The LIN-2/LIN-7/LIN-10 complex mediates basolateral membrane localization of the C. elegans EGF receptor LET-23 in vulval epithelial cells
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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.
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Both CASK and its C. elegans homolog Lin-2 form a tripartite complex with Velis and Mints.
“Both CASK and its C. elegans homolog Lin-2 form a tripartite complex with two other PDZ-domain proteins called Velis (also named MALS, originally discovered in C. elegans as Lin-7) and Mints (also called Lin-10; Butz et al., 1998; Kaech et al., 1998).”
From The Presynaptic Active Zone (2012) · cites this paper as Kaech et al., 1998
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References 42 · Cited by 375
- Authors
- Kaech, S. M., Whitfield, C. W., & Kim, S. K.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Kim, Stuart K
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1998-09
- Volume
- 94
- Issue
- 6
- Pages
- 761-771
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC3224769
- OpenAlex
- W2015889211
- Cited by
- 375
- References
- 42
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 6 · 2023: 2 · 2022: 6 · 2021: 13 · 2020: 7 · 2019: 1 · 2018: 8 · 2017: 5 · 2016: 7 · 2015: 5 · 2014: 5 · 2013: 7 · 2012: 10
- FWCI
- 12.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cell (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM043977)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- LET-23, EGF receptor tyrosine kinase, basolateral membrane localization, receptor trafficking, protein complexes, allele-specific suppression, compensatory mutations, Caenorhabditis elegans
- MeSH terms
- Animals, Drosophila, Epithelial Cells, Female, Mammals, Membrane Proteins, Multienzyme Complexes, Mutation, Precipitin Tests, Protein Binding, Proteins, Substrate Specificity, Vulva, Yeasts, Signal Transduction, Helminth Proteins, Gene Expression Regulation, Enzymologic, Caenorhabditis elegans, Protein Structure, Tertiary, Caenorhabditis elegans Proteins, ErbB Receptors
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