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Vol. 10, Issue 6, 2087-2100, June 1999
and
*Department of Developmental Biology, Stanford University Medical
Center, Stanford, California 94305; and In Caenorhabditis elegans, the EGF receptor (encoded
by let-23) is localized to the basolateral membrane
domain of the epithelial vulval precursor cells, where it acts through
a conserved Ras/MAP kinase signaling pathway to induce vulval
differentiation. lin-10 acts in LET-23 receptor tyrosine
kinase basolateral localization, because lin-10
mutations result in mislocalization of LET-23 to the apical membrane
domain and cause a signaling defective (vulvaless) phenotype. We
demonstrate that the previous molecular identification of
lin-10 was incorrect, and we identify a new gene
corresponding to the lin-10 genetic locus.
lin-10 encodes a protein with regions of similarity to
mammalian X11/mint proteins, containing a phosphotyrosine-binding and
two PDZ domains. A nonsense lin-10 allele that truncates
both PDZ domains only partially reduces lin-10 gene
activity, suggesting that these protein interaction domains are not
essential for LIN-10 function in vulval induction. Immunocytochemical
experiments show that LIN-10 is expressed in vulval epithelial cells
and in neurons. LIN-10 is present at low levels in the cytoplasm and at
the plasma membrane and at high levels at or near the Golgi. LIN-10 may
function in secretion of LET-23 to the basolateral membrane domain, or it may be involved in tethering LET-23 at the basolateral plasma membrane once it is secreted.
Department of
Biology, McGill University, Montreal, Quebec, Canada
Corresponding author. E-mail
address: kim{at}cmgm.stanford.edu
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