- Loss of FrmB results in increased size of developmental structures during the multicellular development of Dictyostelium cells
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Hyeseon Kim , Mi-Rae Lee , Taeck Joong Jeon
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J. Microbiol. 2017;55(9):730-736. Published online September 2, 2017
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DOI: https://doi.org/10.1007/s12275-017-7221-x
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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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Citations
Citations to this article as recorded by  - The IQGAP-related RasGAP IqgC regulates cell–substratum adhesion in Dictyostelium discoideum
Lucija Mijanović, Darija Putar, Lucija Mimica, Sabina Klajn, Vedrana Filić, Igor Weber
Cellular & Molecular Biology Letters.2025;[Epub] CrossRef -
Nhe1 is required for directional sensing in vegetative
Dictyostelium
cell migration
Uri Han, Nara Han, Taeck Joong Jeon
Cell Adhesion & Migration.2025;[Epub] CrossRef - Adhesion of Dictyostelium Amoebae to Surfaces: A Brief History of Attachments
Lucija Mijanović, Igor Weber
Frontiers in Cell and Developmental Biology.2022;[Epub] CrossRef - Opposite functions of RapA and RapC in cell adhesion and migration in Dictyostelium
Jihyeon Jeon, Dongju Kim, Taeck Joong Jeon
Animal Cells and Systems.2021; 25(4): 203. CrossRef
- Minimal amino acids in the I/LWEQ domain required for anterior/posterior localization in Dictyostelium
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Hyeseon Kim , Dong-Yeop Shin , Taeck Joong Jeon
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J. Microbiol. 2017;55(5):366-372. Published online January 26, 2017
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DOI: https://doi.org/10.1007/s12275-017-6550-0
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Abstract
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Establishment of cell polarity is mediated by a series of signal-ing molecules that are asymmetrically activated or localized in the cell upon extracellular stimulation. To understand the mechanism that mediates anterior/posterior asymmetric localization of RapGAP3 during migration, we determined the minimally required amino acids in the I/LWEQ domain that cause posterior localization and found that the minimal region of the F-actin binding domain for posterior localiza-tion could, with some additional deletion at the C-terminal, localize to the anterior. Analysis of the localization and trans-location kinetics to the cell cortex of the truncated proteins suggests that the required regions for anterior/posterior lo-calization might have a preferential binding affinity to pre- existing F-actins at the rear and lateral sides of the cell or newly formed F-actins at the front of the cell, leading to dis-tinct differential sites of the cell.
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