ArticleThe Biochemical journal2003
Different binding motifs in metabotropic glutamate receptor type 7b for filamin A, protein phosphatase 1C, protein interacting with protein kinase C (PICK) 1 and syntenin allow the formation of multimeric protein complexes.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 62 citations in OpenAlex.
- Ubiquitination of Metabotropic Glutamate Receptors and Associated Synaptic ProteinsJournal of cellular signaling · 2025Article
- Biological Role and Aberrant Overexpression of Syntenin-1 in Cancer: Potential Role as a Biomarker and Therapeutic Target.Biomedicines · 2023Review
- Review
- Residue-Level Contact Reveals Modular Domain Interactions of PICK1 Are Driven by Both Electrostatic and Hydrophobic Forces.Frontiers in molecular biosciences · 2020Article
- Syntenin: PDZ Protein Regulating Signaling Pathways and Cellular Functions.International journal of molecular sciences · 2019Review
- Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018Review
- G protein-coupled receptors directly bind filamin A with high affinity and promote filamin phosphorylation.Biochemistry · 2015Article
- Targeting tumor invasion: the roles of MDA-9/Syntenin.Expert opinion on therapeutic targets · 2015Review
- Schistosome syntenin partially protects vaccinated mice against Schistosoma mansoni infection.PLoS neglected tropical diseases · 2014Article
- Regulation of metabotropic glutamate receptor 7 (mGluR7) internalization and surface expression by Ser/Thr protein phosphatase 1.The Journal of biological chemistry · 2013Article
- Expression patterns of MDA-9/syntenin during development of the mouse embryo.Journal of molecular histology · 2013Article
- Structure of metabotropic glutamate receptor C-terminal domains in contact with interacting proteins.Frontiers in molecular neuroscience · 2012Article
- Metabotropic glutamate receptors: from the workbench to the bedside.Neuropharmacology · 2011Review
- PDZ binding to the BAR domain of PICK1 is elucidated by coarse-grained molecular dynamics.Journal of molecular biology · 2011Article
- Article
- Filamin A mutant lacking actin-binding domain restores mu opioid receptor regulation in melanoma cells.Neurochemical research · 2008Article
- Knock-in mice lacking the PDZ-ligand motif of mGluR7a show impaired PKC-dependent autoinhibition of glutamate release, spatial working memory deficits, and increased susceptibility to pentylenetetrazol.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Article
- Target-cell-dependent plasticity within the mossy fibre-CA3 circuit reveals compartmentalized regulation of presynaptic function at divergent release sites.The Journal of physiology · 2008Review
- Cooperative regulation of extracellular signal-regulated kinase activation and cell shape change by filamin A and beta-arrestins.Molecular and cellular biology · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metabotropic glutamate receptor (mGluR) type 7-mediated neurotransmission depends critically on its regulation by associated molecules, such as kinases, phosphatases and structural proteins. The splice variants mGluR7a and mGluR7b are defined by different intracellular C-termini, and simultaneous or exclusive binding of interacting proteins to these domains modulates mGluR7-mediated signalling. However, molecular determinants defining binding regions for associated proteins within mGluR7 C-termini are mostly unknown. In the present study, we have mapped the binding domains of four proteins [filamin A, protein phosphatase (PP) 1C, protein interacting with protein kinase C (PICK) 1 and syntenin] interacting with the mGluR7b variant, and show that the alternatively spliced distal part of the mGluR7b C-terminus was sufficient for the interactions. By individual substitution of all mGluR7b isoform-specific amino acids with alanine and construction of a series of deletion constructs, residues important for the interactions were identified and binding regions could be defined. Interestingly, mGluR7b contains an unusual PP1C-binding motif, located at the N-terminus of the binding domains for PICK1 and syntenin. Consistently, binding of PP1C and PICK1 or PP1C and syntenin to mGluR7b was not competitive. Furthermore, PICK1, but not PP1C, interacted physically with syntenin. Our results represent a molecular description of the binding mechanisms of four mGluR7-associated proteins, and indicate the formation of ternary protein complexes composed of mGluR7b, PP1C, PICK1 and syntenin.
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