiwitten in signaal transductie netwerken te identificeren, Immunohistochemistry, Rats, Cell biology, DNA-Binding Proteins, Biochemistry, chemistry, Protein Tyrosine Phosphatases, Protein Binding, Signal Transduction |
| الوصف: | The specificity of protein–protein interactions in cellular signaling cascades is dependent on the sequence and intramolecular location of distinct amino acid motifs. We used the two-hybrid interaction trap to identify proteins that can associate with the PDZ motif-rich segment in the protein tyrosine phosphatase PTP-BL. A specific interaction was found with the Lin-11, Isl-1, Mec-3 (LIM) domain containing protein RIL. More detailed analysis demonstrated that the binding specificity resides in the second and fourth PDZ motif of PTP-BL and the LIM domain in RIL. Immunohistochemistry on various mouse tissues revealed a submembranous colocalization of PTP-BL and RIL in epithelial cells. Remarkably, there is also an N-terminal PDZ motif in RIL itself that can bind to the RIL-LIM domain. We demonstrate here that the RIL-LIM domain can be phosphorylated on tyrosine in vitro and in vivo and can be dephosphorylated in vitro by the PTPase domain of PTP-BL. Our data point to the presence of a double PDZ-binding interface on the RIL-LIM domain and suggest tyrosine phosphorylation as a regulatory mechanism for LIM-PDZ associations in the assembly of multiprotein complexes. These findings are in line with an important role of PDZ-mediated interactions in the shaping and organization of submembranous microenvironments of polarized cells. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| تدمد: | 1059-1524 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10f3b4bcc767c91c21e5a45f0aeac542 https://doi.org/10.1091/mbc.9.3.671 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....10f3b4bcc767c91c21e5a45f0aeac542 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10591524 |
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