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dc.contributor.authorZhang, Yanshu
dc.contributor.authorYoshida, Aiko
dc.contributor.authorSakai, Nobuaki
dc.contributor.authorUekusa, Yoshitsugu
dc.contributor.authorKumeta, Masahiro
dc.contributor.authorYoshimura, Shige H.
dc.contributor.alternative吉田, 藍子
dc.contributor.alternative粂田, 昌宏
dc.contributor.alternative吉村, 成弘
dc.date.accessioned2018-02-28T07:21:38Z-
dc.date.available2018-02-28T07:21:38Z-
dc.date.issued2017-08
dc.identifier.issn2050-5698
dc.identifier.urihttp://hdl.handle.net/2433/229445-
dc.description.abstractTogether with lamellipodia and stress fibers, a dynamic network of actin filaments in the cell cortex plays a major role in the maintenance of cell morphology and motility. In contrast to lamellipodia, which have been well studied in various motile cells, the dynamics of actin filaments in the cell cortex have not yet been clarified due to a lack of proper imaging techniques. Here, we utilized high-speed atomic force microscopy for live-cell imaging and analyzed cortical actin dynamics in living cells. We successfully measured the polymerization rate and the frequency of filament synthesis in living COS-7 cells, and examined the associated effects of various inhibitors and actin-binding proteins. Actin filaments are synthesized beneath the plasma membrane and eventually descend into the cytoplasm. The inhibitors, cytochalasin B inhibited the polymerization, while jasplakinolide, inhibited the turnover of actin filaments as well as descension of the newly synthesized filaments, suggesting that actin polymerization near the membrane drives turnover of the cortical actin meshwork. We also determined how actin turnover is maintained and regulated by the free G-actin pool and G-actin binding proteins such as profilin and thymosin β4, and found that only a small amount of free G-actin was present in the cortex. Finally, we analyzed several different cell types, and found that the mesh size and the orientation of actin filaments were highly divergent, indicating the involvement of various actin-binding proteins in the maintenance and regulation of cortical actin architecture in each cell type.
dc.format.mimetypeapplication/pdf
dc.language.isoeng
dc.publisherOxford University Press (OUP)
dc.rightsThis is a pre-copyedited, author-produced PDF of an article accepted for publication in 'Microscopy' following peer review. The version of record 'Microscopy, Volume 66, Issue 4, 1 August 2017, Pages 272–282' is available online at: https://academic.oup.com/jmicro/article/66/4/272/3836920
dc.rightsThe full-text file will be made open to the public on 20 May 2018 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
dc.rightsThis is not the published version. Please cite only the published version. この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
dc.subjectcortical actin
dc.subjecthigh-speed atomic force microscopy
dc.subjectactin-binding proteins
dc.subjectcell cortex
dc.subjectin vivo imaging
dc.subjectactin turnover
dc.titleIn vivo dynamics of the cortical actin network revealed by fast-scanning atomic force microscopy
dc.type.niitypeJournal Article
dc.identifier.jtitleMicroscopy
dc.identifier.volume66
dc.identifier.issue4
dc.identifier.spage272
dc.identifier.epage282
dc.relation.doi10.1093/jmicro/dfx015
dc.textversionauthor
dc.addressGraduate School of Biostudies, Kyoto University
dc.addressGraduate School of Biostudies, Kyoto University
dc.addressR&D Group, Olympus Corp.
dc.addressGraduate School of Biostudies, Kyoto University
dc.addressGraduate School of Biostudies, Kyoto University
dc.identifier.pmid28531263
Appears in Collections:Journal Articles

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