Distinct LIN-10 Domains Are Required for Its Neuronal Function, Its Epithelial Function, and Its Synaptic Localization
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- Doreen R. Glodowski
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
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- Tricia Wright
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
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- Keri Martinowich
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
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- Howard Chia-Hao Chang
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
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- Douglas Beach
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
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- Christopher Rongo
- The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
抄録
<jats:p>α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA)-type glutamate receptors (AMPARs) mediate excitatory neurotransmission at neuronal synapses, and their regulated localization plays a role in synaptic plasticity. In Caenorhabditis elegans, the PDZ and PTB domain-containing protein LIN-10 is required both for the synaptic localization of the AMPAR subunit GLR-1 and for vulval fate induction in epithelia. Here, we examine the role that different LIN-10 domains play in GLR-1 localization. We find that an amino-terminal region of LIN-10 directs LIN-10 protein localization to the Golgi and to synaptic clusters. In addition, mutations in the carboxyl-terminal PDZ domains prevent LIN-10 from regulating GLR-1 localization in neurons but do not prevent LIN-10 from functioning in the vulval epithelia. A mutation in the amino terminus prevents the protein from functioning in the vulval epithelia but does not prevent it from functioning to regulate GLR-1 localization in neurons. Finally, we show that human Mint2 can substitute for LIN-10 to facilitate GLR-1 localization in neurons and that the Mint2 amino terminus is critical for this function. Together, our data suggest that LIN-10 uses distinct modular domains for its functions in neurons and epithelial cells and that during evolution its vertebrate ortholog Mint2 has retained the ability to direct AMPAR localization in neurons.</jats:p>
収録刊行物
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- Molecular Biology of the Cell
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Molecular Biology of the Cell 16 (3), 1417-1426, 2005-03
American Society for Cell Biology (ASCB)
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詳細情報 詳細情報について
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- CRID
- 1361418521463330816
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- NII論文ID
- 30018379773
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- ISSN
- 19394586
- 10591524
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