Rac1 switching at the right time and location is essential for Fcγ receptor-mediated phagosome formation

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Rac1 switching at the right time and location is essential for Fcγ receptor-mediated phagosome formation

Persistent ID (NDL): info:ndljp/pid/11498632

Material type: 博士論文

Author: 池田, 結香

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Publication date: 2020-03-24

Material Format: Digital

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Name of awarding university/degree: 香川大学,博士（医学）

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Note (General)：: ABSTRACTLamellipodia are sheet-like cell protrusions driven by actin polymerization mainly through Rac1, a GTPase molecular switch. In Fcγ receptor-me...

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Material Type: 博士論文
Title: Rac1 switching at the right time and location is essential for Fcγ receptor-mediated phagosome formation
Author/Editor: 池田, 結香
Author Heading: 池田, 結香
Publication Date: 2020-03-24
Publication Date (W3CDTF): 2020-03-24
Degree grantor/type: 香川大学
Date Granted: 2020-03-24
Date Granted (W3CDTF): 2020-03-24
Dissertation Number: 甲第729号
Degree Type: 博士（医学）
Conferring No. (Dissertation): 甲第729号
Text Language Code: eng
Alias of Author: Ikeda, Yuka
Subject Heading: Rac1
Phagocytosis
Lamellipodia
Macrophages
Live-cell imaging
Myosin
Optogenetics
Target Audience: 一般
Note (General): ABSTRACTLamellipodia are sheet-like cell protrusions driven by actin polymerization mainly through Rac1, a GTPase molecular switch. In Fcγ receptor-mediated phagocytosis of IgG-opsonized erythrocytes (IgG-Es), Rac1 activation is required for lamellipodial extension along the surface of IgG-Es. However, the significance of Rac1 deactivation in phagosome formation is poorly understood. Our live-cell imaging and electron microscopy revealed that RAW264 macrophages expressing a constitutively active Rac1 mutant showed defects in phagocytic cup formation, while lamellipodia were formed around IgG-Es. Because activated Rac1 reduced the phosphorylation levels of myosin light chains, failure of the cup formation is probably due to inhibition of actin/myosin II contractility. Reversible photo-manipulation of the Rac1 switch in macrophages fed with IgG-Es could phenocopy two lamellipodial motilities: outward-extension and cup-constriction by Rac1 ON and OFF, respectively. In conjunction with fluorescence resonance energy transfer imaging of Rac1 activity, we provide a novel mechanistic model of phagosome formation spatiotemporally controlled by Rac1 switching within a phagocytic cup.
DOI: info:doi/10.1242/jcs.201749
https://doi.org/info:doi/10.1242/jcs.201749
Persistent ID (NDL): info:ndljp/pid/11498632
https://dl.ndl.go.jp/pid/11498632
Collection: 障害者向け資料
Collection (Materials For Handicapped People:1): テキストデータ
Collection (particular): 国立国会図書館デジタルコレクション > デジタル化資料 > 博士論文
https://dl.ndl.go.jp/collections/A00014
Acquisition Basis: 博士論文（自動収集）
Date Accepted (W3CDTF): 2020-06-07T00:39:19+09:00
Date Created (W3CDTF): 2020-10-27
Format (IMT): PDF
Access Restrictions: 国立国会図書館内限定公開
Service for the Digitized Contents Transmission Service: 図書館・個人送信対象外
Availability of remote photoduplication service: 可
Periodical Title (URI): https://kagawa-u.repo.nii.ac.jp/records/416
Data Provider (Database): 国立国会図書館 : 国立国会図書館デジタルコレクション
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