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    Literature Review: Cadherin-mediated cell-cell adhesion.

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    Review of the article titled "Transmembrane control of cadherin-mediated cell adhesion: a 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin." The review includes a short description of what cadherins are, what they do, and how they function with the actin-cytoskeleton, including information about the C-terminal domains. Information is provided specifically on the properties of E-cadherin. This remaining information includes a summary of experimental methods used by the authors of this study. Mutant E-cadherin ELβ20, dissociation/aggregation assay in the presence of Ca2+, immunoprecipitation of E-cadherin, and electrophoretic analysis are methods used by the authors to identify the active domain of E-cadherin.

    Abstract for article:
    "Cadherins are a family of transmembrane glycoproteins which play a key role in Ca(2+)-dependent cell-cell adhesion. Cytoplasmic domains of these molecules are anchored to the cell cytoskeleton and are required for cadherin function. To elucidate how the function of cadherins is controlled through their cytoplasmic domains, we deleted five different regions in the cytoplasmic domain of E-cadherin. After transfecting L cells with cDNA encoding the mutant polypeptides, we assayed aggregating activity of these transfectants; all these mutant proteins were shown to have an extracellular domain with normal Ca(2+)-sensitivity and molecular weight. Two mutant polypeptides with deletions in the carboxy half of the cytoplasmic domain, however, did not promote cell-cell adhesion and had also lost the ability to bind to the cytoskeleton, whereas the mutant molecules with deletions of other regions retained the ability to promote cell adhesion and to anchor to the cytoskeleton. Thus, the cytoplasmic domain contains a subdomain which was involved in the cell adhesion and cytoskeleton-binding functions. When E-cadherin in F9 cells or in L cells transfected with wild-type or functional mutant cadherin polypeptides was solubilized with nonionic detergents and immunoprecipitated, two additional 94 and 102 kDa components were coprecipitated. The 94 kDa component, however, was not detected in the immunoprecipitates from cells expressing the mutant cadherins which had lost the adhesive function. These results suggest that the interaction of the carboxy half of the cytoplasmic domain with the 94 kDa component regulates the cell binding function of the extracellular domain of E-cadherin."

    Full text can be located at: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=361423.

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    Solution Preview

    See the attached file.

    Transmembrane control of cadherin-mediated cell
    adhesion: a 94 kDa protein functionally associated with
    a specific region of the cytoplasmic domain
    of E-cadherin
    Full article text can be located at: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=361423

    Cadherins are a class of transmembrane proteins, responsible for Ca2+ mediated cell adhesion. Soluble and insoluble classes of cadherins exist, and insoluble protein populations are known to anchor to actin cytoskeletal elements. It is currently accepted that classes of cadherins mediate cell-cell interactions via binding to actin-cytoskeletal elements, and that the cadherin binding site is located on the C-terminus and cytoplasmic domain of these proteins. Evidence for this belief is demonstrated by the subclass of E-cadherins in the cadherin family.

    E-cadherins contain a highly conserved C-terminal end, and when mutated, E-cadherin can no longer function to bind cytoskeletal elements and mediate cell-cell interactions. It has been further documented that additional proteins can be co-precipitated with the soluble or ...

    Solution Summary

    The solution writes a literature review on cadherin-mediated cell-cell adhesion.