ArticleEukaryotic cell2002
Loss of the F-actin binding and vesicle-associated protein comitin leads to a phagocytosis defect.
Article in Eukaryotic cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 24 citations in OpenAlex.
- Investigation of the host transcriptional response to intracellular bacterial infection using Dictyostelium discoideum as a host model.BMC genomics · 2019Article
- Ectopic expression of cyclase associated protein CAP restores the streaming and aggregation defects of adenylyl cyclase a deficient Dictyostelium discoideum cells.BMC developmental biology · 2012Article
- The professional phagocyte Dictyostelium discoideum as a model host for bacterial pathogens.Current drug targets · 2011Review
- RpkA, a highly conserved GPCR with a lipid kinase domain, has a role in phagocytosis and anti-bacterial defense.PloS one · 2011Article
- Comparative genomics of the social amoebae Dictyostelium discoideum and Dictyostelium purpureum.Genome biology · 2011Article
- A cytohesin homolog in Dictyostelium amoebae.PloS one · 2010Article
- A Rab21/LIM-only/CH-LIM complex regulates phagocytosis via both activating and inhibitory mechanisms.The EMBO journal · 2005Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Comitin is an F-actin binding and membrane-associated protein from Dictyostelium discoideum, which is present on Golgi and vesicle membranes and changes its localization in response to agents affecting the cytoskeleton. To investigate its in vivo functions we have generated knockout mutants by gene replacement. Based on comitin's in vitro functions we examined properties related to vesicular transport and microfilament function. Whereas cell growth, pinocytosis, secretion, chemotaxis, motility, and development were unaltered, comitin-lacking cells were impaired in the early steps of phagocytosis of Saccharomyces cerevisiae particles and of Escherichia coli, whereas uptake of latex beads was unaffected. Furthermore, the lack of comitin positively affected survival of pathogenic bacteria. Mutant cells also showed an altered response to hyperosmotic shock in comparison to the wild type. The redistribution of comitin during hyperosmotic shock in wild-type cells and its presence on early phagosomes suggest a direct involvement of comitin in these processes.
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Registered trials
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