Loss of FrmB results in increased size of developmental structures during the multicellular development of Dictyostelium cells

• Published in: The journal of microbiology Vol. 55; no. 9; pp. 730 - 736
• Main Authors: Kim, Hyeseon, Lee, Mi-Rae, Jeon, Taeck Joong
• Format: Journal Article
• Language: English
• Published: Seoul The Microbiological Society of Korea 01.09.2017; Springer Nature B.V; 한국미생물학회
• Subjects: Adhesion; Agglomeration; Aggregation; Animals; Biological activity; Biomedical and Life Sciences; Cancer; Cell Adhesion; Cell adhesion & migration; Cell morphology; Cytology; Dictyostelium - cytology; Dictyostelium - genetics; Dictyostelium - growth & development; Dictyostelium - physiology; Fruit bodies; Life Sciences; Metastases; Microbiology; Morphology; Mounds; Null cells; Proteins; Protozoan Proteins - genetics; Protozoan Proteins - physiology; Sequence Homology, Amino Acid; Structures; 생물학; FrmB; FERM domain-containing protein; development; Dictyostelium
• ISSN: 1225-8873; 1976-3794
• DOI: 10.1007/s12275-017-7221-x

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.