Interaction of the ERC family of RIM-binding proteins with the liprin-alpha family of multidomain proteins.
Liprin-alpha/SYD-2 is a family of multidomain proteins with four known isoforms. One of the reported functions of liprin-alpha is to regulate the development of presynaptic active zones, but the underlying mechanism is poorly understood. Here we report that liprin-alpha directly interacts with the ERC (ELKS-Rab6-interacting protein-CAST) family of proteins, members ... of which are known to bind RIMs, the active zone proteins that regulate neurotransmitter release. In vitro results indicate that ERC2/CAST, an active zone-specific isoform, interacts with all of the known isoforms of liprin-alpha and that liprin-alpha1 associates with both ERC2 and ERC1b, a splice variant of ERC1 that distributes to both cytosolic and active zone regions. ERC2 colocalizes with liprin-alpha1 in cultured neurons and forms a complex with liprin-alpha1 in brain. Liprin-alpha1, when expressed alone in cultured neurons, shows a partial synaptic localization. When coexpressed with ERC2, however, liprin-alpha1 is redistributed to synaptic sites. Moreover, roughly the first half of ERC2, which contains the liprin-alpha-binding region, is sufficient for the synaptic localization of liprin-alpha1 while the second half is not. These results suggest that the interaction between ERC2 and liprin-alpha may be involved in the presynaptic localization of liprin-alpha and the molecular organization of presynaptic active zones.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Animals, Brain Chemistry, Carrier Proteins, Embryo, Mammalian, Hippocampus, Humans, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Phosphoproteins, Protein Binding, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Proto-Oncogene Proteins, Rats, Synapses, Two-Hybrid System Techniques
Adaptor Proteins, Signal Transducing, Animals, Brain Chemistry, Carrier Proteins, Embryo, Mammalian, Hippocampus, Humans, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Phosphoproteins, Protein Binding, Protein Isoforms, Protein Structure, Tertiary, Protein Transport, Proto-Oncogene Proteins, Rats, Synapses, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Oct. 24, 2003
PubMed ID: 12923177
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