Dynamics of Myosin II Filaments during Wound Repair in Dividing Cells

Cells

Hiroyuki Adachi¹  Go Itoh²  Shigehiko Yumura³  Md.Istiaq Obaidi Tanvir³ 

[1] Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan;Department of Molecular Medicine and Biochemistry, Akita University Graduate School of Medicine, Akita 010-8543, Japan;Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, Japan;

关键词: actin;    cell membrane;    cleavage furrow;    laserporation;    myosin;    wound repair;   

DOI  :  10.3390/cells10051229

来源: DOAJ

【 摘 要 】

Wound repair of cell membranes is essential for cell survival. Myosin II contributes to wound pore closure by interacting with actin filaments in larger cells; however, its role in smaller cells is unclear. In this study, we observed wound repair in dividing cells for the first time. The cell membrane in the cleavage furrow, where myosin II localized, was wounded by laserporation. Upon wounding, actin transiently accumulated, and myosin II transiently disappeared from the wound site. Ca²⁺ influx from the external medium triggered both actin and myosin II dynamics. Inhibition of calmodulin reduced both actin and myosin II dynamics. The wound closure time in myosin II-null cells was the same as that in wild-type cells, suggesting that myosin II is not essential for wound repair. We also found that disassembly of myosin II filaments by phosphorylation did not contribute to their disappearance, indicating a novel mechanism for myosin II delocalization from the cortex. Furthermore, we observed that several furrow-localizing proteins such as GAPA, PakA, myosin heavy chain kinase C, PTEN, and dynamin disappeared upon wounding. Herein, we discuss the possible mechanisms of myosin dynamics during wound repair.

【 授权许可】

Unknown