ArticleThe Journal of cell biology1997
LI-cadherin-mediated cell-cell adhesion does not require cytoplasmic interactions.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 87 citations in OpenAlex.
- A Novel Anti-Cadherin-17 Monoclonal Antibody, CaAntibodies (Basel, Switzerland) · 2026Article
- Cadherin 17 and digestive cancers: from diagnostic to therapeutic opportunities.Journal of experimental & clinical cancer research : CR · 2026Review
- Antibody-drug conjugates targeting the cadherin, claudin and nectin families of adhesion molecules.Frontiers in molecular medicine · 2025Review
- Cadherin-17 as a target for the immunoPET of adenocarcinoma.European journal of nuclear medicine and molecular imaging · 2024Article
- A proximity labeling method for protein-protein interactions on cell membrane.Chemical science · 2022Article
- Mechanism of dimerization and structural features of human LI-cadherin.The Journal of biological chemistry · 2021Article
- Crystal structure of the nonclassical cadherin-17 N-terminus and implications for its adhesive binding mechanism.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Beyond N-Cadherin, Relevance of Cadherins 5, 6 and 17 in Cancer Progression and Metastasis.International journal of molecular sciences · 2019Review
- Physiological relevance of epithelial geometry: New insights into the standing gradient model and the role of LI cadherin.PloS one · 2018Article
- Water transport through the intestinal epithelial barrier under different osmotic conditions is dependent on LI-cadherin trans-interaction.Tissue barriers · 2017Article
- Expression of Tight Junction Proteins and Cadherin 17 in the Small Intestine of Young Goats Offered a Reduced N and/or Ca Diet.PloS one · 2016Article
- Clinicopathologic and molecular characteristics of gastric cancer showing gastric and intestinal mucin phenotype.Cancer science · 2015Review
- Cadherin 17 is a sensitive and specific marker for metanephric adenoma.The American journal of surgical pathology · 2015Article
- A comparative study of PKH67, DiI, and BrdU labeling techniques for tracing rat mesenchymal stem cells.In vitro cellular & developmental biology. Animal · 2014Article
- Article
- Involvement of liver-intestine cadherin in cancer progression.Medical molecular morphology · 2013Review
- Possible roles of LI-Cadherin in the formation and maintenance of the intestinal epithelial barrier.Tissue barriers · 2013Review
- Single nucleotide polymorphisms in the CDH17 gene of colorectal carcinoma.World journal of gastroenterology · 2012Article
- LI-cadherin cis-dimerizes in the plasma membrane Ca(2+) independently and forms highly dynamic trans-contacts.Cellular and molecular life sciences : CMLS · 2012Article
- Knockdown of liver-intestine cadherin decreases BGC823 cell invasiveness and metastasis in vivo.World journal of gastroenterology · 2012Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The adhesive function of classical cadherins depends on the association with cytoplasmic proteins, termed catenins, which serve as a link between cadherins and the actin cytoskeleton. LI-cadherin, a structurally different member of the cadherin family, mediates Ca2+-dependent cell-cell adhesion, although its markedly short cytoplasmic domain exhibits no homology to this highly conserved region of classical cadherins. We now examined whether the adhesive function of LI-cadherin depends on the interaction with catenins, the actin cytoskeleton or other cytoplasmic components. In contrast to classical cadherins, LI-cadherin, when expressed in mouse L cells, was neither associated with catenins nor did it induce an upregulation of beta-catenin. Consistent with these findings, LI-cadherin was not resistant to detergent extraction and did not induce a reorganization of the actin cytoskeleton. However, LI-cadherin was still able to mediate Ca2+-dependent cell-cell adhesion. To analyze whether this function requires any interaction with proteins other than catenins, a glycosyl phosphatidylinositol-anchored form of LI-cadherin (LI-cadherin(GPI)) was constructed and expressed in Drosophila S2 cells. The mutant protein was able to induce Ca2+-dependent, homophilic cell-cell adhesion, and its adhesive properties were indistinguishable from those of wild type LI-cadherin. These findings indicate that the adhesive function of LI-cadherin is independent of any interaction with cytoplasmic components, and consequently should not be sensitive to regulatory mechanisms affecting the binding of classical cadherins to catenins and to the cytoskeleton. Thus, we postulate that the adhesive function of LI-cadherin is complementary to that of coexpressed classical cadherins ensuring cell-cell contacts even under conditions that downregulate the function of classical cadherins.
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