2006
DOI: 10.1038/nsmb1162
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Solution structures of the adhesion molecule DdCAD-1 reveal new insights into Ca2+-dependent cell-cell adhesion

Abstract: DdCAD-1 is a novel Ca(2+)-dependent cell adhesion molecule that lacks a hydrophobic signal peptide and a transmembrane domain. DdCAD-1 is expressed by the social amoeba Dictyostelium discoideum at the onset of development. It is synthesized as a soluble protein and then transported to the plasma membrane by contractile vacuoles. Here we describe the novel features of the solution structures of Ca(2+)-free and Ca(2+)-bound monomeric DdCAD-1. DdCAD-1 contains two beta-sandwich domains, belonging to the betagamma… Show more

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Cited by 29 publications
(55 citation statements)
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“…The cell adhesion molecule DdCad-1 from D. discoideum is involved in cell-cell adhesion in a Ca 2ϩ -dependent manner via dimer formation through two ␤␥-crystallin domains (91). During its transport, the protein is internalized in vacuoles in a Ca 2ϩ -and conformation-dependent manner (92,93).…”
Section: ؉ Binding and Domain Stabilizationmentioning
confidence: 99%
“…The cell adhesion molecule DdCad-1 from D. discoideum is involved in cell-cell adhesion in a Ca 2ϩ -dependent manner via dimer formation through two ␤␥-crystallin domains (91). During its transport, the protein is internalized in vacuoles in a Ca 2ϩ -and conformation-dependent manner (92,93).…”
Section: ؉ Binding and Domain Stabilizationmentioning
confidence: 99%
“…Subcellular localization shows that DdCAD-1 was distributed in cytoplasm in the initial of development and is transferred to plasma membrane quickly within 3 h [3]. DdCAD-1 contains two domains, N-terminal domain has homophilic binding function, while C-terminal domain is responsible for tethering DdCAD-1 on cell membrane [4,5]. DdCAD-1 is transported to cell surface by contractile vacuoles [6], and time-lapse images show that some of DdCAD-1 is imported to contractile vacuoles by membrane invagination [7].…”
Section: Introductionmentioning
confidence: 99%
“…Rescue of cadA -phenotype by in vitro reconstitution of DdCAD-1 DdCAD-1 is synthesized as a soluble protein, which adheres to the cell surface via interaction with an as yet unidentified membrane anchoring protein (Lin et al, 2006). As this membrane anchoring protein is expected to be present in cadAcells, exogenously added DdCAD-1 should bind to cadA -cells.…”
Section: Dynamic Changes In the Temporal And Spatial Distribution Of mentioning
confidence: 99%
“…DdCAD-1 contains two distinct domains with -sandwich architecture. Whereas the N-terminal domain is involved in homophilic binding, the C-terminal domain tethers the protein to a membrane anchor (Lin et al, 2006). Studies on cadA -cells have implicated DdCAD-1 in cell sorting and cell-type proportioning (Wong et al, 2002).…”
Section: Introductionmentioning
confidence: 99%