ArticleThe Journal of cell biology1994
Replacement of the phospholipid-anchor in the contact site A glycoprotein of D. discoideum by a transmembrane region does not impede cell adhesion but reduces residence time on the cell surface.
Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 36 citations in OpenAlex.
- Species recognition in social amoebae.Journal of biosciences · 2018Article
- Genetic control of morphogenesis in Dictyostelium.Developmental biology · 2015Review
- Dynamics of clathrin-mediated endocytosis and its requirement for organelle biogenesis in Dictyostelium.Journal of cell science · 2012Article
- Adhesion-induced receptor segregation and adhesion plaque formation: A model membrane study.Biophysical journal · 1999Article
- An uncleaved glycosylphosphatidylinositol signal mediates Ca(2+)-sensitive protein degradation.The Biochemical journal · 1996Article
- Targeted disruption of genes for gp138, a cell-fusion-related protein in Dictyostelium discoideum, revealed the existence of a third gene.Development, growth & differentiation · 1996Article
- Ordered yeast artificial chromosome clones representing the Dictyostelium discoideum genome.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Replacement of the glycoinositol phospholipid anchor of Drosophila acetylcholinesterase with a transmembrane domain does not alter sorting in neurons and epithelia but results in behavioral defects.Molecular biology of the cell · 1996Article
- Cell adhesion in the life cycle of Dictyostelium.Experientia · 1995Review
- A talin homologue of Dictyostelium rapidly assembles at the leading edge of cells in response to chemoattractant.The Journal of cell biology · 1995Article
- Lack of glycosyl-phosphatidylinositol anchoring leads to precursor retention by a unique mechanism in Dictyostelium discoideum.The Biochemical journal · 1995Article
- Ponticulin is an atypical membrane protein.The Journal of cell biology · 1994Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The contact site A (csA) glycoprotein of Dictyostelium discoideum, a cell adhesion molecule expressed in aggregating cells, is inserted into the plasma membrane by a ceramide-based phospholipid (PL) anchor. A carboxyterminal sequence of 25 amino acids of the primary csA translation product proved to contain the signal required for PL modification. CsA is known to be responsible for rapid, EDTA-resistant cohesion of cells in agitated suspensions. To investigate the role of the PL modification of this protein, the anchor was replaced by the transmembrane region and short cytoplasmic tail of another plasma membrane protein of D. discoideum. In cells transformed with appropriate vectors, PL-anchored or transmembrane csA was expressed under the control of an actin promoter during growth and development. The transmembrane form enabled the cells to agglutinate in the presence of shear forces, similar to the PL-anchored wild-type form. However, the transmembrane form was much more rapidly internalized and degraded. In comparison to other cell-surface glycoproteins of D. discoideum the internalization rate of the PL-anchored csA was extremely slow, most likely because of its exclusion from the clathrin-mediated pathway of pinocytosis. Thus, our results indicate that the phospholipid modification is not essential for the csA-mediated fast type of cell adhesion but guarantees long persistence of the protein on the cell surface.
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