Distinct LIN-10 Domains Are Required for Its Neuronal Function, Its Epithelial Function, and Its Synaptic Localization

  • Doreen R. Glodowski
    The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
  • Tricia Wright
    The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
  • Keri Martinowich
    The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
  • Howard Chia-Hao Chang
    The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
  • Douglas Beach
    The Waksman Institute, Department of Genetics, Rutgers University, Piscataway, NJ 08854
  • 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>

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詳細情報 詳細情報について

  • CRID
    1361418521463330816
  • NII論文ID
    30018379773
  • DOI
    10.1091/mbc.e04-10-0885
  • ISSN
    19394586
    10591524
  • データソース種別
    • Crossref
    • CiNii Articles

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