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Rongo, C. et al.

LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia.

We tested the model that neurons and epithelial cells use a shared mechanism for polarized protein sorting by comparing the pathways for localizing basolateral and postsynaptic proteins in C. elegans. GLR-1 glutamate receptors are localized to postsynaptic elements of central synapses and, when ectopically expressed, to basolateral membranes of epithelial cells. Proper localization of GLR-1 in both neurons and epithelia requires the PDZ protein LIN-10, defining LIN-10 as a shared component of the basolateral and postsynaptic localization pathways. Changing the GLR-1 carboxy-terminal sequence from a group I PDZ-binding consensus (-TAV) to a group II consensus (-FYV) restores GLR-1 synaptic localization in lin-10 mutants. Thus, these interneurons utilize at least two separate postsynaptic localization pathways.[1]

References

LIN-10 is a shared component of the polarized protein localization pathways in neurons and epithelia. Rongo, C., Whitfield, C.W., Rodal, A., Kim, S.K., Kaplan, J.M. Cell (1998) [Pubmed]

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