Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-10-13
pubmed:abstractText
In C. elegans, the LET-23 receptor tyrosine kinase is localized to the basolateral membranes of polarized vulval epithelial cells. lin-2, lin-7, and lin-10 are required for basolateral localization of LET-23, since LET-23 is mislocalized to the apical membrane in lin-2, lin-7, and lin-10 mutants. Yeast two-hybrid, in vitro binding, and in vivo coimmunoprecipitation experiments show that LIN-2, LIN-7, and LIN-10 form a protein complex. Furthermore, compensatory mutations in lin-7 and let-23 exhibit allele-specific suppression of apical mislocalization and signaling-defective phenotypes. These results present a mechanism for basolateral localization of LET-23 receptor tyrosine kinase by direct binding to the LIN-2/LIN-7/LIN-10 complex. Each of the binding interactions within this complex is conserved, suggesting that this complex may also mediate basolateral localization in mammals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
761-71
pubmed:dateRevised
2011-9-22
pubmed:meshHeading
pubmed-meshheading:9753323-Animals, pubmed-meshheading:9753323-Caenorhabditis elegans, pubmed-meshheading:9753323-Caenorhabditis elegans Proteins, pubmed-meshheading:9753323-Drosophila, pubmed-meshheading:9753323-Epithelial Cells, pubmed-meshheading:9753323-Female, pubmed-meshheading:9753323-Gene Expression Regulation, Enzymologic, pubmed-meshheading:9753323-Helminth Proteins, pubmed-meshheading:9753323-Mammals, pubmed-meshheading:9753323-Membrane Proteins, pubmed-meshheading:9753323-Multienzyme Complexes, pubmed-meshheading:9753323-Mutation, pubmed-meshheading:9753323-Precipitin Tests, pubmed-meshheading:9753323-Protein Binding, pubmed-meshheading:9753323-Protein Structure, Tertiary, pubmed-meshheading:9753323-Proteins, pubmed-meshheading:9753323-Receptor, Epidermal Growth Factor, pubmed-meshheading:9753323-Signal Transduction, pubmed-meshheading:9753323-Substrate Specificity, pubmed-meshheading:9753323-Vulva, pubmed-meshheading:9753323-Yeasts
pubmed:year
1998
pubmed:articleTitle
The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells.
pubmed:affiliation
Department of Developmental Biology, Stanford University School of Medicine, California 94305, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.