ArticleMolecular biology of the cell1998
PDZ motifs in PTP-BL and RIL bind to internal protein segments in the LIM domain protein RIL.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 135 citations in OpenAlex.
- PDLIM4 promotes dephosphorylation of STAT transcription factors by recruiting PTP-BL and inhibits Th1, Th2, and Th17 cell differentiation.International immunology · 2026Article
- Autoregulation of the LIM kinases by their PDZ domain.Nature communications · 2023Article
- The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022Review
- Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer.Biomolecules · 2020Review
- Specificity in PDZ-peptide interaction networks: Computational analysis and review.Journal of structural biology: X · 2020Review
- Understanding the effect of alternative splicing in the folding and function of the second PDZ from protein tyrosine phosphatase-BL.Scientific reports · 2015Article
- Characterization of diverse internal binding specificities of PDZ domains by yeast two-hybrid screening of a special peptide library.PloS one · 2014Article
- Actin cytoskeleton remodeling by the alternatively spliced isoform of PDLIM4/RIL protein.The Journal of biological chemistry · 2011Article
- PTPN13/PTPL1: an important regulator of tumor aggressiveness.Anti-cancer agents in medicinal chemistry · 2011Review
- Genetics and pathological mechanisms of Usher syndrome.Journal of human genetics · 2010Review
- Sequence requirement and subtype specificity in the high-affinity interaction between human frizzled and dishevelled proteins.Protein science : a publication of the Protein Society · 2009Article
- Reversion-induced LIM interaction with Src reveals a novel Src inactivation cycle.The Journal of cell biology · 2009Article
- Localization of reversion-induced LIM protein (RIL) in the rat central nervous system.Acta histochemica et cytochemica · 2009Article
- Domain swapping within PDZ2 is responsible for dimerization of ZO proteins.The Journal of biological chemistry · 2007Article
- PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration.The Journal of biological chemistry · 2007Article
- Subcellular localization and differentiation-induced redistribution of the protein tyrosine phosphatase PTP-BL in Neuroblastoma cells.Cellular and molecular neurobiology · 2005Article
- NHERF family and NHE3 regulation.The Journal of physiology · 2005Review
- Mystique is a new insulin-like growth factor-I-regulated PDZ-LIM domain protein that promotes cell attachment and migration and suppresses Anchorage-independent growth.Molecular biology of the cell · 2005Article
- The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus.BMC cell biology · 2005Article
- The interaction of PTP-BL PDZ domains with RIL: an enigmatic role for the RIL LIM domain.Molecular biology reports · 2004Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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