Cell Structure and Function | |
Localization of Type I Myosin and F-actin to the Leading Edge Region of the Forespore Membrane in Schizosaccharomyces pombe | |
Chikashi Shimoda1  Taro Nakamura1  Akiko Itadani1  | |
[1] Department of Biology, Graduate School of Science, Osaka City University | |
关键词: calmodulin; F-actin; forespore membrane; leading edge; myosin-I; | |
DOI : 10.1247/csf.06027 | |
学科分类:分子生物学,细胞生物学和基因 | |
来源: Japan Society for Cell Biology | |
【 摘 要 】
References(45)Cited-By(4)Myo1, a heavy chain of type I myosin of the fission yeast Schizosaccharomyces pombe, is essential for sporulation. Here we have analyzed the expression, localization and cellular function of the type I myosin light chain calmodulin, Cam2, encoded by cam2+. Transcription of cam2+ was constitutive and markedly enhanced in meiosis. The cam2 null mutant was viable and completed sporulation normally at 28°C, but formed four-spored asci poorly at 34°C. In those sporulation-defective cells, the forespore membrane was formed abnormally. A Cam2-GFP fusion protein accumulated at the cell poles in interphase cells and at the medial septation site in postmitotic cells, colocalizing with Myo1 and F-actin patches. During the mating process, a single Cam2-GFP dot was detected at the tip of the mating projection. During meiosis-I, the Cam2-GFP dots dispersed into the cell periphery and the cytoplasm. At metaphase-II, intense Cam2-GFP signals appeared near Meu14 rings which were formed at the leading edge of expanding forespore membranes. This localization of Cam2 was dependent upon Myo1; and sporulation defect of cam2Δ at 34°C was alleviated by overexpressing Myo1ΔIQ. These results suggest a close relationship between Cam2 and Myo1. In addition, both F-actin and Myo1 localized with Cam2 in the leading edge region. In summary, type I myosin and F-actin accumulate at the leading edge area of the forespore membrane and may play a pivotal role in its assembly.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
---|---|---|---|
RO201912080705081ZK.pdf | 2458KB | download |