ArticleDevelopmental biology2015
Absence of catalytic domain in a putative protein kinase C (PkcA) suppresses tip dominance in Dictyostelium discoideum.
Article in Developmental biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Two endogenousProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamics of Actin Cytoskeleton and Their Signaling Pathways during Cellular Wound Repair.Cells · 2022Article
- Article
- A telomerase with novel non-canonical roles: TERT controls cellular aggregation and tissue size in Dictyostelium.PLoS genetics · 2019Article
- An endogenous chemorepellent directs cell movement by inhibiting pseudopods at one side of cells.Molecular biology of the cell · 2019Article
- Functional interaction of PkcA and PldB regulate aggregation and development in Dictyostelium discoideum.Cellular signalling · 2017Article
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Authors and funding
4 authors.
Funding
Abstract
A number of organisms possess several isoforms of protein kinase C but little is known about the significance of any specific isoform during embryogenesis and development. To address this we characterized a PKC ortholog (PkcA; DDB_G0288147) in Dictyostelium discoideum. pkcA expression switches from prestalk in mound to prespore in slug, indicating a dynamic expression pattern. Mutants lacking the catalytic domain of PkcA (pkcA(-)) did not exhibit tip dominance. A striking phenotype of pkcA- was the formation of an aggregate with a central hollow, and aggregates later fragmented to form small mounds, each becoming a fruiting body. Optical density wave patterns of cAMP in the late aggregates showed several cAMP wave generation centers. We attribute these defects in pkcA(-) to impaired cAMP signaling, altered cell motility and decreased expression of the cell adhesion molecules - CadA and CsaA. pkcA(-) slugs showed ectopic expression of ecmA in the prespore region. Further, the use of a PKC-specific inhibitor, GF109203X that inhibits the activity of catalytic domain phenocopied pkcA(-).
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