ArticleJournal of microbiology (Seoul, Korea)2017
Loss of FrmB results in increased size of developmental structures during the multicellular development of Dictyostelium cells.
Article in Journal of microbiology (Seoul, Korea), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Nhe1 is required for directional sensing in vegetativeCell adhesion & migration · 2025Article
- The IQGAP-related RasGAP IqgC regulates cell-substratum adhesion in Dictyostelium discoideum.Cellular & molecular biology letters · 2025Article
- Adhesion ofFrontiers in cell and developmental biology · 2022Review
- Opposite functions of RapA and RapC in cell adhesion and migration inAnimal cells and systems · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
FERM domain-containing proteins are involved in diverse biological and pathological processes, including cell-substrate adhesion, cell-cell adhesion, multicellular development, and cancer metastasis. In this study, we determined the functions of FrmB, a FERM domain-containing protein, in the cell morphology, cell adhesion, and multicellular development of Dictyostelium cells. Our results show that FrmB appears to play an important role in regulating the size of developmental structures. frmB null cells showed prolonged aggregation during development, resulting in increased size of developmental structures, such as mounds and fruiting bodies, compared to those of wild-type cells, whereas FrmB overexpressing cells exhibited decreased size of developmental structures. These results suggest that FrmB may be necessary for limiting the sizes of developmental structures. Loss of FrmB also resulted in decreased cell-substrate adhesion and slightly increased cell area, suggesting that FrmB had important roles in the regulation of cell adhesion and cell morphology. These studies would contribute to our understanding of the intertwined and overlapped functions of FERM domain-containing proteins.
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